|
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 ... |
183-292 |
1.44e-74 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 243.85 E-value: 1.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 183 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQV 262
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKI 75
|
90 100 110
....*....|....*....|....*....|
gi 2124423178 263 KLVNIRNDDIADGNPKLTLGLIWTIILHFQ 292
Cdd:cd21188 76 KLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
305-410 |
6.52e-72 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 236.46 E-value: 6.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 2124423178 385 PEDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
180-303 |
1.83e-71 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 235.69 E-value: 1.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2124423178 260 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 303
Cdd:cd21235 76 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
178-301 |
9.36e-70 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 231.03 E-value: 9.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 178 ATDERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYL 257
Cdd:cd21236 10 YKDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYL 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2124423178 258 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 301
Cdd:cd21236 85 KRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
306-410 |
7.47e-66 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.80 E-value: 7.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 2124423178 386 EDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
180-302 |
3.24e-61 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 206.42 E-value: 3.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2124423178 260 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 302
Cdd:cd21237 76 RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
306-410 |
2.56e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.43 E-value: 2.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 2124423178 386 EDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
304-410 |
1.35e-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: 178.31 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 304 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 383
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 2124423178 384 DPEDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
185-293 |
1.12e-48 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 169.87 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 185 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 264
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77
|
90 100
....*....|....*....|....*....
gi 2124423178 265 VNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21186 78 VNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
3.38e-46 |
|
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.
Pssm-ID: 427337 Cd Length: 92 Bit Score: 162.30 E-value: 3.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 7 MPLDQLRAIYEVLFREGVMVAKKDRRPrSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKDFNL-PKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 2124423178 87 HLPPEIVPASLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
306-406 |
7.55e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 161.81 E-value: 7.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 2124423178 386 EDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
180-289 |
9.73e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 161.77 E-value: 9.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLK 85
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21246 86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
184-517 |
2.18e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 176.67 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 184 RVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQ 261
Cdd:COG5069 8 KVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 262 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLF 340
Cdd:COG5069 84 VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 341 NAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD---- 407
Cdd:COG5069 161 SALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidi 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 408 AMPRVPDVQDGVKANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE--LPAKEAD-KN 484
Cdd:COG5069 241 ALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHS 318
|
330 340 350
....*....|....*....|....*....|...
gi 2124423178 485 RSKGIYQSLEgAVQAGQLKVPPGYHPLDVEKEW 517
Cdd:COG5069 319 LAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
181-293 |
2.85e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.54 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 181 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 258
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21241 78 SKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
181-293 |
4.63e-44 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 156.96 E-value: 4.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 181 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 258
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
306-406 |
5.20e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2124423178 386 EDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
180-289 |
7.50e-42 |
|
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: 150.91 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLr 258
Cdd:cd21193 11 EERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL- 84
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21193 85 KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
305-410 |
3.83e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 148.62 E-value: 3.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 2124423178 385 PEDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
293-408 |
5.91e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 148.28 E-value: 5.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 372
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
181-293 |
2.53e-39 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 143.43 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 181 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNK 77
|
90 100 110
....*....|....*....|....*....|...
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21242 78 SIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
302-406 |
1.52e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 141.30 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 302 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 381
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 2124423178 382 LLDPEDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
180-289 |
3.77e-38 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 141.32 E-value: 3.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
302-406 |
5.71e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.81 E-value: 5.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 302 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 381
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 2124423178 382 LLDPEDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
180-289 |
2.07e-37 |
|
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: 138.65 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21317 26 DEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLK 100
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21317 101 EQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1486-2117 |
2.42e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 155.48 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEE-EERLaeqqraeerERLAAVEAalEKQRQLAEAHAQAKaQAEQeAQELQRRMQEevarreeaavdaqqqkRS 1564
Cdd:COG1196 176 EAERKLEAtEENL---------ERLEDILG--ELERQLEPLERQAE-KAER-YRELKEELKE----------------LE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1565 IQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1644
Cdd:COG1196 227 AELLLLKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1645 RLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVE 1724
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1725 LQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1804
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1805 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEE 1881
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAA 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1882 ELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAk 1961
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL- 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1962 RQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2041
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2042 LAQLRKASESELE--RQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQaELEAM 2117
Cdd:COG1196 703 EEEERELAEAEEErlEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER-EIEAL 779
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
305-406 |
3.03e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 137.30 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 2124423178 385 PEDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
183-289 |
1.58e-36 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 135.21 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 183 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQ 261
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKG 77
|
90 100
....*....|....*....|....*...
gi 2124423178 262 VKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21214 78 VKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
185-291 |
2.36e-36 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 134.84 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 185 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 262
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGV 78
|
90 100
....*....|....*....|....*....
gi 2124423178 263 KLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21215 79 KLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
180-293 |
4.56e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 133.89 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQK 76
|
90 100 110
....*....|....*....|....*....|....
gi 2124423178 260 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21231 77 NNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
309-410 |
9.13e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 132.94 E-value: 9.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 309 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2124423178 388 VDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1588-2196 |
2.62e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.93 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1588 EAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1667
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1668 VKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1747
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1748 VAVAQLreeaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE 1827
Cdd:COG1196 341 ELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1907
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLASKARAEEESRSTSEKSK----QRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAervlA 1983
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLlaglRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE----Y 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1984 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT 2063
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2064 LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 2143
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2144 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQA 2196
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1828-2396 |
2.78e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.93 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1907
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLAEKLA 1987
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1988 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKgLVEDTLRQR 2067
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2068 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2147
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2148 ARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQEQSM 2222
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2223 LERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQA 2302
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2303 ALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2382
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570
....*....|....
gi 2124423178 2383 QMEELGKLKARIEA 2396
Cdd:COG1196 765 LERELERLEREIEA 778
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
290-406 |
3.55e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.10 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 290 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 369
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 370 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1461-2048 |
1.31e-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: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1461 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQ-------LAEAHAQAKAQ 1532
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1533 AEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER------------------SR 1594
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeaeaelaeaeealleaEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1595 LRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEA 1674
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1675 AREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLR 1754
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1755 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQ 1829
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1830 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRA 1909
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1910 EMEVLLASKARAEEESRSTSEKSKQRleaeasrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAI 1989
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1990 GEATRLKTEAEIALKEKEAENERlrrlAEDE-AFQRRRLEEQAAQHkADIEERLAQLRKA 2048
Cdd:COG1196 763 EELERELERLEREIEALGPVNLL----AIEEyEELEERYDFLSEQR-EDLEEARETLEEA 817
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1625-2199 |
4.04e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.08 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1625 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQRKRqaeaelavrVKAEAEAA------------REKQRALQALEEFR 1689
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAeryrelkeelkeLEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1690 LQAEEAERRLRQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAER 1769
Cdd:COG1196 239 AELEELEAELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1770 AREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAE 1849
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1850 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS 1929
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1930 EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA----AIGEATRLKTEAEIALKE 2005
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2006 KEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAA 2085
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2086 AGK----AELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERL 2161
Cdd:COG1196 623 LGRtlvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590
....*....|....*....|....*....|....*...
gi 2124423178 2162 KAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEK 2199
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-114 |
1.52e-33 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 127.45 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 5 MLMPLDQLRAIYEVLFREGVMVAKKDRrPRSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQ 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKDP-KGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90 100 110
....*....|....*....|....*....|
gi 2124423178 85 YLHLPPEIVPASLQRVRRPVAMVMPARRTP 114
Cdd:PTZ00034 80 YLHLPPDVFPATHKKKSVNFERKTEEEGSR 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1492-2198 |
2.02e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 143.74 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1492 EEEERLAEQQRAEERERlaaVEAALEKQRQLAEAHAQAKAQAEQEAQELqRRMQEevARREEAAVDAQQQKRSiqEELQH 1571
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGK---AEEARKAEEAKKKAEDARKAEEARKAEDA-RKAEE--ARKAEDAKRVEIARKA--EDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1572 LRQSSEAEiqaKARQVEAAERSrlrieEEIRVVRlQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1651
Cdd:PTZ00121 1166 AEEARKAE---DAKKAEAARKA-----EEVRKAE-ELRKAEDAR-----KAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1652 DETQRKRQAEAELAVRVKaEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA--LETAQRSAEVELQSKR 1729
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1730 ASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1809
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1810 EKQKEEAEREARRRGKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1889
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1890 AAAATQKRQELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEASRFRELAEEAARLRAlAEEAKRQRQ 1965
Cdd:PTZ00121 1469 AKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1966 LAEEDAARQRAEAERvlAEKLAAIGEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 2045
Cdd:PTZ00121 1539 AKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2046 RKASESELERQKGLVEDTLRQRrqveEEILALKVSFEKAAAGKAELELELGRIRS-----NAEDTLRSKEQA--ELEAMR 2118
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEEDKKKAEEAkkAEEDEK 1688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2119 QRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRL 2194
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
....
gi 2124423178 2195 QAEE 2198
Cdd:PTZ00121 1769 KAEE 1772
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
305-403 |
1.58e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.69 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 2124423178 385 PEDVDVPQPDEKSIITYVS 403
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
306-406 |
1.61e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 123.67 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2124423178 386 EDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
185-293 |
9.81e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 121.65 E-value: 9.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 185 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 264
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVEL 77
|
90 100
....*....|....*....|....*....
gi 2124423178 265 VNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21232 78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
184-294 |
1.26e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 121.79 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 184 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ 261
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDE 88
|
90 100 110
....*....|....*....|....*....|....
gi 2124423178 262 -VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21311 89 gIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
185-293 |
1.30e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 121.24 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 185 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 262
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGI 78
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 263 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21227 79 KLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1041-1118 |
2.44e-31 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 119.24 E-value: 2.44e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1041 LAWQSLSRDVQLIRSWSLVTFRTMKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSHHYQQLLQS 1118
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
293-408 |
2.83e-31 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 120.71 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 293 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 372
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 373 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 408
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
309-410 |
5.01e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 119.29 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 309 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2124423178 388 VDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
309-411 |
1.26e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.49 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 309 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 386
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 2124423178 387 DVDVPQPDEKSIITYVSSLYDAMPR 411
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
305-403 |
1.28e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.40 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 2124423178 385 PEDVDVPQPDEKSIITYVS 403
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
180-289 |
1.83e-30 |
|
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: 119.76 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1371-2090 |
3.24e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 133.34 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1371 QDAKRRQEQIQAmvlADSRAVREQLRQEKALLEEIERHGEKVEECQRfAKQYINAIKDYELQlvtyKAQLEPVASPAKKP 1450
Cdd:PTZ00121 1137 EDARKAEEARKA---EDAKRVEIARKAEDARKAEEARKAEDAKKAEA-ARKAEEVRKAEELR----KAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1451 KVQSGSESViQEYVDLRTryselttltsqyikfiSETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK 1530
Cdd:PTZ00121 1209 EEERKAEEA-RKAEDAKK----------------AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1531 AQAEQ--EAQELQR----------RMQEEVARREEAAVDAQQQKRSIQ-----EELQHLRQSSEAEIQAKARQVEAAERS 1593
Cdd:PTZ00121 1272 IKAEEarKADELKKaeekkkadeaKKAEEKKKADEAKKKAEEAKKADEakkkaEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1594 RLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE----------AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE 1663
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadeakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1664 LAVRVKAEAEAAREKQRALQALEEFRlQAEEAERRlrqaeAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1743
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKK-----AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1744 QEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlQAEEVAQQKSLAQAEAEKqkeeaerearrr 1823
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK---KAEELKKAEEKKKAEEAK------------ 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 gKAEEqavrQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1903
Cdd:PTZ00121 1571 -KAEE----DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1904 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRAlAEEAKRQRQLaeedaaRQRAEAERVLA 1983
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEAKKAEEL------KKKEAEEKKKA 1718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1984 EKLAAIGEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRrleeqAAQHKADIEERLAQLRKASESELErqKGLVEDT 2063
Cdd:PTZ00121 1719 EELKKAEEENKIK--AEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIE--EELDEED 1789
|
730 740
....*....|....*....|....*..
gi 2124423178 2064 LRQRRQVEEEILALKVSFEKAAAGKAE 2090
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
311-406 |
3.50e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.06 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 311 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 389
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 2124423178 390 VPQPDEKSIITYVSSLY 406
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
181-295 |
4.13e-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: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 181 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLR 258
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 295
Cdd:cd21191 78 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1930-2613 |
7.21e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.21 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1930 EKSKQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLaaigEATRLKTEAEIALKEKEAE 2009
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2010 NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKVSFEKAAAGKA 2089
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2090 ELELELgrirSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2169
Cdd:COG1196 348 EAEEEL----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2170 RLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLqqeqsmlERLRGEAEAARRAAEEAEEARERAER 2249
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE-------EAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2250 EAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfAEQTLRQKA 2329
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA--------AAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2330 QVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEELFSLRVQMEELGKLKARIEAENRALILRDKDNT 2409
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR---EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2410 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2489
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2490 ARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgeklh 2565
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL----- 800
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2124423178 2566 rtelaTQEKVTLVQTLeiqrqqsdhdaERLRQAIAELEREKEKLKQEA 2613
Cdd:COG1196 801 -----SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
291-408 |
4.71e-29 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 114.41 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 291 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 370
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2124423178 371 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
184-291 |
1.21e-28 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 112.57 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
309-408 |
2.24e-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: 111.99 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 309 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 387
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 2124423178 388 VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1632-2620 |
3.69e-28 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 126.09 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1632 AEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAE--AEAAREKQRALQALEEFRLQAE-EAERRLRQAEAERAR 1708
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1709 QVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVaqlreeaerraqqqaeaeraREEAERELERWQLKA 1785
Cdd:NF041483 161 TESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA--------------------RAEAEAILRRARKDA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1786 NEALR-LRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrlAAEQELIR 1864
Cdd:NF041483 221 ERLLNaASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAE--AKEAAAKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1865 LRAETEQGEQQRQLLEEELARLQHEAAA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSKQRLEAEA 1940
Cdd:NF041483 296 LASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1941 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVlAEKLAAIG----------------EATRLKTEAEIALK 2004
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ-AEQLKGAAkddtkeyraktvelqeEARRLRGEAEQLRA 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2005 EKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIE------------------ERLAQLRKASESELERQKGLVE 2061
Cdd:NF041483 455 EAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADelrstataeservrteaiERATTLRRQAEETLERTRAEAE 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2062 dtlRQRRQVEEEILALKVSFEKAA------------AGKAELELELGRIRSNAEDTLRSKEQAELEamrqrqlaaeeeqr 2129
Cdd:NF041483 535 ---RLRAEAEEQAEEVRAAAERAArelreeteraiaARQAEAAEELTRLHTEAEERLTAAEEALAD-------------- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2130 rreaeervqkslaAEEEAARQRKAALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQDAAQKRLQAEEKAhafavqq 2207
Cdd:NF041483 598 -------------ARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGENVA------- 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2208 keqelqqtlqqeqsmlERLRGEAEaarraaeeaeeareraereaaqsrrqvEEAERLKQSAEEQAQAQAQAQAAAEKlrK 2287
Cdd:NF041483 658 ----------------VRLRSEAA---------------------------AEAERLKSEAQESADRVRAEAAAAAE--R 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2288 EAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTL-RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEA 2366
Cdd:NF041483 693 VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQEReRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSA 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2367 ARQRS------------QVEEELFSLRVQMEELGKlKARIEAENRALILR------------DKDNTQRVLQEEAEKMKH 2422
Cdd:NF041483 773 AEQTAqqvrdsvaglqeQAEEEIAGLRSAAEHAAE-RTRTEAQEEADRVRsdayaereraseDANRLRREAQEETEAAKA 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2423 VAEEAarLSVAAQEAARLRELAEEDLAQQRALAEKMLKekmQAVQEATRLKAEA---------ELLQQQKEL---AQEQA 2490
Cdd:NF041483 852 LAERT--VSEAIAEAERLRSDASEYAQRVRTEASDTLA---SAEQDAARTRADAredanrirsDAAAQADRLigeATSEA 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2491 RRLQEDKEQMAQQLEQETQ---GFQRTLEAERQRQL--EMSAEAERLKLRVAE-MSRAQARAE---EDAQRFRKQAEEIG 2561
Cdd:NF041483 927 ERLTAEARAEAERLRDEARaeaERVRADAAAQAEQLiaEATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEA 1006
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2562 EKLhRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKS 2620
Cdd:NF041483 1007 ERL-RTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRT 1064
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1825-2612 |
1.53e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.48 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaETEQGEQQRQllEEELARLQHEAAAATQKRQELEAEL 1904
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARK--AEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1905 AKVRAEMEVLLASKARAEEESRSTSEKSKqrleaeASRFRElAEEAARlralAEEAKRQRQLAEEDAARQRAEAERvlAE 1984
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRK------AEELRK-AEDARK----AEAARKAEEERKAEEARKAEDAKK--AE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1985 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ-HKADIEERLAQLRKASESELERQKglvedt 2063
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEK------ 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2064 lrqrRQVEEeilalkvsfekaAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 2143
Cdd:PTZ00121 1302 ----KKADE------------AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2144 EEEAARQRKAALEEVERLKAKVEEARR---LRERAEQESARQLQLAQDAAQKRL------QAEEKAHAFAVQQKEQELQQ 2214
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKadeakkKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2215 TLQQEQSMLERLRGEAEAARRaaeeaeeareraereaaQSRRQVEEAERlkqsaeeqaqaQAQAQAAAEKLRKEAEQEAA 2294
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKA-----------------EEAKKADEAKK-----------KAEEAKKADEAKKKAEEAKK 1497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2295 RRAQAEQAALRQKQAADAEMEKHKKFAEQTlrQKAQVEQELTTLRLQLEETDHQKSILDEELQrlKAEVTEAARQRSQVE 2374
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAE 1573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2375 EELFSLRVQMEELGKL-KARIEAENRALILRDKDNTQRVLQEEAEKMKhvAEEAARlsvaAQEAARLRELAEEDLAQQRA 2453
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKK 1647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2454 LAEKMLKEKMQAVQEATRLKAEAEllqQQKELAQEqARRLQEDKEQMAQQLEQETQgfqrtlEAERQRQLEMSAEAERLK 2533
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAE---EDKKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK 1717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2534 lrVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAE-LEREKEKLKQE 2612
Cdd:PTZ00121 1718 --AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRME 1795
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
293-408 |
2.13e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 109.79 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 372
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1389-2178 |
5.08e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 122.09 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1389 RAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDY-ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLR 1467
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELrELELALLVLRLE--ELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1468 TRYSELTTLTSQYIKFISETlrrmeeEERLAEQQraEERERLAAVEAALEKQRQLaeaHAQAKAQAEQEAQELQRRMQEE 1547
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSEL------EEEIEELQ--KELYALANEISRLEQQKQI---LRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1548 VARREEAAVDAQQQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRA 1627
Cdd:TIGR02168 329 ESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1628 RAEEAEAQKRQAQEEAERLRRQVQDetQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAE-- 1705
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREla 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1706 RARQVQVALETAQRSAEVELQSKRASFAEKtaqleRTLQEEHVAVAQLREEAerraqqqaeaerareeaerelERWQLKA 1785
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQ-----SGLSGILGVLSELISVD---------------------EGYEAAI 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1786 NEALRLRLQA----------EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELA------------------ 1837
Cdd:TIGR02168 540 EAALGGRLQAvvvenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLgvakdlvkfdpklrkals 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1838 ------------EQELEKQRQL-----------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1882
Cdd:TIGR02168 620 yllggvlvvddlDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1883 LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEASRfRELAEEAARLRALAE 1958
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEI-EELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1959 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAeialKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 2038
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2039 EERLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDtLRSK------EQA 2112
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE-LREKlaqlelRLE 932
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2113 ELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRkaalEEVERLKAKVEEARRLRERAEQE 2178
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEE 994
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1495-2614 |
1.16e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 121.09 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1495 ERLAEQQRAEERERLAavEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1574
Cdd:NF041483 93 ERELRDARAQTQRILQ--EHAEHQARLQAELHTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1575 SSEAEiqakARQVEAAERSRL-RIEEEirvvrlqlettERQRGGAEGElqalRARAeEAEAQKRQAQEEAERLRRQVQDE 1653
Cdd:NF041483 171 ESRAE----AEQALAAARAEAeRLAEE-----------ARQRLGSEAE----SARA-EAEAILRRARKDAERLLNAASTQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1654 TQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQaeEAERRLRQAEAERARQVQVALETAqrsaevelqSKRASFA 1733
Cdd:NF041483 231 AQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA---------AKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1734 EKT-AQLERTLQEEhvaVAQL-REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1811
Cdd:NF041483 300 ESAnEQRTRTAKEE---IARLvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1812 QKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARLQHEa 1890
Cdd:NF041483 377 LTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRLRGE- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1891 aaATQKRQELEAELAKVRAEM----------------EVLLASKARAEE-ESRSTSEKSKQRLEA--EASRFRELAE--- 1948
Cdd:NF041483 449 --AEQLRAEAVAEGERIRGEArreavqqieeaartaeELLTKAKADADElRSTATAESERVRTEAieRATTLRRQAEetl 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1949 -----EAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLAEKLA-AIGEATRLKTEAE-------IALKEKEAENERLR 2014
Cdd:NF041483 527 ertraEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEALADARAEAERIR 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2015 RLAEDEAfqrRRLEEQAAqhkadieERLAQLRKASESELERQKGLVEDTLRQRRqVEEEILALKVSFEKAAagkaelelE 2094
Cdd:NF041483 607 REAAEET---ERLRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAAR-AEGENVAVRLRSEAAA--------E 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2095 LGRIRSNAEDTlRSKEQAELEAMRQRqlaaeeeqrrrEAEERVQKSLAAEEEAARQRKaalEEVERLKAKVEEARRLRER 2174
Cdd:NF041483 668 AERLKSEAQES-ADRVRAEAAAAAER-----------VGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERER 732
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2175 AEQESARQLQlaqdAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQS 2254
Cdd:NF041483 733 AREQSEELLA----SARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAER 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2255 RRQ--VEEAERLKQSAEEQAQAQAQAQAaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAEQTLRQkAQVE 2332
Cdd:NF041483 809 TRTeaQEEADRVRSDAYAERERASEDAN------------------------RLRREAQEETEAAKALAERTVSE-AIAE 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2333 QElttlRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQ------------MEELGKLKARIEAENRA 2400
Cdd:NF041483 864 AE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDaaaqadrligeaTSEAERLTAEARAEAER 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2401 LILRDKDNTQRVLQEEAEKMKHV------------AEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEkmqAVQE 2468
Cdd:NF041483 940 LRDEARAEAERVRADAAAQAEQLiaeatgeaerlrAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTE---AREE 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2469 ATRLKAEA-ELLQQQKELAQEQARRLQEDKEQMAQQL--EQETQGFQRTLEAERQRQLEMSA---EAERLKLR------- 2535
Cdd:NF041483 1017 ADRTLDEArKDANKRRSEAAEQADTLITEAAAEADQLtaKAQEEALRTTTEAEAQADTMVGAarkEAERIVAEatvegns 1096
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2536 VAEMSRAQAR-----AEEDAQRFRKQAEEIG-------EKLH---RTELATQEKVT------LVQTLEIQRQQSDHDAER 2594
Cdd:NF041483 1097 LVEKARTDADellvgARRDATAIRERAEELRdritgeiEELHeraRRESAEQMKSAgercdaLVKAAEEQLAEAEAKAKE 1176
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*.
gi 2124423178 2595 LR--------------------------QAIAELEREKEKLKQEAK 2614
Cdd:NF041483 1177 LVsdanseaskvriaavkkaegllkeaeQKKAELVREAEKIKAEAE 1222
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
293-408 |
1.30e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.50 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 372
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1485-2625 |
7.13e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 118.39 E-value: 7.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1485 SETLRRMEEEE--RLAEQQRAEERERLAAVEAalEKQRQLAEAHAQAKAQAEQ---EAQELQRRMQEEVARREEAAVDAQ 1559
Cdd:NF041483 154 AEQLRARTESQarRLLDESRAEAEQALAAARA--EAERLAEEARQRLGSEAESaraEAEAILRRARKDAERLLNAASTQA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1560 QQKRSIQEELqhlRQSSEAEIQAKARQveAAERSRlrieeeirvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQA 1639
Cdd:NF041483 232 QEATDHAEQL---RSSTAAESDQARRQ--AAELSR---------------AAEQRMQEAEEALREARAEAEKVVAEAKEA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1640 QeeAERLRRQVQDETQRKRQAEAELAVRV-KAEAEAAREKQRALQALEEFRLQAE----EAERRLRQAEAER-ARQVQVA 1713
Cdd:NF041483 292 A--AKQLASAESANEQRTRTAKEEIARLVgEATKEAEALKAEAEQALADARAEAEklvaEAAEKARTVAAEDtAAQLAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1714 LETAQR-----SAEVELQSKRAS------FAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL--ER 1780
Cdd:NF041483 370 ARTAEEvltkaSEDAKATTRAAAeeaeriRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLrgEA 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1781 WQLKAN---EALRLRLQAEEVAQQKslaqaeaekQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-EGTAQQRL 1856
Cdd:NF041483 450 EQLRAEavaEGERIRGEARREAVQQ---------IEEAARTAEELLTKAKADADELRSTATAESERVRTEAiERATTLRR 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1857 AAEQELIRLRAE--------TEQGEQQRQLLEEELARLQHEAAAATQKRQ-ELEAELAKVRAEMEVLLASKARAEEESRS 1927
Cdd:NF041483 521 QAEETLERTRAEaerlraeaEEQAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLTAAEEALADARA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1928 TSEKSKQRLEAEASRFRelAEEAARLRAL----AEEAKRQRQLAEEDAARQRAEAERVlaeklaaigeATRLKTEAeial 2003
Cdd:NF041483 601 EAERIRREAAEETERLR--TEAAERIRTLqaqaEQEAERLRTEAAADASAARAEGENV----------AVRLRSEA---- 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2004 kekEAENERLRRLAEDEAfQRRRLEEQAAQhkadieERLAQlrKASESELERQkglvEDTLRQRRQVEEEIlalkvsfek 2083
Cdd:NF041483 665 ---AAEAERLKSEAQESA-DRVRAEAAAAA------ERVGT--EAAEALAAAQ----EEAARRRREAEETL--------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2084 aAAGKAELELELGRIRSNAEDTLRSK----EQAELEAMR----QRQLAAEEEQRRREAEERVQKSLA-----AEEEAARQ 2150
Cdd:NF041483 720 -GSARAEADQERERAREQSEELLASArkrvEEAQAEAQRlveeADRRATELVSAAEQTAQQVRDSVAglqeqAEEEIAGL 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2151 RKAALEEVERLKAKV-EEARRLRERAEQESARQlqlAQDAAQKRLQAEEKAHAfavqqkeqelqqtlqqEQSMLERLRGE 2229
Cdd:NF041483 799 RSAAEHAAERTRTEAqEEADRVRSDAYAERERA---SEDANRLRREAQEETEA----------------AKALAERTVSE 859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2230 AeaarraaeeaeeareraereaaqsrrqVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQA 2309
Cdd:NF041483 860 A---------------------------IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAA 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2310 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT-EAARQRSQVEEELFSLRVQMEELG 2388
Cdd:NF041483 913 AQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIR 992
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2389 KLKARIEAENRAlilrDKDNTQRVLQEEAEKMKHVAEEAA--RLSVAAQEAARLRELAEEDL------AQQRALAEKMLK 2460
Cdd:NF041483 993 TEAERVKAEAAA----EAERLRTEAREEADRTLDEARKDAnkRRSEAAEQADTLITEAAAEAdqltakAQEEALRTTTEA 1068
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2461 EKMQ------AVQEATRLKAEA-----ELLQQQKELAQE---QARR----LQEDKEQMAQQLEQETQGFQRtlEAERQRQ 2522
Cdd:NF041483 1069 EAQAdtmvgaARKEAERIVAEAtvegnSLVEKARTDADEllvGARRdataIRERAEELRDRITGEIEELHE--RARRESA 1146
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2523 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTelATQEKVTLVQTLEIQRQQSDHDAERLR-QAIAE 2601
Cdd:NF041483 1147 EQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIA--AVKKAEGLLKEAEQKKAELVREAEKIKaEAEAE 1224
|
1210 1220
....*....|....*....|....
gi 2124423178 2602 LEREKEKLKQEAKLLQLKSEEMQT 2625
Cdd:NF041483 1225 AKRTVEEGKRELDVLVRRREDINA 1248
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1552-2376 |
8.32e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 118.71 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1552 EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE 1631
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1632 aEAQKRQAQEEAERLR-----RQVQD--ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAE- 1703
Cdd:PTZ00121 1114 -ARKAEEAKKKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEe 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1704 ---AERARQVQVAletaqRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER 1780
Cdd:PTZ00121 1193 lrkAEDARKAEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1781 WQ--LKANEALRlrlqAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGtaqqrlaa 1858
Cdd:PTZ00121 1268 RQaaIKAEEARK----ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADA-------- 1333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1859 eqelIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEmevllASKARAEEESRStsEKSKQRLEA 1938
Cdd:PTZ00121 1334 ----AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-----AAKKKAEEKKKA--DEAKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1939 EASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERvlaeklaaigEATRLKTEAEIALKEKEAENERLRRLAE 2018
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK----------KADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2019 DEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEeilaLKVSFEKAAAGKAElelelgri 2098
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAK-------- 1540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2099 rsNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEeaarqrkaaLEEVErlKAKVEEARRLRERAEQE 2178
Cdd:PTZ00121 1541 --KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE---------AKKAE--EARIEEVMKLYEEEKKM 1607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2179 SARQLQLAQDAaqkRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQv 2258
Cdd:PTZ00121 1608 KAEEAKKAEEA---KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA- 1683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2259 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTlrqKAQVEQELTTL 2338
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA---KKDEEEKKKIA 1760
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423178 2339 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2376
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1248-2048 |
1.69e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.08 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1248 AEEVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1327
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1328 VAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIER 1407
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1408 hgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISET 1487
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1488 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE-EVARREEAAVDAQQQKR--- 1563
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAALGGRlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1564 -------SIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAE 1630
Cdd:TIGR02168 550 vvvenlnAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1631 EAEAQKRQAQEEAERLRRQVQDETQRKRQAeaeLAVRVKAEAEAAREKQRalQALEEFRLQAEEAERRLRQAEAE--RAR 1708
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLDGDLVRPGG---VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAlaELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1709 QVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvaVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1788
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1789 LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAE 1868
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1869 TEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEASRFRE 1945
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEVRIDN 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1946 LAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIGEATRLkteaeiALKEKEAENERLRRLaedeafqr 2024
Cdd:TIGR02168 941 LQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL-------- 1005
|
810 820
....*....|....*....|....
gi 2124423178 2025 rrleeqaAQHKADIEERLAQLRKA 2048
Cdd:TIGR02168 1006 -------TAQKEDLTEAKETLEEA 1022
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
184-291 |
1.86e-25 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 103.72 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERE 77
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21228 78 SIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
311-406 |
1.99e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.39 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 311 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 389
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 2124423178 390 VPQPDEKSIITYVSSLY 406
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1869-2751 |
2.06e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1869 TEQGEQQRQLLEEELARLQHEAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFREL-- 1946
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1947 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAIGEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 2024
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2025 RRLEEQaaqHKADIEERLAQLRKASESelerqkglvedtlrqrRQVEEeilalkvsfekaaAGKAELELELGRIRsNAED 2104
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2105 TLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2184
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2185 LAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERlrgeaeaarraaeeaeeareraereaaqsRRQVEEAERL 2264
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2265 KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2344
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2345 TDHQksildEELQRLKAEVTEAARQRSQVEEelfslRVQMEELGKlkaRIEAENRALILRDKDNTQRVLQE---EAEKMK 2421
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEAK 1496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2422 HVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDK 2497
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2498 EQMAQQLEQETQgfqrtleAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtl 2577
Cdd:PTZ00121 1577 NMALRKAEEAKK-------AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK-- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2578 vqtleiqrqqsdHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLlqetqalqqsflsEKDTLLQRErfiE 2657
Cdd:PTZ00121 1647 ------------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-------------KAAEALKKE---A 1698
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2658 QEKAKLEQL---FQDEVAKAQKLREEQQRQQKqmeeekqqlvasmeEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLL 2734
Cdd:PTZ00121 1699 EEAKKAEELkkkEAEEKKKAEELKKAEEENKI--------------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
890 900
....*....|....*....|
gi 2124423178 2735 AEENQRLRERLQR---LEEE 2751
Cdd:PTZ00121 1765 EEEKKAEEIRKEKeavIEEE 1784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1824-2520 |
3.01e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 116.78 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQ----ELIRLRAETEQGEQQRQLleeELARLQHEAAAATQKRQE 1899
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEEarkaEDARKAEEARKAEDAKRV---EIARKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1900 LEAELAK-VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRElAEEAARLRAL--AEEAKRQRQLAEEDAARQRA 1976
Cdd:PTZ00121 1173 EDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARK-AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1977 EAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAED--EAFQRRRLEEqaAQHKADIEERLAQLRKASESELE 2054
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2055 RQKGLvedtlrqRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAE-----LEAMRQRQLAAEEEQR 2129
Cdd:PTZ00121 1330 KADAA-------KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2130 RREAEERVQKSLAAEEEAARQRKAALE--EVERLKAKVEEARRLRE-RAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQ 2206
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2207 QKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQS--RRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2284
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2285 LRKEAEQEAARRAQAEQAALRQ--KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQRLKAE 2362
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKK 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2363 VTEAARQRSQVEEELFSLRVQMEELGKlKARiEAENRALILR----DKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAA 2438
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAK-KAE-EDKKKAEEAKkaeeDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2439 RLRELAEEDLAQQRALAEKMLKEKMQAvQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlEQETQGFQRTLEAE 2518
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVD 1797
|
..
gi 2124423178 2519 RQ 2520
Cdd:PTZ00121 1798 KK 1799
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
293-408 |
3.67e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 103.61 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 372
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
180-293 |
4.71e-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: 103.30 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423178 259 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
305-411 |
6.72e-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: 101.98 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 305 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 381
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 382 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 411
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
184-294 |
1.29e-24 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 102.03 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDRE 89
|
90 100 110
....*....|....*....|....*....|....
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21310 90 HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
309-409 |
2.96e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 99.85 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 309 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 388
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 2124423178 389 DVPQPDEKSIITYVSSLYDAM 409
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
188-290 |
3.30e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 99.70 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 188 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKL 264
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKV 76
|
90 100
....*....|....*....|....*.
gi 2124423178 265 VNIRNDDIADGnPKLTLGLIWTIILH 290
Cdd:smart00033 77 VLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
307-406 |
4.22e-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: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 307 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 386
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 2124423178 387 D-VDVPQPDEKSIITYVSSLY 406
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
940-1006 |
6.22e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.72 E-value: 6.22e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 940 QLKPRNpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVVSSSGSEAAVPSVCFLVP 1006
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
185-293 |
1.08e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 98.51 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 185 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-V 262
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgV 78
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 263 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:pfam00307 79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
306-410 |
2.82e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.17 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 2124423178 386 EDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1828-2666 |
2.95e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.76 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1907
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLASKARAEEESRSTSEkskqrleaeasRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1987
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1988 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrRLEEQAAQHKADIEERLAQLrKASESELERQKGLVEDtlRQR 2067
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEE--LLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2068 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2147
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE-QALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2148 ARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQ-LAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLErL 2226
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE-I 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2227 RGEAEAARRAAEEAEEARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2299
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2300 EQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELFS 2379
Cdd:TIGR02168 667 KTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2380 LRVQMEELGKLKARIEAEnralilrdkdntqrvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKmL 2459
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-L 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2460 KEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLEQETQgfqrtleaerqrqlEMSAEAERLKLRVAE 2538
Cdd:TIGR02168 802 REALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------------ELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2539 MSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQl 2618
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ- 942
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 2124423178 2619 kseemQTVQQEQLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQL 2666
Cdd:TIGR02168 943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
306-406 |
2.99e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 97.11 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 2124423178 386 EDVDVPQ-PDEKSIITYVSSLY 406
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1384-2201 |
4.12e-23 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 109.53 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1384 VLADSRAVREQLrqekalleeierhgekveecqrfakqyinaikdyelqlvtykaqlepVASPAKKPKVQSGSESVIQEY 1463
Cdd:NF041483 335 ALADARAEAEKL-----------------------------------------------VAEAAEKARTVAAEDTAAQLA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1464 VDLRTryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAAvEAALEKQRQLAEAHAQakaqaeqeAQELQRR 1543
Cdd:NF041483 368 KAART---------------AEEVLTKASEDAKATTRAAAEEAERIRR-EAEAEADRLRGEAADQ--------AEQLKGA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1544 MQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE---IQAKAR-----QVEAAERSRLRIEEEIRVVRLQLETT---- 1611
Cdd:NF041483 424 AKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEgerIRGEARreavqQIEEAARTAEELLTKAKADADELRSTatae 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1612 -ERQRGGAEGELQALRARAEEAEAQKRqaqEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRL 1690
Cdd:NF041483 504 sERVRTEAIERATTLRRQAEETLERTR---AEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1691 QAeEAERRLRQAEaERARQVQVALETAQRSAEVELQSKRASFAEKTaqleRTLQEEHVAVAQLREEAERRAQQQAEAERA 1770
Cdd:NF041483 581 HT-EAEERLTAAE-EALADARAEAERIRREAAEETERLRTEAAERI----RTLQAQAEQEAERLRTEAAADASAARAEGE 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1771 REEAERELErwqlKANEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1850
Cdd:NF041483 655 NVAVRLRSE----AAAEAERLKSEAQESADR--VRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQ 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1851 TAQQRLAAEQELI---RLRAETEQGEQQRqLLEEELARLQHEAAAATQKRQELEAELAKV--RAEMEV--LLASKARAEE 1923
Cdd:NF041483 729 ERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAE 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1924 ESRSTSEKSKQRLEAEASRFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLAEklaAIGEATRLKTEAEI 2001
Cdd:NF041483 808 RTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASD 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2002 ALKEKEAENERLRRLAEDEAFQRRrlEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSF 2081
Cdd:NF041483 885 TLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2082 EKAAAGKAElelelgRIRSNAEDTLRSKEQAeleAMRQRQLAAEEEQRrreaeervqkslaAEEEAARQRKAALEEVERL 2161
Cdd:NF041483 963 IAEATGEAE------RLRAEAAETVGSAQQH---AERIRTEAERVKAE-------------AAAEAERLRTEAREEADRT 1020
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 2124423178 2162 --KAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAH 2201
Cdd:NF041483 1021 ldEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1163-1727 |
6.80e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1163 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1242
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1243 RSTHGAEEVLKAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVE 1322
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1323 RWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1402
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1403 EEIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyik 1482
Cdd:COG1196 477 AALAE-----------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1483 fisetlrrMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEA----HAQAKAQAEQEAQELQRRMQEEVARREEAAVDA 1558
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1638
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1639 AQEEAERLRRQvqdETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA-LETA 1717
Cdd:COG1196 692 ELELEEALLAE---EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEeLERE 768
|
570
....*....|
gi 2124423178 1718 QRSAEVELQS 1727
Cdd:COG1196 769 LERLEREIEA 778
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-112 |
1.03e-22 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 95.76 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 5 MLMPLDQLRAIYEVLFREGVMVAKKDRRpRSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQ 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|....*...
gi 2124423178 85 YLHLPPEIVPASLQRVRRPVAmvMPARR 112
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ--RPQRR 104
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
306-404 |
3.15e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 94.23 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 2124423178 385 PEDVDVPQPDEKSIITYVSS 404
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1988-2771 |
5.15e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 105.99 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1988 AIGEATRLKTEAEIALKEKeAENERLRRLAEDEAFQRRRLEEQaaqHKADIEERLAQLRKASESELERQKGLVEDTLR-- 2065
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK-AEEARKAEEAKKKAEDARKAEEA---RKAEDARKAEEARKAEDAKRVEIARKAEDARKae 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2066 QRRQVEEEilalkvsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQrqlaaeeeqrrreaeerVQKSLAAEE 2145
Cdd:PTZ00121 1168 EARKAEDA--------KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK-----------------AEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2146 EaarQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAhafavQQKEQELQQTLQQEQSMLER 2225
Cdd:PTZ00121 1223 A---KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-----EEARKADELKKAEEKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2226 LRgeaeaarraaEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALR 2305
Cdd:PTZ00121 1295 AK----------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2306 QKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEEtDHQKSildEELQRLKAEVTEAARQRSQVEEelfslrvqME 2385
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEE-DKKKA---DELKKAAAAKKKADEAKKKAEE--------KK 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2386 ELGKLKARIEAENRALILRDKdntqrvlQEEAEKmkhvAEEAARLSVAAQEAARLRELAEEdlaqqRALAEKMLKEKMQA 2465
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKK-------AEEAKK----AEEAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2466 VQEATRLKAEAELLQQQKELAQ-EQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAErlKLRVAEMSRaqa 2544
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAK--- 1570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2545 RAEEDAQRFRKQAEEigeklhrteLATQEKVTLVQTLEIQRQQSDHDAERLRQAiaelerEKEKLKQEakllQLKSEEmq 2624
Cdd:PTZ00121 1571 KAEEDKNMALRKAEE---------AKKAEEARIEEVMKLYEEEKKMKAEEAKKA------EEAKIKAE----ELKKAE-- 1629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2625 tvqqeqllqetqalqqsflSEKDTLLQRERFIEQEKAKLEQLFQDE----------VAKAQKLREEQQRQQKQMEEEK-- 2692
Cdd:PTZ00121 1630 -------------------EEKKKVEQLKKKEAEEKKKAEELKKAEeenkikaaeeAKKAEEDKKKAEEAKKAEEDEKka 1690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2693 -QQLVASMEEARQ----RQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQA 2767
Cdd:PTZ00121 1691 aEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
....
gi 2124423178 2768 TAVK 2771
Cdd:PTZ00121 1771 EEIR 1774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1688-2611 |
5.96e-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: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1688 FRLQAEEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVAVAQLREEAERRAQQQA 1765
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1766 eaerareeaerelerwQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAE-----QE 1840
Cdd:TIGR02168 247 ----------------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1841 LEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKAR 1920
Cdd:TIGR02168 300 LEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1921 AEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAE 2000
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2001 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELE-----RQKGLVEDTLRQRRQVEEEil 2075
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllknqSGLSGILGVLSELISVDEG-- 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2076 alkvsFEKAaagkaeLELELGrirSNAEDTLRSKEQAELEAmrqrqlaaeeeqrrreaeervqksLAAEEEAARQRKAAL 2155
Cdd:TIGR02168 535 -----YEAA------IEAALG---GRLQAVVVENLNAAKKA------------------------IAFLKQNELGRVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2156 EEV---ERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQ--------AEEKAHAFAvQQKEQELQQTLQQEQSMLE 2224
Cdd:TIGR02168 577 PLDsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLDNALE-LAKKLRPGYRIVTLDGDLV 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2225 RLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAER-LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAarraqaeqaa 2303
Cdd:TIGR02168 656 RPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAeLEKALAELRKELEELEEELEQLRKELEELS---------- 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 lRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRvq 2383
Cdd:TIGR02168 726 -RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-- 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2384 mEELGKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKE 2461
Cdd:TIGR02168 803 -EALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2462 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRtLEAERQRQLEMSAEAERLKLRVAEmsR 2541
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAE--A 958
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2542 AQARAEEDAQRFRKQAEEIGEKLHR----TELATQEKVTLVQTLE-IQRQQSDHDA--ERLRQAIAELERE-KEKLKQ 2611
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYDfLTAQKEDLTEakETLEEAIEEIDREaRERFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1272-2072 |
2.48e-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: 103.60 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1272 LEATKAALKKLRAQAEAQQpMFDALRDELRGAQE--VGERLQQRHGERDvEVERWRERVAQLLERWQAVLAQTDLrqrEL 1349
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAE-RYKELKAELRELELalLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEE---KL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1350 EQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDY 1429
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1430 ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTtltsQYIKFISETLRRMEEE-ERLAEQQRAEERER 1508
Cdd:TIGR02168 350 KEELESLEAELE--ELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNNEIERLEARlERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1509 LAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR------QSSEAEIQA 1582
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1583 KARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAE----GELQALRARAEEAEAQKRQAQEEAERLRR---------- 1648
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikg 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1649 QVQDETQRKRQAEAELAVRVKAEAEAAREK-QRALQALEEFRLQAEEAERRLRQAEAERARQVQVALE------------ 1715
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitg 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1716 --TAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRL 1793
Cdd:TIGR02168 664 gsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1794 QAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1873
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1874 QQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEASRFRELAEEAARL 1953
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELESELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1954 RALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAE----NERLRRLAEDEAFQRRRLEE 2029
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALEN 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2030 QAAQHKADIEERLAQLRK----------ASESELERQKGLVEDTLRQRRQVEE 2072
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENkikelgpvnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
310-407 |
2.70e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.94 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 310 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 388
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2124423178 389 DVPQPDEKSIITYVSSLYD 407
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
306-406 |
4.25e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 88.17 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 2124423178 386 EDVDV--PQPDEKSIITYVSSLY 406
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
184-294 |
4.41e-20 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 89.37 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRE 90
|
90 100 110
....*....|....*....|....*....|....
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21309 91 SIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
184-294 |
4.75e-20 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 88.99 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRE 93
|
90 100 110
....*....|....*....|....*....|....
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21308 94 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1585-2401 |
5.59e-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: 98.98 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1585 RQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1653
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1654 TQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAR--QVQVALETAQRSAEVELQSKRAS 1731
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1732 FAEKTAQLERtLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1811
Cdd:TIGR02168 339 LAELEEKLEE-LKEELESLEAELE-----------------------ELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1812 QKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAA 1891
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1892 AATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEASRFRELAEEAARLRALAEEAKRQR--QLA 1967
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRlqAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1968 EEDAARQRAEAErvlAEKLAAIGEATRLkteAEIALKEKEAENERLRRLAEDEAFQR--RRLEEQAAQHKADIEERLAQL 2045
Cdd:TIGR02168 552 VENLNAAKKAIA---FLKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLGGV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2046 RKASEselerqkglVEDTLRQRRQVEEEILALKVSFEKAAAG----KAELELELGRI-RSNAEDTLRSK--EQAELEAMR 2118
Cdd:TIGR02168 626 LVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTNSSILeRRREIEELEEKieELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2119 QRQLAAEEEQRRREAEERVQKsLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2198
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQL-RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2199 KAHAfaVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQA 2278
Cdd:TIGR02168 776 ELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2279 QAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQR 2358
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2124423178 2359 LKAEVteaARQRSQVEEElfsLRVQMEELGKLKARIEAENRAL 2401
Cdd:TIGR02168 934 LEVRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2223-2837 |
1.66e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2223 LERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQA 2302
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-------------AELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2303 ALRQKQAADAEMEKHKKFAEQtlrQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2382
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2383 QMEELgklkARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEK 2462
Cdd:COG1196 366 ALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2463 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA 2542
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2543 QARAEEDAQRFRKQAEEIGEklhrTELATQEKVTLVQTLEIQRQQSDHDAERL--RQAIAELEREKEKLKQEAKLLQLKS 2620
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALE----AALAAALQNIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2621 EEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASME 2700
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAAR-LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2701 EARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDAP 2780
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2781 DGPATEAEPEHAFDGLRQKVpaQRLQEVGILSTEELQRLVQGRTTVAElaQREDVRR 2837
Cdd:COG1196 757 PEPPDLEELERELERLEREI--EALGPVNLLAIEEYEELEERYDFLSE--QREDLEE 809
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
306-405 |
2.28e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 85.99 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 2124423178 386 ED-VDVPQPDEKSIITYVSSL 405
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
302-407 |
2.64e-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: 86.15 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 302 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 381
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 2124423178 382 LLDPEDV-DVPQPDEKSIITYVSSLYD 407
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
309-405 |
3.85e-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: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 309 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 384
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2124423178 385 PEDVDVPQPDEKSIITYVSSL 405
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1479-2117 |
5.75e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.49 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1479 QYIKFISETLRRMEEEERLAEQQR----------AEERERLAAVEAALEKQRQlaeahaqAKAQAEQEAQELQRRMQEEV 1548
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1549 ARREEaavdaqqqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQAL 1625
Cdd:PRK02224 286 ERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1626 RARAEEaeaqkrqAQEEAERLrrqvqdetqrkrqaEAELavrvkAEAEAAREKQRAlqALEEFRLQAEEAERRLRQAEae 1705
Cdd:PRK02224 355 EERAEE-------LREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAP-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1706 rarqvqVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVAVAQlreeaerraqqqaeaerareeaerelerwqlka 1785
Cdd:PRK02224 405 ------VDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEE--------------------------------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1786 NEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAEqELEKQRqLAEGTAQQRLAAEQELIRL 1865
Cdd:PRK02224 445 AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA-ELEDLE-EEVEEVEERLERAEDLVEA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1866 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLEAEASRFRE 1945
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1946 LAEEAARLRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAIGEatrLKTEAEIALKEKeaeNERLRRLAEDeaFQRR 2025
Cdd:PRK02224 584 LKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDERRERLAEK---RERKRELEAE--FDEA 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2026 RLEE------QAAQHKADIEERLAQLRkASESELERQKGLVE------DTLRQRR-QVEEEILALKVSFEKAaagkAELE 2092
Cdd:PRK02224 647 RIEEaredkeRAEEYLEQVEEKLDELR-EERDDLQAEIGAVEneleelEELRERReALENRVEALEALYDEA----EELE 721
|
650 660
....*....|....*....|....*
gi 2124423178 2093 LELGRIRSNaedtLRSKEQAELEAM 2117
Cdd:PRK02224 722 SMYGDLRAE----LRQRNVETLERM 742
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1618-2514 |
9.22e-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: 95.04 E-value: 9.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1618 AEGELQALRARAEEAEAQKRQAQEE----AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAE 1693
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAEliidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1694 EAERRLRQAEAERARQVQVAletaqrsAEVELQSKRASFAEKTAQLErtLQEEHVAVAQLREEAERRAQQQAEAERAREE 1773
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEK-------EEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1774 AERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQ 1853
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKEL---------KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1854 QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSK 1933
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1934 QRLEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEiaLKEKEAENERL 2013
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKL-EERSQKESKARSGLKVLLALIKDGVGGRIISAHG--RLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2014 RRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELEL 2093
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2094 ELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2173
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2174 RAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQ 2253
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2254 SRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2333
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2334 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVL 2413
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2414 QEEAEKMKHVAEEAarlsvaaqeaarLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2493
Cdd:pfam02463 941 LLEEADEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
890 900
....*....|....*....|.
gi 2124423178 2494 QEDKEQMAQQLEQETQGFQRT 2514
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSI 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2145-2676 |
9.27e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 9.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2145 EEAARQRKAALEEVERLKAKVEEARRLRERAEQEsARQLQLAQDAAQKRLQAEEKAHAfAVQQKEQELQQTLQQEQSMLE 2224
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELE-EAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2225 RLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2304
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2305 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2384
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2385 EELGKLKARIEAENRALILRDKDNTQR--VLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEE--DLAQQRALAEKMLK 2460
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2461 EKMQA--VQEATRLKAEAELLQQQKE--------LAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAE 2530
Cdd:COG1196 546 AALQNivVEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2531 RLKLRVAEMSRAQARAEEDAQRFRKQAEEI----GEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREK 2606
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGgsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2607 EKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQLfQDEVAKAQK 2676
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2015-2769 |
1.41e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 94.35 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2015 RLAEDEAFQRRRLEEQAA---QHKADIEERLAQLRKASESeLERQKGLVEDTLRQ----RRQVEeeiLALKVSFEKAAAG 2087
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKETERKLERTREN-LDRLEDILNELERQlkslERQAE---KAERYKELKAELR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2088 KAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK---AALEEVERLKAK 2164
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2165 VEEARRLRERAEQESAR-QLQLAQDAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEA 2243
Cdd:TIGR02168 304 KQILRERLANLERQLEElEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2244 RERAEREAAQSRRQVEEA--------ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEME 2315
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLnneierleARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2316 KHKKFAEQTLRQKaqvEQELTTLRLQLEETDHQKSILDEELQRLK------AEVTEAARQRSQVEEELFSLrVQMEElgK 2389
Cdd:TIGR02168 461 EALEELREELEEA---EQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSEL-ISVDE--G 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2390 LKARIEA---ENRALILRDKDNTQRV---LQEEAEKMKHV----------------AEEAARLSVAAQEAARLRELAE-- 2445
Cdd:TIGR02168 535 YEAAIEAalgGRLQAVVVENLNAAKKaiaFLKQNELGRVTflpldsikgteiqgndREILKNIEGFLGVAKDLVKFDPkl 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2446 --------------EDLAQQRALAEKMLKEKMQAVQEATRL--------------------KAEAELLQQQKELAQEQAR 2491
Cdd:TIGR02168 615 rkalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2492 RLQ---EDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTE 2568
Cdd:TIGR02168 695 ELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2569 LATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDT 2648
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2649 LLQRERFIEQEKAKLEQLfQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQ 2728
Cdd:TIGR02168 854 IESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 2124423178 2729 QQEKLLAEENQRLRERLQRLEEEhraALAHSEEIAASQATA 2769
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEA 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1484-2196 |
1.99e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.98 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1484 ISETLRRMEEEERLAEQQRAEERERLAAVEAALEKqrqLAEAHAQAKAQAEQEAQELQRRMqEEVARREEAAVDAQQQKR 1563
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1564 SIQEELQHLRQSSEAEIQAKARQVEAaersrlrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1637
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1638 --------QAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQAEAER-- 1706
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1707 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAerelERWQLKAN 1786
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG----ERYATAIE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1787 EALRLRLQA-----EEVAQQK---------------SLAQAEAEKQKEEAEREARRRGKA---------EEQAVR---QR 1834
Cdd:TIGR02169 543 VAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkYEPAFKyvfGD 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1835 ELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1888
Cdd:TIGR02169 623 TLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1889 EAAAATQKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQ 1965
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1966 LAEEDAARQRAEAERVLAEKLAAIGEATRLKT-EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 2044
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2045 LRKAsESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKE--QAELEAMRQRQL 2122
Cdd:TIGR02169 863 KEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELSEIEDPKG 941
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2123 AAEEEQRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQA 2196
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1484-2167 |
2.37e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 93.70 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1484 ISETLRRMEEEERL---AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQ 1560
Cdd:pfam01576 273 ISELQEDLESERAArnkAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1561 QKRSIQEELQ-HLRQSSEAEIQ-AKARQVEAAERSRLriEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1638
Cdd:pfam01576 353 KHTQALEELTeQLEQAKRNKANlEKAKQALESENAEL--QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1639 AQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERA--RQVQVALET 1716
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslQEQLEEEEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1717 AQRSAEVELQSKRASFAEktaqLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQlKANEALRLRLQAE 1796
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE-KTKNRLQQELDDL 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1797 EVAQQkslaqaeaekqkeeaerearrrgkaeeqavRQRELAEQELEKQRQLAEGTAQQRLAAEQEL-IRLRAETEQGEQQ 1875
Cdd:pfam01576 586 LVDLD------------------------------HQRQLVSNLEKKQKKFDQMLAEEKAISARYAeERDRAEAEAREKE 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1876 RQLLEeelarLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAeEESRSTSEKSKQRLEAEASRFRELAEEA----- 1950
Cdd:pfam01576 636 TRALS-----LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDV-GKNVHELERSKRALEQQVEEMKTQLEELedelq 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1951 ----ARLR------ALAEEAKRQRQLAEEDA-------ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERL 2013
Cdd:pfam01576 710 atedAKLRlevnmqALKAQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAA 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2014 RRLAEDEAFQRRRLEEQAAQHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEILALKV 2079
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERDELAD 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2080 SFEKAAAGKAELELELGRIR---SNAEDTLrSKEQAELEAMRQRQlaaeeeQRRREAEERVQKSLAAEEEAARQRKAALE 2156
Cdd:pfam01576 869 EIASGASGKSALQDEKRRLEariAQLEEEL-EEEQSNTELLNDRL------RKSTLQVEQLTTELAAERSTSQKSESARQ 941
|
730
....*....|....*
gi 2124423178 2157 EVER----LKAKVEE 2167
Cdd:pfam01576 942 QLERqnkeLKAKLQE 956
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
186-291 |
3.45e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 82.63 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 186 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVK 263
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVD 77
|
90 100
....*....|....*....|....*...
gi 2124423178 264 LVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21212 78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1478-2208 |
4.17e-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: 93.11 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1478 SQYIKFISETLRRMEEEERLAE-QQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVA-----RR 1551
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKlIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldylkLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1552 EEAAVDAQQQKRSIQEELQHLRQSSEAE---IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRAR 1628
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1629 AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAR 1708
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1709 QVQVALETAQrsaEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1788
Cdd:pfam02463 396 ELELKSEEEK---EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1789 LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRL 1865
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1866 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeasrfRE 1945
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1946 LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 2025
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2026 RLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAED- 2104
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKl 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2105 ------TLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2178
Cdd:pfam02463 787 kveeekEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
730 740 750
....*....|....*....|....*....|...
gi 2124423178 2179 SARQ---LQLAQDAAQKRLQAEEKAHAFAVQQK 2208
Cdd:pfam02463 867 ELLQellLKEEELEEQKLKDELESKEEKEKEEK 899
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1486-2055 |
5.33e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 92.67 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQR------AEERERLAAVEAALEKQRQLAEAHAQAKAQAEQE-AQELQRRMQEEVARREEAAVDA 1558
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERqrggaegELQALRA 1627
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAE-------EFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1628 RA----EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-------------VRVKAE-AEAAREKQRALQALEEFr 1689
Cdd:COG4913 388 EAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrksniparlLALRDAlAEALGLDEAELPFVGEL- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1690 LQAEEAERRLRQAeAERA----------------------------RQVQVALETAQRSAEVELQSKRASFAEK------ 1735
Cdd:COG4913 467 IEVRPEEERWRGA-IERVlggfaltllvppehyaaalrwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAGKldfkph 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1736 --TAQLERTLQEE--HVAV---AQLREEA----ERRAQQQAEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKS 1803
Cdd:COG4913 546 pfRAWLEAELGRRfdYVCVdspEELRRHPraitRAGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1804 LAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLE 1880
Cdd:COG4913 626 LAEAEERLEAL----------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1881 EELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEA 1960
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1961 KRQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRRLEEQAAQHKAD 2037
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVAD 850
|
650
....*....|....*...
gi 2124423178 2038 IEERLAQLRKASESELER 2055
Cdd:COG4913 851 LLSKLRRAIREIKERIDP 868
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
187-289 |
1.37e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.85 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 187 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-K 263
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpE 76
|
90 100
....*....|....*....|....*..
gi 2124423178 264 LVNIRNDDI-ADGNPKLTLGLIWTIIL 289
Cdd:cd00014 77 LDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
306-405 |
4.41e-17 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 79.90 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 2124423178 386 ED-VDVPQPDEKSIITYVSSL 405
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
310-407 |
5.57e-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: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 310 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 388
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2124423178 389 DVPQPDEKSIITYVSSLYD 407
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1113-2022 |
5.90e-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: 88.97 E-value: 5.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1113 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1192
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1193 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTHG----AEEVLKAHEEQLKEAQ 1263
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1264 AVPATL-PELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1342
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1343 dlRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAmvladsravreqlrqekalleEIERHGEKVEECQRFAKQY 1422
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1423 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTtltsqyiKFISETLRRMEEEERLAEQQR 1502
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVE-------KELSKLQRELAEAEAQARASE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1503 AEERERlAAVEAALEKQ--------RQLAEAHAQAKAQAEQEAQElqrRMQEEVARREEAAVDAQQQKRS---------- 1564
Cdd:TIGR02169 504 ERVRGG-RAVEEVLKASiqgvhgtvAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflp 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1565 ---IQEELQHLRQSSEA--------------EIQAKARQV-------EAAERSRlRIEEEIRVVRLQLETTERQ---RGG 1617
Cdd:TIGR02169 580 lnkMRDERRDLSILSEDgvigfavdlvefdpKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1618 A-EGELQALRARAEEAEAQKRQAQEEA-ERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEfrlqaeea 1695
Cdd:TIGR02169 659 SrAPRGGILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------- 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1696 errlrqaEAERARQVQVALETAQRSAEVELQSKRASFAE---KTAQLERTLQEEHVAVAQLREEAERraqqqaeaerare 1772
Cdd:TIGR02169 731 -------EEEKLKERLEELEEDLSSLEQEIENVKSELKEleaRIEELEEDLHKLEEALNDLEARLSH------------- 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1773 eaerelERWQLKANEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA 1852
Cdd:TIGR02169 791 ------SRIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1853 QQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS 1932
Cdd:TIGR02169 862 KKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1933 KQRLE--AEASRFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLAEKLAaigeatRLKTEAEiALKEK 2006
Cdd:TIGR02169 941 GEDEEipEEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILER 1008
|
970
....*....|....*.
gi 2124423178 2007 EAENERLRRLAEDEAF 2022
Cdd:TIGR02169 1009 IEEYEKKKREVFMEAF 1024
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2389-2841 |
1.29e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2389 KLKARI-EAENRaliLRD-KDNTQRV--LQEEAEK-MKHVAEEAARlsvaAQEAARLRELAEEDLAQQRALAEKMLKEKM 2463
Cdd:COG1196 169 KYKERKeEAERK---LEAtEENLERLedILGELERqLEPLERQAEK----AERYRELKEELKELEAELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2464 QAVQ-EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGF----QRTLEAERQRQLEM------SAEAERL 2532
Cdd:COG1196 242 EELEaELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEerrrelEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2533 KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQE 2612
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2613 AKLLQLKSEEMQtvqqeqllqetqALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEK 2692
Cdd:COG1196 402 LEELEEAEEALL------------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2693 QQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKA 2772
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2773 LPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQRLV-QGRTTVAELAQREDVRRYLQG 2841
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgAAVDLVASDLREADARYYVLG 619
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
308-419 |
1.58e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 78.49 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 2124423178 388 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 419
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1248-1738 |
1.63e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.89 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1248 AEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQ--RHGERDVEVERWR 1325
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkKKADELKKAAAAK 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1326 ERVAQLLERWQAVLAQTDLRQRELEqlgrqlryyRESADPLGAWLQDAKRRQEQIQAmvlADSRAVREQLRQEKALLEEI 1405
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEE---------AKKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1406 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqeyvdlrtRYSELTTLTSQYIKfiS 1485
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---------KKAEEKKKADELKK--A 1554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQlaeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1565
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1566 QEELQHLRQ--SSEAEIQAKARQV-EAAERSRLRIEEEIRVVRLQLETTERQRGGAEGElqalrARAEEAEAQKRQAQEE 1642
Cdd:PTZ00121 1629 EEEKKKVEQlkKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-----KKAAEALKKEAEEAKK 1703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1643 AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAER--RLRQAEAERARQVQVALETAQRS 1720
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKiaHLKKEEEKKAEEIRKEKEAVIEE 1783
|
490
....*....|....*...
gi 2124423178 1721 AEVELQSKRASFAEKTAQ 1738
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1111-1745 |
1.64e-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: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1111 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkepaRECAQRIAEQQK----AQAEVEGLGK 1185
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1186 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKE--- 1261
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqle 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1262 --AQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQ-QRHGERDVEVERWRERVAQLLERWQAV 1338
Cdd:TIGR02168 383 tlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1339 LAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMV----------------LADSRAVREQLRQ--EKA 1400
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallknqsglsgilgvLSELISVDEGYEAaiEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1401 L--------------------------------LEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP-- 1446
Cdd:TIGR02168 543 LggrlqavvvenlnaakkaiaflkqnelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYll 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1447 -------------AKKPKVQSGSESVIQEYVDLRTRYSelttLTSQYIKFISETL---RRMEEEERLAEQQRAEERERLA 1510
Cdd:TIGR02168 623 ggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1511 AVEAALEKQRQLAEAHAQAKAQAEQEAQELqRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAA 1590
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKELTEL----EAEIEELEERLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1591 ERSRLRIEEEIrvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKA 1670
Cdd:TIGR02168 774 EEELAEAEAEI-------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1671 EAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERArQVQVALETAqRSAEVELQSKRASFAEKTAQLERTLQE 1745
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1504-2048 |
2.11e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.28 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1504 EERERLAAVEAALEKQRQLAEAHAQAkaqaeQEAQElQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqsseaeIQAK 1583
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEAL-----EDARE-QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1584 ARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDETQ 1655
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1656 RKRQAE----------AELAVRVKAEAEAAREKQRALQ-ALEEFRLQAEEAERRLRQAEAERArqvqvALETAQRSAEVE 1724
Cdd:COG4913 367 LLAALGlplpasaeefAALRAEAAALLEALEEELEALEeALAEAEAALRDLRRELRELEAEIA-----SLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1725 LQSKRASFAEKTAQLERTLQ--EEHVAVAQLReeaerraqqqaeaerareeaerelERWQLKANEAL---RLRL------ 1793
Cdd:COG4913 442 LLALRDALAEALGLDEAELPfvGELIEVRPEE------------------------ERWRGAIERVLggfALTLlvppeh 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1794 --QAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAE 1868
Cdd:COG4913 498 yaAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1869 TEQG---------------------------EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARA 1921
Cdd:COG4913 578 TRAGqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1922 EEESRSTS--------EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIG 1990
Cdd:COG4913 658 WDEIDVASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLE 737
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1991 EATRLKTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 2048
Cdd:COG4913 738 AAEDLARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1248-2177 |
4.61e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.28 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1248 AEEVLKAHEEQLKEAQAVpatLPELEATKAALKKLRAQAEAqqpmFDALRDELRGAqEVGERLQQrhgerdveverWRER 1327
Cdd:TIGR02169 175 ALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAER----YQALLKEKREY-EGYELLKE-----------KEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1328 VAQLlerwQAVLAQTDLRQRELEQLGRQLRyyrESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIER 1407
Cdd:TIGR02169 236 ERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1408 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltsqyikfiset 1487
Cdd:TIGR02169 309 ---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1488 LRRMEEEERLAeqqrAEERERLAAVEAALEK-QRQLaeahaqakaqaeQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1566
Cdd:TIGR02169 370 RAELEEVDKEF----AETRDELKDYREKLEKlKREI------------NELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1567 EELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaERL 1646
Cdd:TIGR02169 434 AKINEL----EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1647 RRQVQDETQRKRQAE----AELaVRVKAEAEAARE---KQRALQALEEFRLQAEEAERRLRQAEAERA--------RQVQ 1711
Cdd:TIGR02169 509 GRAVEEVLKASIQGVhgtvAQL-GSVGERYATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplnkmRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1712 VALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQqqaeaerareeaerelerwqlkaneaLRL 1791
Cdd:TIGR02169 588 RDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGK--------------------------YRM 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1792 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVR------QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1865
Cdd:TIGR02169 642 VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERleglkrELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1866 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLeaEASRFRE 1945
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA----LNDLEARL--SHSRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1946 LAEEaarLRALAEEAKRQR-QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRrlaedeafqR 2024
Cdd:TIGR02169 796 IQAE---LSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK---------K 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2025 RRLEEQAAQHKA---DIEERLAQLRKASEsELERQKGLVEdtlRQRRQVEEEILALKVSFEKAAAGKAELELELGRIrsn 2101
Cdd:TIGR02169 864 EELEEELEELEAalrDLESRLGDLKKERD-ELEAQLRELE---RKIEELEAQIEKKRKRLSELKAKLEALEEELSEI--- 936
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2102 aEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2177
Cdd:TIGR02169 937 -EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
311-406 |
4.77e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 77.02 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 311 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 389
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 2124423178 390 VPQPDEKSIITYVSSLY 406
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1384-2074 |
6.79e-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: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1384 VLADSRAVREQLRQEKALLEEIERHgekveecQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEY 1463
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1464 VDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERerlaaVEAALEKQRQLAEAHAQAKAQAEQEAQELQRR 1543
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT-----LHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1544 MQEEvarrEEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrLQLETTERQRGGAEGELQ 1623
Cdd:TIGR00618 382 HTLQ----QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-----LQQRYAELCAAAITCTAQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1624 ALRARaeEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAE---RRL 1699
Cdd:TIGR00618 453 CEKLE--KIHLQEsAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltRRM 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1700 RQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEhVAVAQLREEAERRAQQQAEAERAREEAEREle 1779
Cdd:TIGR00618 531 QRGEQTYAQ-----LETSEEDVYHQLTSERKQRASLKEQMQEIQQSF-SILTQCDNRSKEDIPNLQNITVRLQDLTEK-- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1780 rwQLKANEALRLRLQAEEVAQQkslaqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQ---RL 1856
Cdd:TIGR00618 603 --LSEAEDMLACEQHALLRKLQ-------------------------PEQDLQDVRLHLQQCSQELALKLTALHAlqlTL 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1857 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLAS-KARAEEESRSTSEKSK-- 1933
Cdd:TIGR00618 656 TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASSSLGSDla 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1934 QRLEAEA---SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLkteaeiaLKEKEAEN 2010
Cdd:TIGR00618 736 AREDALNqslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------LKTLEAEI 808
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2011 ERLRRLAEDEafqRRRLEEQAAQHKADIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEI 2074
Cdd:TIGR00618 809 GQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSA-TLGEITHQLLKYEECSKQLAQLTQEQ 868
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
308-407 |
6.90e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 76.16 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 2124423178 388 VDV--PQPDEKSIITYVSSLYD 407
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1289-2199 |
9.52e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 85.23 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1289 QQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQA----------VLAQTDLRQRELEQLGRQLRY 1358
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1359 YRESADPLGAWLQ-DAKRRQEQIQAM--VLADSRAVREQLRQEKALLEeierhgekveecqrfAKqyinaIKDYELQLVT 1435
Cdd:pfam01576 83 RLEEEEERSQQLQnEKKKMQQHIQDLeeQLDEEEAARQKLQLEKVTTE---------------AK-----IKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1436 YKAQlepvasPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTLTSQYIKFISETLRRMEEEE----RLAEQQRAEERE 1507
Cdd:pfam01576 143 LEDQ------NSKLSKERKLLEERISEFTSNLAEEEEkaksLSKLKNKHEAMISDLEERLKKEEkgrqELEKAKRKLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1508 RLAAVEAALEKQRQLAEAHAQAkAQAEQEAQELQRRMQEEVARREEaavdAQQQKRSIQEELQHLRQSSEAEIQAKARqv 1587
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQL-AKKEEELQAALARLEEETAQKNN----ALKKIRELEAQISELQEDLESERAARNK-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1588 eaAERSRLRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELav 1666
Cdd:pfam01576 290 --AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1667 rvkaeAEAAREKQRALQALEEFRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEktAQLERTLQEE 1746
Cdd:pfam01576 362 -----TEQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1747 HVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAQAEAEKqkeeaerearrrgka 1826
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL--------------- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1827 EEQAVRQRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEaelak 1906
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA----- 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1907 vrAEMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEASRFRE-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAe 1979
Cdd:pfam01576 566 --AAYDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQKKFDQmLAEEKAISARYAEERDRAEAEAREKETRALSLA- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1980 RVLAEKLAAIGEATR----LKTEAEIALKEKEA------ENERLRRLAEDEAFQ-RRRLEE-----QAAQH-KADIEERL 2042
Cdd:pfam01576 643 RALEEALEAKEELERtnkqLRAEMEDLVSSKDDvgknvhELERSKRALEQQVEEmKTQLEEledelQATEDaKLRLEVNM 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2043 AQLRKASESELERQKGLVEDT----LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAeLEAMR 2118
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEA-VKQLK 801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2119 QRQLAAEEEQRRREAEERVQKS-LAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQDAAQKRLQA 2196
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDEiLAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQ 881
|
...
gi 2124423178 2197 EEK 2199
Cdd:pfam01576 882 DEK 884
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1560-2503 |
9.94e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.12 E-value: 9.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1560 QQKRSIQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEA----- 1634
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1635 QKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAR------EKQRALQALEEFRLQAEEAE-----RRLRQAE 1703
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1704 AERARQVQVALETaqrsaEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwql 1783
Cdd:TIGR02169 311 AEKERELEDAEER-----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1784 kanEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQEL 1862
Cdd:TIGR02169 367 ---EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1863 IRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAE 1939
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1940 ASRFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAigeatrlktEAEIALKEKEAENER---LRRL 2016
Cdd:TIGR02169 524 HGTVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKM 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2017 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQ--------VEEEIlalkvsFEKAAAgk 2088
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLmgkyrmvtLEGEL------FEKSGA-- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2089 aeleLELGRIRSNAEDTLRSKEQAELEAMRQRqlaaeeeqrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEA 2168
Cdd:TIGR02169 655 ----MTGGSRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDEL 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2169 RRLRERAEQE----SARQLQLAQDAAQKRLQAEEkahafaVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEAR 2244
Cdd:TIGR02169 708 SQELSDASRKigeiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2245 ERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQT 2324
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2325 LRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfsLRVQMEELGKLKARIEaenralILR 2404
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ---LRELERKIEELEAQIE------KKR 916
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2405 DKDNTQRV-LQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQK 2483
Cdd:TIGR02169 917 KRLSELKAkLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
970 980
....*....|....*....|
gi 2124423178 2484 ELAQEQARRLQEDKEQMAQQ 2503
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKK 1015
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
308-411 |
1.12e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 75.86 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 2124423178 388 VDV--PQPDEKSIITYVSSLYDAMPR 411
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2140-2834 |
2.01e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2140 SLAAEEEAARQRKAALEEVERLKAKVEEARRlRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2219
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2220 QSMLERLrgeaeaarraaeeaeeareraereaaQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2299
Cdd:PTZ00121 1154 VEIARKA--------------------------EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2300 EQAALRQKQAADAEMEKHK---KFAEQTlRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVE-- 2374
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAeavKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKka 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2375 EElfslRVQMEELGKLKARIEAENRALILRDKDNTQRvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2454
Cdd:PTZ00121 1287 EE----KKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2455 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLEQEtqgfqrtlEAERQRQLEMSAEAErlKL 2534
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKA--------AAAKKKADEAKKKAE--EK 1430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2535 RVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvqtleiQRQQSDHDAERLRQAiAELEREKEKLKQEAK 2614
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------KADEAKKKAEEAKKA-DEAKKKAEEAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2615 LLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQ----MEE 2690
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEedknMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2691 EKQQLVASMEEAR-----------------QRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2753
Cdd:PTZ00121 1581 RKAEEAKKAEEARieevmklyeeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2754 ---AALAHSEEIAASQA-TAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQ--------RLQEVGILSTEELQRLVQ 2821
Cdd:PTZ00121 1661 ikaAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkkaeelkKAEEENKIKAEEAKKEAE 1740
|
730
....*....|...
gi 2124423178 2822 GRTTVAELAQRED 2834
Cdd:PTZ00121 1741 EDKKKAEEAKKDE 1753
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1096-1647 |
2.70e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1096 EDRLQAEREYGSCSHHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRIAEQQK 1175
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1176 AQAEVEGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAH 1255
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1256 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLErw 1335
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1336 qavlAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRqekalLEEIERHGEKVEEC 1415
Cdd:COG1196 485 ----ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-----AALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1416 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEE 1494
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1495 ERLAEQQRAEERERLAAVEAALEKQRqLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1574
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1575 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ-------AQEEAERLR 1647
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELE 794
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4189-4227 |
2.96e-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: 2.96e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 4189 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4227
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3611-3649 |
3.30e-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: 3.30e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3611 LLEAQIATGGIIDPVHSHRVPVEVAYQRGYFDEEMNRVL 3649
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1248-1751 |
4.37e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1248 AEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpmfDALRDELRGAQEVGERLQQRHGERDVEVErwRER 1327
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAG--LDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1328 VAQllerwQAVLAQTDLRQRELEQLGRQLRYYRESAdplGAWLQDAKRRQEQIQAMvlaDSRAvrEQLRQEKALLE-EIE 1406
Cdd:PRK02224 307 ADA-----EAVEARREELEDRDEELRDRLEECRVAA---QAHNEEAESLREDADDL---EERA--EELREEAAELEsELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1407 RHGEKVEECQrfakqyiNAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfISE 1486
Cdd:PRK02224 374 EAREAVEDRR-------EEIEELEEEIEELRERFG--DAPVDLGNAEDFLEELREERDELREREAELEAT-------LRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1487 TLRRMEEEERLAEQ-------QRAEERERLAAVEAALEKQRQLAEAHAQAKAQaeqeaqelqrrmQEEVARREEAAVDAQ 1559
Cdd:PRK02224 438 ARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------------VEEVEERLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1560 QQKRsiqeELQHLRQSSEAEIQAKARQVEAAERSRLRIEE-EIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1638
Cdd:PRK02224 506 EAED----RIERLEERREDLEELIAERRETIEEKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1639 AQ--EEAERLRR--QVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA--ERRLRQAEAERAR---- 1708
Cdd:PRK02224 582 AElkERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERaeey 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2124423178 1709 QVQVALETAQRSAE-VELQSKRASFAEKTAQLERtLQEEHVAVA 1751
Cdd:PRK02224 662 LEQVEEKLDELREErDDLQAEIGAVENELEELEE-LRERREALE 704
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1206-1959 |
4.65e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 82.71 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1206 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKtislvirSTHGAEEVLKAHEEQLKE-AQAVPATLPELEATKAALKKLRA 1284
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKK-------SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1285 QAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQlgRQLRYYRESAD 1364
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1365 PLGAWLQDAKRRQEQI---QAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYElQLVTYKAQLE 1441
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1442 pvaspAKKPKVQSGSesviqeyvdlrtrySELTTLTSQYIKFISETLRRMEEEERL--AEQQRAEERERLAAVEAALEKQ 1519
Cdd:TIGR00618 390 -----TLTQKLQSLC--------------KELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1520 RQ---LAEAHAQ-------AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA--EIQAKARQV 1587
Cdd:TIGR00618 451 AQcekLEKIHLQesaqslkEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1588 EAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1667
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1668 VKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1747
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL---QLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1748 VAVAQLREEAER---RAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArrrg 1824
Cdd:TIGR00618 687 SEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE---- 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 kaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQHEAAAATQKRQE 1899
Cdd:TIGR00618 762 --AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEE 839
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1900 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEE 1959
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1461-1970 |
4.80e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.12 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1461 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERL---AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE--Q 1535
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1536 EAQELQRRMQEEVARREEAavdaQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQR 1615
Cdd:COG4717 133 ELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1616 GGAEGELQALRARAEEAEAQKRQAQEEAERlrrqvQDETQRKRQAEAELAVRVkaeaeaarekqrALQALEEFRLQAEEA 1695
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEA-----AALEERLKEARLLLLIAA------------ALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1696 ERRLRQAEAERARQVQVALETAQRsaevelqsKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAE 1775
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAR--------EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1776 RELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1855
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1856 LAAEQELIRLRAETEQGEQqrqlLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQR 1935
Cdd:COG4717 411 LEELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQE 477
|
490 500 510
....*....|....*....|....*....|....*
gi 2124423178 1936 LEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1970
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1504-2199 |
7.16e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 82.32 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1504 EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR--QSSEAEIQ 1581
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLReaLQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1582 AKARQVEAAERSRLRIEEEIRVVRLQLETTERQrggaegelQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqAE 1661
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ--------EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR-IH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1662 AELAVRvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALetaqrsaevelqSKRASFAEKTAQLER 1741
Cdd:TIGR00618 314 TELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT------------SIREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1742 TLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAlrlRLQAEEVAQQKSLAQAEA--------EKQK 1813
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAaitctaqcEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1814 EEAEREARRRGKAEEQAVRQRE-LAEQELEKQ----RQLAEGTAQQRLAAEQELIRLRAET------------EQGEQQR 1876
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEqIHLQETRKKavvlARLLELQEEPCPLCGSCIHPNPARQdidnpgpltrrmQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1877 QLLEEELARLQHEAAAATQKRQELEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEaeasrfRELAEEAARLRAL 1956
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQ------DLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1957 AEEAKRQ-RQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 2035
Cdd:TIGR00618 611 ACEQHALlRKLQPEQDLQDVRLHLQQCSQELAL--KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2036 adiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALkvsfekaAAGKAELelelgrirsNAEDTLRSKEQAELE 2115
Cdd:TIGR00618 689 ---KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS-------SSLGSDL---------AAREDALNQSLKELM 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2116 AMRQRQLAAEEEQRRREAEERV------QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE-SARQLQLAQD 2188
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIlNLQCETLVQE 829
|
730
....*....|.
gi 2124423178 2189 AAQKRLQAEEK 2199
Cdd:TIGR00618 830 EEQFLSRLEEK 840
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2952-2990 |
1.01e-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: 1.01e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 2952 LLEAQIATGGVIDPVHSHRVPVEVAYQRGYFDEEMNRVL 2990
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3870-3908 |
1.16e-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: 1.16e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3870 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3908
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1212-2077 |
1.24e-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: 81.65 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1212 SELELTLGKLEQVRslsaiylEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATK--AALKKLRAQAEAQ 1289
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1290 QPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLaQTDLR--QRELEQLGRQLRYYRESadplg 1367
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIAEKERE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1368 awLQDAKRRQEQIQAmvladsravreqlrQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPA 1447
Cdd:TIGR02169 317 --LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1448 KKPKvqsgsesviQEYVDLRTRYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHA 1527
Cdd:TIGR02169 381 AETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1528 QAKAQAEQEAQELQRRMQeevarreeaavDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1607
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1608 LETTERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDETQRKRQAEaeLAVRVKA------EAEAAREK 1678
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIE--LLKRRKAgratflPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1679 QRALQALEE-----FRLQAEEAERRLRQAEAERARQVQV--ALETAQR--------SAEVELQSKRA-----SFAEKTAQ 1738
Cdd:TIGR02169 587 RRDLSILSEdgvigFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1739 LERTLQEEHVAVAqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEaer 1818
Cdd:TIGR02169 667 LFSRSEPAELQRL----------------------------RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--- 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1819 earrrgKAEEQAVRQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqhEAA 1891
Cdd:TIGR02169 716 ------RKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1892 AATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1970
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1971 AARQRAEAERVLAEKLAAI----GEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLR 2046
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIE 937
|
890 900 910
....*....|....*....|....*....|...
gi 2124423178 2047 KASESELE-RQKGLVEDTLRQRRQ-VEEEILAL 2077
Cdd:TIGR02169 938 DPKGEDEEiPEEELSLEDVQAELQrVEEEIRAL 970
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1221-1689 |
1.92e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.73 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1221 LEQVRSLSAIYLEKLKTISLVIRSTHGAEeVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDEL 1300
Cdd:COG4913 254 LEPIRELAERYAAARERLAELEYLRAALR-LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1301 RGAQevGERLQQRhgERDVE-VERWRERVAQLLERWQAVLAQTDLR----QRELEQLGRQLRYYRESADPLGAWLQDAKR 1375
Cdd:COG4913 333 RGNG--GDRLEQL--EREIErLERELEERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1376 RQEQiqamVLADSRAVREQLRQEKALLE---------------EIERH-GEKVEEC------------------------ 1415
Cdd:COG4913 409 EAEA----ALRDLRRELRELEAEIASLErrksniparllalrdALAEAlGLDEAELpfvgelievrpeeerwrgaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1416 --QRF-----------AKQYINAIKDyELQLVTYKAqlEPVASPAKKPKVQSGS--------ESVIQEYVD--LRTRYS- 1471
Cdd:COG4913 485 ggFALtllvppehyaaALRWVNRLHL-RGRLVYERV--RTGLPDPERPRLDPDSlagkldfkPHPFRAWLEaeLGRRFDy 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1472 -------ELT------TLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERERLAAVEAALEKQRQLAEAHAQA 1529
Cdd:COG4913 562 vcvdspeELRrhpraiTRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1530 KAQAEQEAQELQRRmqEEVARREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQLE 1609
Cdd:COG4913 640 LDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1610 TTERQRGGAEGELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF 1688
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
.
gi 2124423178 1689 R 1689
Cdd:COG4913 797 N 797
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
308-409 |
1.99e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 72.42 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 2124423178 388 -VDVPQPDEKSIITYVSSLYDAM 409
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1863-2664 |
2.22e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.78 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1863 IRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1940
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1941 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdE 2020
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2021 AFQRRRLEEQAAQHKADIEERLAQLRKASESELERQkglvedtlrQRRQVEEeilalkvsfeKAAAGKAELELELGRIRS 2100
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2101 NAEdtLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2180
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2181 rQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEE 2260
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2261 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRL 2340
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2341 QLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEEL-------GKLKARIEAENRALI--LRDKDNTQR 2411
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlteklSEAEDMLACEQHALLrkLQPEQDLQD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2412 VLQEEAEKMKHVAEEAARLSVAA--------QEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2483
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2484 ELAQEQARRLQEDKEQMAQQLEQETQGfqrTLEAERQRQLEMSAEA-ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2562
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAA---REDALNQSLKELMHQArTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2563 KLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQeakLLQLKSEEMQTVQQEQLLQETQALQQsf 2642
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS---RLEEKSATLGEITHQLLKYEECSKQL-- 861
|
810 820
....*....|....*....|..
gi 2124423178 2643 lsekDTLLQRERFIEQEKAKLE 2664
Cdd:TIGR00618 862 ----AQLTQEQAKIIQLSDKLN 879
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
306-406 |
2.57e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.41 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 385
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 2124423178 386 ED-VDVPQPDEKSIITYVSSLY 406
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1377-2384 |
2.74e-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: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1377 QEQIQAM--VLADSRAVREQLRQEKALLEEI--------ERHGEKVEECQRFAKQYINAIKDYELQL-----VTYKAQLE 1441
Cdd:pfam01576 46 QEQLQAEteLCAEAEEMRARLAARKQELEEIlhelesrlEEEEERSQQLQNEKKKMQQHIQDLEEQLdeeeaARQKLQLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1442 PVASPAKKPKVQS-------GSESVIQEYVDLRTRYSELTT--------------LTSQYIKFISETLRRMEEEE----R 1496
Cdd:pfam01576 126 KVTTEAKIKKLEEdillledQNSKLSKERKLLEERISEFTSnlaeeeekakslskLKNKHEAMISDLEERLKKEEkgrqE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1497 LAEQQRAEERERLAAVEAALEKQRQLAEAHAQAkAQAEQEAQELQRRMQEEVARREEAavdaQQQKRSIQEELQHLRQSS 1576
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQL-AKKEEELQAALARLEEETAQKNNA----LKKIRELEAQISELQEDL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1577 EAEIQAKARqveaAERSRLRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQ 1655
Cdd:pfam01576 281 ESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1656 RKRQAEAELAvrvkaeaEAAREKQRALQALEEFRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEk 1735
Cdd:pfam01576 353 KHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1736 tAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAQAEAEKqkee 1815
Cdd:pfam01576 424 -SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1816 aerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQ 1895
Cdd:pfam01576 495 -----------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1896 KRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEASRFRE-LAEEAARLRALAEEAKRQRQLAE 1968
Cdd:pfam01576 560 QLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQKKFDQmLAEEKAISARYAEERDRAEAEAR 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1969 EDAARQRAEAeRVLAEKLAAIGEATR----LKTEAEIALKEKEA------ENERLRRLAEDEAFQ-RRRLEE-----QAA 2032
Cdd:pfam01576 633 EKETRALSLA-RALEEALEAKEELERtnkqLRAEMEDLVSSKDDvgknvhELERSKRALEQQVEEmKTQLEEledelQAT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2033 QH-KADIEERLAQLRKASESELERQKGLVEDT----LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLR 2107
Cdd:pfam01576 712 EDaKLRLEVNMQALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANK 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2108 SKEQAeLEAMRQRQLAAEEEQRRREAEERVQKS-LAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQL 2185
Cdd:pfam01576 792 GREEA-VKQLKKLQAQMKDLQRELEEARASRDEiLAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEI 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2186 AQDAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSMLERLRGEAEAARR---AAEEAEEARERAEREAAQSRRQVEEA 2261
Cdd:pfam01576 871 ASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttELAAERSTSQKSESARQQLERQNKEL 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2262 eRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAE---------MEKHKKFAEQTLRQKAQVE 2332
Cdd:pfam01576 951 -KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEkklkevllqVEDERRHADQYKDQAEKGN 1029
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 2333 QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2384
Cdd:pfam01576 1030 SRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1161-1709 |
3.05e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.34 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1161 EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1240
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1241 VIRStHGAEEVlkaheEQLKEaqavpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVE 1320
Cdd:COG4913 331 QIRG-NGGDRL-----EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1321 VERWRERVAQllERWQAVLAQTDLRqRELEQLGRQLRYYRESADPLGAWLQDAkrRQEQIQAMVLADSRA--------VR 1392
Cdd:COG4913 396 LEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLAL--RDALAEALGLDEAELpfvgelieVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1393 -EQLRQEKAlleeIER--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqey 1463
Cdd:COG4913 471 pEEERWRGA----IERvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG------ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1464 vdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-AVEAALEK--QRQLAEAH------AQ 1528
Cdd:COG4913 539 --------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1529 AKAQAEQEAQELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEI--QAKARQVEAAERSRLRIEE---EIRV 1603
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAssdDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1604 VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQ 1683
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
570 580
....*....|....*....|....*.
gi 2124423178 1684 ALEEfRLQAEEAERRLRQAEAERARQ 1709
Cdd:COG4913 770 NLEE-RIDALRARLNRAEEELERAMR 794
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
186-291 |
6.64e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 70.79 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 186 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRH 259
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMAS 73
|
90 100 110
....*....|....*....|....*....|..
gi 2124423178 260 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21213 74 KRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
179-290 |
7.01e-14 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 70.77 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 179 TDERDrvqKKTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQ 248
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVE 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2124423178 249 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 290
Cdd:cd21219 66 NCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
183-287 |
7.11e-14 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 70.64 E-value: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 183 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEE 77
|
90 100
....*....|....*....|....*....
gi 2124423178 260 R-QVKLVNIRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21225 78 DlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1269-1694 |
1.16e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.89 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1269 LPELEATKAALKKLRAQAEAqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWR--ERVAQLLERWQAVLAQTDLRQ 1346
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1347 RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQekaLLEEIERHGEKVEECQRFAKQYINAI 1426
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1427 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EE 1495
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1496 RLAEQQRAEERERL--AAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKrsIQEELQHLR 1573
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1574 QSSEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLET---------TERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1644
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllgeleellEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1645 RLRRQVQ-----DETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEE 1694
Cdd:COG4717 457 ELEAELEqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
306-403 |
1.27e-13 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 69.72 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 381
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 2124423178 382 LLDPEDVDVPQPDEKSIITYVS 403
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2322-2617 |
1.38e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 77.86 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2322 EQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQRLKAEVTEAARQRSQVEEELFSL--RVQMEELGKLK-------A 2392
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2393 RIEAENRALILRDKDNTQRVLQEEAEKmkhvAEEAARLSVAAQEAARLRELAEEDLAQQR-----------ALAEKMLKE 2461
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEERKR----ELERIRQEEIAMEISRMRELERLQMERQQknervrqeleaARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2462 KMQAVQEATRLKAEaELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQlemsAEAERLKLRVAEMSR 2541
Cdd:pfam17380 410 ERQRKIQQQKVEME-QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE----EERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2542 AQARAEEDAqrfRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRqaIAELEREKEKLKQEAKLLQ 2617
Cdd:pfam17380 485 DRKRAEEQR---RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEMEERRRIQ 555
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
765-943 |
1.41e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 72.86 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 765 LYSFVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVESFQ 844
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 845 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDERDQLNEY 924
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 2124423178 925 RGHLSGLARRAKAIVQLKP 943
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
306-406 |
2.16e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 69.29 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 385
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 2124423178 386 ED-VDVPQPDEKSIITYVSSLY 406
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3204-3242 |
5.22e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 5.22e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3204 LLEAQAGTGHIIDPATSARLTVDEAVRSGLVGPELHEKL 3242
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
205-288 |
5.36e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.39 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 205 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGN 276
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGH 100
|
90
....*....|..
gi 2124423178 277 PKLTLGLIWTII 288
Cdd:cd21223 101 REKTLALLWRII 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1825-2625 |
7.31e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQ-QRLAAEQELIR-----LRAETEQGEQQRQLLEEELARLQHEAAAATQKR- 1897
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQlASLEEELEKLTeeiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKi 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1898 QELEAELAKVRAEMEVLLASKARAEEESRST-SEKSKQRLEAEASRfRELAEEAARLRALAEEAKRQRQlaEEDAARQRA 1976
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKLLAEIEELE-REIEEERKRRDKLTEEYAELKE--ELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1977 EAErvlAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrRRLEEQAAQHKADI---EERLAQLRKASES-- 2051
Cdd:TIGR02169 374 EEV---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELADLNAAIagiEAKINELEEEKEDka 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2052 -ELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRirsnAEDTLRSKEQAELEAMRQRQLAAEEEQRr 2130
Cdd:TIGR02169 448 lEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAVEEVLKASIQG- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2131 reaeerVQKSLAAEEEAARQRKAALEEV--ERLKAKVEE----ARRLRERAEQESARQL------QLAQDAAQKRLQAEE 2198
Cdd:TIGR02169 523 ------VHGTVAQLGSVGERYATAIEVAagNRLNNVVVEddavAKEAIELLKRRKAGRAtflplnKMRDERRDLSILSED 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2199 KAHAFAV-----QQKEQELQQTLQQEQSMLER---------------LRGEAEAARRAAEEAEEARERAEREAAQSRRQV 2258
Cdd:TIGR02169 597 GVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDieaarrlmgkyrmvtLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2259 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2338
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2339 RLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEaE 2418
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-K 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2419 KMKHvaEEAARLSVAAQEAARLRELaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKE 2498
Cdd:TIGR02169 834 EIQE--LQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKERDELEAQLRELERKIE 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2499 QMAQQLEQEtqgfqrtleaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQrfrkqAEEIGEKLHRTELATQEKVtlv 2578
Cdd:TIGR02169 907 ELEAQIEKK-----------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-----EELSLEDVQAELQRVEEEI--- 967
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 2124423178 2579 QTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2625
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1825-2041 |
9.67e-13 |
|
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: 73.26 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1904
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1905 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEASRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1980
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423178 1981 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2041
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1271-1753 |
1.04e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.34 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1271 ELEATKAALKKLRAQAEAQQPM------FDALRDELRGAQEVGERLQQRHGERdvEVERWRERVAQLLERWQAVLAQTDL 1344
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1345 RQRELEQLGRQLRyyresadplgawlqDAKRRQEQIqamvladsravreQLRQEKALLEEIERHGEKVEECQRFAKQYIN 1424
Cdd:COG4913 314 LEARLDALREELD--------------ELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1425 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSELT------------------TLTSQYIKF- 1483
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDLRrelreleaeiaslerrksNIPARLLALr 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1484 --ISETLRRMEEEER-LAE--QQRAEERERLAAVEAALEKQRQ--LAEAHAQAKAQAEQEAQELQRRMQ-EEVARREEAA 1555
Cdd:COG4913 447 daLAEALGLDEAELPfVGEliEVRPEEERWRGAIERVLGGFALtlLVPPEHYAAALRWVNRLHLRGRLVyERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1556 VDAQQQKRSIQEEL------------QHLRQS-------SEAEIQAKARQVEAA-----ERSRLRIEEEIRVVRL----- 1606
Cdd:COG4913 527 ERPRLDPDSLAGKLdfkphpfrawleAELGRRfdyvcvdSPEELRRHPRAITRAgqvkgNGTRHEKDDRRRIRSRyvlgf 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1607 ----QLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR--QVQDETQRKRQAEAELAvRVKAEAEAAREKQR 1680
Cdd:COG4913 607 dnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIA-ELEAELERLDASSD 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1681 ALQALEEfrlQAEEAERRLRQAEAERArqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1753
Cdd:COG4913 686 DLAALEE---QLEELEAELEELEEELD-----ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1506-2031 |
1.10e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 75.28 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1506 RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR 1585
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1586 QVEAAERSRLRIEEEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1662
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1663 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1742
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1743 LQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARR 1822
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1823 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEA 1902
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1903 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1982
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2124423178 1983 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 2031
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1573-2207 |
1.24e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 74.87 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1573 RQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1646
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1647 RRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1726
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1727 SKRASFAEKTAQLERTLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1805
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1806 QAEAEKQKEEAEREARRRGKAEEQAV-RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelA 1884
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE--L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1885 RLQHEAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE 1958
Cdd:pfam12128 526 ELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1959 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 2038
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2039 EERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILA-LKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAM 2117
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAyWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2118 RQRQLAAEEEQRRREAEERVQKSLaaeEEAARQRKAALE-----------EVERLKAKVEEARRLRERAEQESARQlqlA 2186
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKI---ERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARL---I 834
|
650 660
....*....|....*....|.
gi 2124423178 2187 QDAAQKRLQAEEKAHAFAVQQ 2207
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQ 855
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1552-2174 |
1.51e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1552 EEAAVDAQQQKRSIQEELQHLRQ--SSEAEIQakaRQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1629
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKfiKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1630 EEAEAQKRQAQEEAERLR------RQVQDETQRKRQAEAELAVRVKaEAEAAREKQRALQALEEFRLQAEEAERRLRQAE 1703
Cdd:PRK03918 238 EEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1704 AERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTLQEehvavaqlreeaerraqqqaeaerareeaERELERWQL 1783
Cdd:PRK03918 317 SRLEEEINGIEERIK-----ELEEKEERLEELKKKLKELEKR-----------------------------LEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1784 KANEALRLRLQAEEVaqqkslaqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1863
Cdd:PRK03918 363 LYEEAKAKKEELERL----------------------------------KKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1864 RLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE-----LAKVRAEMEVLLASKARAEEESRSTsEKSKQRLE- 1937
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKL-RKELRELEk 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1938 --AEASRFRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIA---LKEKEAENER 2012
Cdd:PRK03918 488 vlKKESELIKLKELAEQLKELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2013 LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SESELERQKGLVEDTLRQRRQVEEEILALKVSFEK 2083
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2084 AaagKAELElELGRIRSnaEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 2163
Cdd:PRK03918 645 L---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
650
....*....|.
gi 2124423178 2164 KVEEARRLRER 2174
Cdd:PRK03918 719 ALERVEELREK 729
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1521-1941 |
1.64e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.00 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1521 QLAEAHAQAKAQAEQEAQELQRRMQEEVARreeaavdaqQQKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1593
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1594 RLRIEEEIRVVRLQLEttERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELAVRVK-AEA 1672
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1673 EAAREKQRALQALEEFRLQAEEA-ERRLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvava 1751
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1752 qlreeaerraqqqaEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeeaerearrrgkaEEQav 1831
Cdd:pfam17380 470 --------------EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI---------------------EEE-- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1832 RQRELAEQELEkQRQLAEGTAQQRLAAEQElirlraeteqgeQQRQLLEEELARLQHEAAAATQKRQELEAelakvraeM 1911
Cdd:pfam17380 513 RKRKLLEKEME-ERQKAIYEEERRREAEEE------------RRKQQEMEERRRIQEQMRKATEERSRLEA--------M 571
|
410 420 430
....*....|....*....|....*....|
gi 2124423178 1912 EvllaskaRAEEESRSTSEKSKQRLEAEAS 1941
Cdd:pfam17380 572 E-------REREMMRQIVESEKARAEYEAT 594
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1252-1658 |
1.65e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1252 LKAHEEQLKEAQAvpatlpELEATKAALKKLRAQaeaqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQL 1331
Cdd:TIGR02168 679 IEELEEKIEELEE------KIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1332 LERWqavlaqtDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEK 1411
Cdd:TIGR02168 746 EERI-------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1412 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspaKKPKVQSGSESVIQEYvdlrtryselttltsqyikfiSETLRRM 1491
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIE------ELSEDIESLAAEIEEL---------------------EELIEEL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1492 EEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1571
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1572 LRQSSEAEIQAKARQVEAAERSRLRIEEEI-RVVRLQLEtterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1650
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKIkELGPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
410
....*....|
gi 2124423178 1651 Q--DETQRKR 1658
Cdd:TIGR02168 1024 EeiDREARER 1033
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1833-2715 |
1.71e-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: 74.44 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1833 QRELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAe 1910
Cdd:pfam01576 109 EEQLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1911 MEVLLASKARAEEESRSTSEKSKQRLEAEASrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIG 1990
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1991 EATRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQ---------------AAQH--KADIEERLAQLRKASESEL 2053
Cdd:pfam01576 265 KIREL--EAQISELQEDLESERAARNKAEK--QRRDLGEElealkteledtldttAAQQelRSKREQEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2054 ERQKGLVEDTLRQRRQVEEEilaLKVSFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEAMRQRQlaaeeeqrr 2130
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK--------- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2131 rEAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR----------QLQLAQDAAQkrlqaEEKA 2200
Cdd:pfam01576 409 -KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesQLQDTQELLQ-----EETR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2201 HAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAE----RLKQSAEEQAQAQA 2276
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEegkkRLQRELEALTQQLE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2277 QAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKF--------------AEQTLRQKAQVEQELT---TLR 2339
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFdqmlaeekaisaryAEERDRAEAEAREKETralSLA 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2340 LQLEETDHQKSILDEELQRLKAE--------------VTEAARQRSQVEEELFSLRVQMEELG-------KLKARIEAEN 2398
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEmedlvsskddvgknVHELERSKRALEQQVEEMKTQLEELEdelqateDAKLRLEVNM 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2399 RALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELA-------EEDLAQQRALAEKMLKEKMQAVQEATR 2471
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKK 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2472 LKAEAELLQQQKE---LAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA----ERQRQLE-----------------MSA 2527
Cdd:pfam01576 803 LQAQMKDLQRELEearASRDEILAQSKESEKKLKNLEAELLQLQEDLAAseraRRQAQQErdeladeiasgasgksaLQD 882
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2528 EAERLKLRVA----EMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDHDAERLRQAIAELE 2603
Cdd:pfam01576 883 EKRRLEARIAqleeELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKELKAKLQEME 958
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2604 RE-KEKLKQ-----EAKLLQLksEEMQTVQQEQLLQETQALQQSFLSEKDTLLQrerfIEQEKAKLEQlFQDEVAKAQkl 2677
Cdd:pfam01576 959 GTvKSKFKSsiaalEAKIAQL--EEQLEQESRERQAANKLVRRTEKKLKEVLLQ----VEDERRHADQ-YKDQAEKGN-- 1029
|
970 980 990
....*....|....*....|....*....|....*...
gi 2124423178 2678 reeqqrqqkqmeEEKQQLVASMEEARQRQREAEEGVRR 2715
Cdd:pfam01576 1030 ------------SRMKQLKRQLEEAEEEASRANAARRK 1055
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3535-3573 |
1.97e-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: 1.97e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3535 LLEAQAATGFLVDPVRNQRLYVHEAVKAGIVGPELHEKL 3573
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
308-407 |
2.09e-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: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 383
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 2124423178 384 DPEDVdVPQPDEKSIITYVSSLYD 407
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
308-408 |
2.91e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 65.84 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 2124423178 388 VdVPQPDEKSIITYVSSLYDA 408
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1460-1958 |
4.30e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 73.45 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1460 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEahaqakaqaeqeaqE 1539
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1540 LQRRMQEEVARREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--RQVEAAERSRLRIEEEIRVVRLQLEtterqrgg 1617
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1618 aegelqalraRAEEAEAQKRQAQEEAERLRRQVQD-----ETQRKRQAEAELAVRVKAEAE-----AAREKQRALQALEE 1687
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADyqqalDVQQTRAIQYQQAVQALERAKqlcglPDLTADNAEDWLEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1688 FRLQAEEA-------ERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVAVAQLreeaer 1759
Cdd:PRK04863 447 FQAKEQEAteellslEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL------ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1760 raqqqaeaeRAREEAERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQ 1839
Cdd:PRK04863 516 ---------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---------------------DEDELEQLQEELEA 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1840 ELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEAAAATQKRQELEAELAKvraemevlLA 1916
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------LL 637
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2124423178 1917 SKARAEEESRSTSEKSKQRLEAEASRFREL-AEEAARLRALAE 1958
Cdd:PRK04863 638 ERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4458-4496 |
4.88e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.88e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 4458 LLEAQACTGGIIDPNTGERFPVTDAVNKGLVDKIMVDRI 4496
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1496-1958 |
5.09e-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: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1496 RLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEqEAQELQRRmQEEVARREEAAVDaqqqkrsiqeelqHLrqs 1575
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMAR-ELEELSAR-ESDLEQDYQAASD-------------HL--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1576 seAEIQAKARQVEAAERSRLRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQD--- 1652
Cdd:COG3096 337 --NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLADyqq 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1653 --ETQRKRQAEAELAVRVKAEAEAAREK-----QRALQALEEFRLQAEEAERRLRQAE------AERARQVQVALETAQR 1719
Cdd:COG3096 404 alDVQQTRAIQYQQAVQALEKARALCGLpdltpENAEDYLAAFRAKEQQATEEVLELEqklsvaDAARRQFEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1720 -SAEVElqskRASFAEKTAQLERTLQeEHVAVAQlreeaerraqqqaeaerareeaerELERWQLKANEA-LRLRLQAEE 1797
Cdd:COG3096 484 iAGEVE----RSQAWQTARELLRRYR-SQQALAQ------------------------RLQQLRAQLAELeQRLRQQQNA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1798 VAQQKSLaqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1877
Cdd:COG3096 535 ERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1878 LLEEElARLQHEAAAATQKRQELEAE----LAKVRAEMEVLLaSKARAEEESRSTSEKSKQRLEAEASRFRELA-EEAAR 1952
Cdd:COG3096 596 ELAAR-APAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERDELAARKQALESQIERLSQPGgAEDPR 673
|
....*.
gi 2124423178 1953 LRALAE 1958
Cdd:COG3096 674 LLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3280-3318 |
5.71e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 5.71e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3280 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETSKAL 3318
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
308-403 |
5.77e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.10 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 308 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 386
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 2124423178 387 DVDVPQPDEKSIITYVS 403
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4113-4151 |
8.11e-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: 8.11e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 4113 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4151
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1246-1743 |
8.46e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1246 HGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELrgAQEVGERLQQRHGERDVEVERWR 1325
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1326 ERVAQLLERWQAVLAQtdLRQ---RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1402
Cdd:COG4913 316 ARLDALREELDELEAQ--IRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1403 EEIERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIK 1482
Cdd:COG4913 394 EALEEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1483 FISETLRRMEEEERLaeqQRAEER-------------ERLAAVEAALEKQR-------QLAEAHAQAKAQAEQEAQELQR 1542
Cdd:COG4913 462 FVGELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1543 RM-----------QEEVARREEAA-VDAQQQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKARQ 1586
Cdd:COG4913 539 KLdfkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1587 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDET 1654
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1655 QRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSKRASF 1732
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDAL 778
|
570
....*....|.
gi 2124423178 1733 AEKTAQLERTL 1743
Cdd:COG4913 779 RARLNRAEEEL 789
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3946-3984 |
8.77e-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: 8.77e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3946 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3984
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2876-2914 |
9.21e-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: 9.21e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 2876 LLEAQAASGFLLDPVQNRRLTVNEAVKEGVVGPELHHKL 2914
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1682-2198 |
1.22e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1682 LQALEEFRLQAEEAE---RRLRQAEAERARQVQVALETAQRSAEVE-LQSKRASFAEKTAQLERTLQEEHVAVAQLREEA 1757
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1758 ERRAQQQAEAERAREEAEReLERWQLKANEALRLRLQ-AEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1836
Cdd:PRK02224 241 EVLEEHEERREELETLEAE-IEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1837 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1916
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1917 SKARAEEEsRSTSEKSKQRLEAEASRFRE-LAEEAARLRALAEEAKRQRQLAEE----DAARQRAEAERV--LAEKLAAI 1989
Cdd:PRK02224 399 RFGDAPVD-LGNAEDFLEELREERDELRErEAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1990 GEATRLKTEAEIALKEKEAENERLRRLAEDEAF------QRRRLEEQAAQHKADIEE---RLAQLRKAS---ESELERQK 2057
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDRierleeRREDLEELIAERRETIEEkreRAEELRERAaelEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2058 glvEDTLRQRRQVEEEILALKVSFEKAAAGKAELElELGRIRS------NAEDTL-----RSKEQAELEAMRQRQLaaee 2126
Cdd:PRK02224 558 ---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTllaaiaDAEDEIerlreKREALAELNDERRERL---- 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2127 eqrrreaeervqkslaaeeEAARQRKAALEEvERLKAKVEEARRLRERAEQ------ESARQLQLAQDAAQKRLQAEE 2198
Cdd:PRK02224 630 -------------------AEKRERKRELEA-EFDEARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVE 687
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1929-2766 |
1.32e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1929 SEKSKQRLEAEASRFRElaeeaARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIgEATRLKTEAEIALKEK-- 2006
Cdd:TIGR02169 170 RKKEKALEELEEVEENI-----ERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKea 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2007 -EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAA 2085
Cdd:TIGR02169 242 iERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2086 AGKAELELELGRIRSNAEDtlrSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQR---KAALEEVERLK 2162
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2163 AKVEE----ARRLRERAEQESARQLQLAQDAA-----QKRLQAEEKAHAFAVQQKEQElqqtlqqeqsmLERLRGEAEAA 2233
Cdd:TIGR02169 399 REINElkreLDRLQEELQRLSEELADLNAAIAgieakINELEEEKEDKALEIKKQEWK-----------LEQLAADLSKY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2234 RRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAqaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAE 2313
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV--------------------------------RGGRAVEEV 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2314 MEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-EVTEAARQRSQVEEELFSLR 2381
Cdd:TIGR02169 516 LKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2382 VQMEELGKLKARIEAENR-----------ALILRDKDNTQRV------------LQEEAEKMKHVAEEAARL-SVAAQEA 2437
Cdd:TIGR02169 594 SEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLmgkyrmvtlegeLFEKSGAMTGGSRAPRGGiLFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2438 ARLRELAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQET 2508
Cdd:TIGR02169 674 AELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2509 QGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQS 2588
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2589 DHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQalqqsfLSEKDTLLQRERF-IEQEKAKLEQLF 2667
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLGDLKKERDeLEAQLRELERKI 905
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2668 QDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEgvrrkqeelqlleqqrQQQEKLLAEENQRLRERLQR 2747
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE----------------ELSLEDVQAELQRVEEEIRA 969
|
890
....*....|....*....
gi 2124423178 2748 LEEEHRAALAHSEEIAASQ 2766
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRL 988
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1620-2198 |
1.67e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1620 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA--ER 1697
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1698 RLRQAEAERARQVQVALETA---QRSAEVELQSKRASFAEKTAQLERTLQEehvavaqlreeaerraqqqAEAERAREEA 1774
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------------------LEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1775 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE--REARRRGKAEEQAVRQRELA---EQELEKQRQLAE 1849
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAaelESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1850 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVR---AEMEVLLA---------- 1916
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1917 ----SKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE--EDAARQRAEAERVLAEKLAAIG 1990
Cdd:PRK02224 461 vegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1991 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---------ERLAQLRKASESELERQKGLVE 2061
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2062 ------DTLRQRRqveEEILALKVSFEKAAAGKAELElelgriRSNAEDTLRSKEQaELEAMRQRQlaaeeeqrrreaeE 2135
Cdd:PRK02224 621 lnderrERLAEKR---ERKRELEAEFDEARIEEARED------KERAEEYLEQVEE-KLDELREER-------------D 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2136 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2198
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1505-1989 |
1.71e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1505 ERERLAAVEAALEKQRQLAEAHAQAKAQaeqeaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqssEAEIQAKA 1584
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAE-----QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ---TALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1585 --RQVEAAERSRLRIEEEIRVVRLQLEtterqrggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRkrqaea 1662
Cdd:PRK04863 350 ieRYQADLEELEERLEEQNEVVEEADE------------------QQEENEARAEAAEEEVDELKSQLADYQQA------ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1663 elavrVKAEAEAAREKQRALQALEEFR-------LQAEEAERRLRQAEAERARQVQVALETAQRsaeVELQSKRASFAEK 1735
Cdd:PRK04863 406 -----LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQFEQ 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1736 TAQLERTLQEEHVAvaqlreeaerraqqqaeaerareeaerelERWQLKANEALR----LRLQAEEVAQQKslaqaeaek 1811
Cdd:PRK04863 478 AYQLVRKIAGEVSR-----------------------------SEAWDVARELLRrlreQRHLAEQLQQLR--------- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1812 qkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgeqQRQLLEEELARLQHEAA 1891
Cdd:PRK04863 520 --------------MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA---RLESLSESVSEARERRM 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1892 AATQKRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAK 1961
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAPAWLAAQDALArlreqsgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
490 500
....*....|....*....|....*...
gi 2124423178 1962 RQRQLAEEDAARQRAEAERVLAEKLAAI 1989
Cdd:PRK04863 663 RLSQPGGSEDPRLNALAERFGGVLLSEI 690
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1490-2613 |
1.94e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.97 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1490 RMEEEERLAEQQRAEERERLAAVEAAL----EKQRQLAEAHA--QAKAQAEQE---------------AQELQRRMQEEV 1548
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalQEQLQAETElcaeaeemrarlaarKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1549 AR---REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR-QVE--AAERSRLRIEEEIRVVrlqlettERQRGGAEGEL 1622
Cdd:pfam01576 82 SRleeEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEkvTTEAKIKKLEEDILLL-------EDQNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1623 QALRARAEEAEAQKRQAQEEAERLrrqvqdeTQRKRQAEA---ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRL 1699
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSL-------SKLKNKHEAmisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1700 RQAEAERARQVQvaletaqrSAEVELQSKRASFAEKTAQ---LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAER 1776
Cdd:pfam01576 228 QAQIAELRAQLA--------KKEEELQAALARLEEETAQknnALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1777 ELerwqlkanEALRLRLQ--AEEVAQQKSLAQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1854
Cdd:pfam01576 300 EL--------EALKTELEdtLDTTAAQQELRSKREQEVTELK--------KALEEETRSHEAQLQEMRQKHTQALEELTE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1855 RLaaeQELIRLRAETEQGeqqRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLAskaraeeesrSTSEKSKQ 1934
Cdd:pfam01576 364 QL---EQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQA----------RLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1935 RLEAeASRFRELAEEAARLRALAEEAKRQRQLAEEDAarqrAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 2014
Cdd:pfam01576 428 RAEL-AEKLSKLQSELESVSSLLNEAEGKNIKLSKDV----SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2015 RLAEDEAFQRRRLEEQAAQHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKVSFEKAAAGKAELELE 2094
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2095 LGRIRSNAEDTLrskeqaeLEAMRQRQLAAEEEQRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRER 2174
Cdd:pfam01576 575 KNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2175 AEQESARQLQLAQDAAQKRLQAEekahafavqqkeqelqqtlqqeqsmLERLRGEAEAARRAAEEAEEARERAEREAAQS 2254
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2255 RRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKKfaeQTLRQKAQVEQE 2334
Cdd:pfam01576 698 KTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQVRELEAE 757
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2335 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQ 2414
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2415 EEAEKMKHVAEEAARLSVAAQEAARLRELAEEdLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQ 2494
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDELADE-IASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKST 916
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2495 EDKEQMAQQLEQETQGFQRTLEA----ERQ------RQLEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEK 2563
Cdd:pfam01576 917 LQVEQLTTELAAERSTSQKSESArqqlERQnkelkaKLQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2564 LHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEA 2613
Cdd:pfam01576 997 VRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1164-1749 |
2.00e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1164 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLEklktislv 1241
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMA-------- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1242 irsthgaeevLKAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpmfdalrDELRGAQEVGERLQQrHGERDVE 1320
Cdd:PRK04863 584 ----------LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1321 VERWRERVAqllERWQAVLAQTD-LRQRELEQLGRQLRYyresADPLGAWL----------QDA----KRRQEQIQAMVL 1385
Cdd:PRK04863 643 LTVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDApyfsALYGPARHAIVV 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1386 ADSRAVREQLRQEKALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQS 1454
Cdd:PRK04863 716 PDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRA 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1455 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETL----------------RRMEEEERLAEQQRAEERERLAAVEAALEK 1518
Cdd:PRK04863 794 EREELAERYATLSFDVQKLQRLHQAFSRFIGSHLavafeadpeaelrqlnRRRVELERALADHESQEQQQRSQLEQAKEG 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1519 QRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAE----- 1591
Cdd:PRK04863 874 LSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrd 953
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1592 -RSRLRIEEEIRVVRLQLETTERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELavrv 1668
Cdd:PRK04863 954 aKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL---- 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1669 KAEAEAAREK-QRALQALEEFRLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAEKTAQ 1738
Cdd:PRK04863 1026 KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYH 1105
|
650
....*....|.
gi 2124423178 1739 LERTLQEEHVA 1749
Cdd:PRK04863 1106 EMREQVVNAKA 1116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1825-2122 |
2.33e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQ-RELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRqllEEELARLQHEAAAATQKR---QEL 1900
Cdd:pfam17380 295 KMEQERLRQeKEEKAREVERRRKLEE-AEKARQAEMDRQAAIYAEQERMAMER---ERELERIRQEERKRELERirqEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1901 EAELAKVRaEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAE---EAARLRALAEEAkRQRQLAEEDAARQRaE 1977
Cdd:pfam17380 371 AMEISRMR-ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-RQREVRRLEEERAR-E 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1978 AERVLAEKLAAIGEATRLKteaeialkEKEAENERLRRLAEDEAFQRRRLEEQ---------AAQHKADIEERlaQLRKA 2048
Cdd:pfam17380 448 MERVRLEEQERQQQVERLR--------QQEEERKRKKLELEKEKRDRKRAEEQrrkilekelEERKQAMIEEE--RKRKL 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2049 SESELE-RQKGLVEDtlRQRRQVEEEilalkvsfekaaaGKAELELElGRIRSNAEDTLRSKEQAELEAM-RQRQL 2122
Cdd:pfam17380 518 LEKEMEeRQKAIYEE--ERRREAEEE-------------RRKQQEME-ERRRIQEQMRKATEERSRLEAMeREREM 577
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1479-2190 |
2.34e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 70.53 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1479 QYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDA 1558
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLetteRQRGGA--------EGELQALR 1626
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1627 AR----AEEAEAQKRQAQEEAERLRRQVQDetqRKRQAEAELAVRVKA---EAEAAREKQRALQAleefrlQAEEAERRL 1699
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEITGlteKASSARSQANSIQS------QLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1700 RQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQeehVAVAQLREEAERRAQQQAEAERAREEAERELE 1779
Cdd:pfam15921 309 RNQNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1780 RWQLKANEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EG 1850
Cdd:pfam15921 385 DLHKREKE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1851 TAQQRLAAEQ----ELIRLRAETEQGEQQRQLLEEELARLqheaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESR 1926
Cdd:pfam15921 445 QMERQMAAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1927 STSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAIGEATRL-KTEAE 2000
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2001 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASESELERQKGL--VEDTLRQRRQVEEEI 2074
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDY 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2075 LALKVSF----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2147
Cdd:pfam15921 677 EVLKRNFrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEA 756
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2148 ---ARQRKAALEE-------------VERLKAKVE-EARRLRERAEQESARQLQLAQDAA 2190
Cdd:pfam15921 757 mtnANKEKHFLKEeknklsqelstvaTEKNKMAGElEVLRSQERRLKEKVANMEVALDKA 816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2322-2808 |
2.34e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2322 EQTLRQKAQVEQE--LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfslRVQMEELGKlkaRIEAENR 2399
Cdd:PTZ00121 1057 EGKAEAKAHVGQDegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE----ARKAEEAKK---KAEDARK 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2400 ALILRDKDNTQRVlqEEAEKmkhvAEEAARLSVA--AQEAARLRELAEEDLAQQRALAEKMLK-EKMQAVQEATRLKAEA 2476
Cdd:PTZ00121 1130 AEEARKAEDARKA--EEARK----AEDAKRVEIArkAEDARKAEEARKAEDAKKAEAARKAEEvRKAEELRKAEDARKAE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2477 ELLQQQKELAQEQARRLQEDKE-QMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfRK 2555
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-----AR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2556 QAEEIG---EKLHRTELATQEKVTLVQTLEIQrqqsdhdAERLRQAiAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLL 2632
Cdd:PTZ00121 1279 KADELKkaeEKKKADEAKKAEEKKKADEAKKK-------AEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2633 QETQALQQSFLSEKDTLLQRERfIEQEKAKLEQLFQ--DEVAKAQKLREEQQRQQKQMEEEKQQlVASMEEARQRQREAE 2710
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAE 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2711 EGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRA--ALAHSEEIAASQATAVKALPNGRDAPDGPATEAE 2788
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500
....*....|....*....|
gi 2124423178 2789 PEHAfDGLRQKVPAQRLQEV 2808
Cdd:PTZ00121 1509 KKKA-DEAKKAEEAKKADEA 1527
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
188-294 |
2.80e-11 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 63.41 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 188 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1097-1746 |
3.62e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1097 DRLQAEREYgscSHHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRIAEQQKA 1176
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1177 QAEVEGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVL 1252
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1253 KAHEEQLKEAQA-----VPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQE------------------VGER 1309
Cdd:TIGR02169 335 LAEIEELEREIEeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkleklkreinelkreldrLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1310 LQQRHGER---DVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQ---AM 1383
Cdd:TIGR02169 415 LQRLSEELadlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1384 VLADSRAVREQLRQEKALLEEIERHGEKV-------------------------------------EECQRFAKQY---- 1422
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvveddavaKEAIELLKRRkagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1423 -----INAIK---------------DYELQLVTYKAQLEPVASpakkpkvQSGSESVIQEYVDLRTRY------------ 1470
Cdd:TIGR02169 575 atflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFK-------YVFGDTLVVEDIEAARRLmgkyrmvtlege 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1471 ----SELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAEERErLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRmQ 1545
Cdd:TIGR02169 648 lfekSGAMTGGSRAPRGgILFSRSEPAELQRLRERLEGLKRE-LSSLQSELRRIENRLDELSQELSDASRKIGEIEKE-I 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1546 EEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEE------------IRVVRLQLETTER 1613
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlshsrIPEIQAELSKLEE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1614 QRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELAVRVKAEAEAAREKQRALQALEEfRL 1690
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLES-RL 884
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1691 QAEEAERRLRQAEAERARQVQVALETAQRSAEV---ELQSKRASFAEKTAQLERTLQEE 1746
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKrlsELKAKLEALEEELSEIEDPKGED 943
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1503-1989 |
3.96e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.98 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1503 AEERERLaaVEAALEKQRQLAEAHAQaKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKrsiqeelQHLrqsseAEIQA 1582
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQ-LAEEQYRLVEMARELEELSARESDLEQDYQAAS-------DHL-----NLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1583 KARQVEAAERSRLRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEA 1662
Cdd:COG3096 342 ALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1663 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqskrasfaEKTAQLERT 1742
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---------AARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1743 LQeehvAVAQLREEAERRaqqqaeaerareeaerelERWQlKANEALR----LRLQAEEVAQQKSlaqaeaekqkeeaer 1818
Cdd:COG3096 478 YE----LVCKIAGEVERS------------------QAWQ-TARELLRryrsQQALAQRLQQLRA--------------- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1819 earRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQ 1898
Cdd:COG3096 520 ---QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1899 ELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE 1968
Cdd:COG3096 589 QLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGG 668
|
490 500
....*....|....*....|.
gi 2124423178 1969 EDAARQRAEAERVLAEKLAAI 1989
Cdd:COG3096 669 AEDPRLLALAERLGGVLLSEI 689
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1301-1726 |
4.13e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.98 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1301 RGAQEvgERLQQRHGERDVEVERWR---------ERVAQLLERW-------------QAVLAQTDLRQRELEqlgRQLRY 1358
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELE---RELAQ 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1359 YRESADPLGAWLQDAKRRQEQI-----QAMVLADsravrEQLRQekaLLEEIERHGEKVEECQRFAKQYINAIkdyelql 1433
Cdd:COG3096 855 HRAQEQQLRQQLDQLKEQLQLLnkllpQANLLAD-----ETLAD---RLEELREELDAAQEAQAFIQQHGKAL------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1434 vtykAQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltSQYIKFISETLRRM------EEEERLAEQQRAEE-- 1505
Cdd:COG3096 920 ----AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRL----KQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEkl 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1506 RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHLrqsseaEIQAKAR 1585
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL------GVQADAE 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1586 QVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDETQRKR 1658
Cdd:COG3096 1053 AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERR 1132
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1659 QAEAELAVrvkaeaeaarekqralQALEEFRLQAEEAERRLRQAEAERArQVQVALETAQ--RSAEVELQ 1726
Cdd:COG3096 1133 LHRRELAY----------------LSADELRSMSDKALGALRLAVADNE-HLRDALRLSEdpRRPERKVQ 1185
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1272-1979 |
4.77e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.98 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1272 LEATKAALKKLRAQAEaqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWRERV----AQLLERWQAVLAQT----D 1343
Cdd:COG3096 340 QTALRQQEKIERYQED-----LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslkSQLADYQQALDVQQtraiQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1344 LRQ--RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMV------LADSRAVREQLRQEKALLEEIERHGEKVEEC 1415
Cdd:COG3096 415 YQQavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVleleqkLSVADAARRQFEKAYELVCKIAGEVERSQAW 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1416 QRfAKQYINAIKDYELQLvtykAQLEPVAspakkpkvqsgsesviQEYVDLRTRYS---ELTTLTSQYIKFISETLRRME 1492
Cdd:COG3096 495 QT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRLRqqqNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1493 EEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQ---------EAQELQRRMQEEVArreEAAVDAQQQKR 1563
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlAAQDALERLREQSG---EALADSQEVTA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1564 SIQEELQHLRQSSEAEIQAKARqveaaersRLRIEEEIRvvRLQletterQRGGAE-GELQALRAR-------------- 1628
Cdd:COG3096 631 AMQQLLEREREATVERDELAAR--------KQALESQIE--RLS------QPGGAEdPRLLALAERlggvllseiyddvt 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1629 ---AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DETQRKRQaEAELAVRVKAE---------- 1671
Cdd:COG3096 695 ledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVFDAE-ELEDAVVVKLSdrqwrysrfp 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1672 -----AEAAREKQralqaLEEFRLQAEE-----AERRLRQAEAER---------ARQVQVALETaqrSAEVELQSKRASF 1732
Cdd:COG3096 774 evplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvGGHLAVAFAP---DPEAELAALRQRR 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1733 AEKTAQLERTLQEEHVAVAQLREEAERRA-------QQQAEAERAREEAERELERWQLKANEALR-LRLQAEEVAQ-QKS 1803
Cdd:COG3096 846 SELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELREELDAAQEAQAfIQQHGKALAQlEPL 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1804 LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLAAEQELI-RLRAETEQGEQQRQLLEE 1881
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREARE 1005
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1882 ELARLQHEAAAATQKR--------------QELEAELakvrAEMEVLLAskARAEEESRSTSEKSKQRLEAEASRFRELA 1947
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAEERARIRRDELHEELSQNRSRRSQLE 1079
|
810 820 830
....*....|....*....|....*....|..
gi 2124423178 1948 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1979
Cdd:COG3096 1080 KQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1662-2198 |
7.88e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.12 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1662 AELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEVELQSKRAS--------- 1731
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1732 -FAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAE 1810
Cdd:COG3899 792 aRAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1811 KQKEEAEREARRrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEA 1890
Cdd:COG3899 872 ALAAAAAAAAAA---AALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1891 AAATQKRQELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1970
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1971 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASE 2050
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2051 SELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRR 2130
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2131 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2198
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2305-2507 |
9.52e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2305 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2384
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2385 EEL----------GKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2454
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2455 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQE 2507
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1554-1753 |
2.48e-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: 65.94 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1554 AAVDAQQQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAE 1633
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1634 AQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF---------RLQAEEAERRLRQAEA 1704
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreqaeELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423178 1705 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1753
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1864-2396 |
2.88e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1864 RLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEASRF 1943
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1944 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE---AENERLRRLA 2017
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2018 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILALK-------VSFEKA 2084
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2085 AAGKAELELELGRIRSNA---EDTLRSKEQAELEAMRQRQ----------LAAEEEQRRREAEERVQKSLAAEEEAARQR 2151
Cdd:PRK02224 411 EDFLEELREERDELREREaelEATLRTARERVEEAEALLEagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2152 KAALEE-VERLKAKVEEARRLRERAEQESArqlqLAQDAAQKRLQAEEKAHAfavqqkeqelqqtlqqeqsmLERLRgea 2230
Cdd:PRK02224 491 VEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRER--------------------AEELR--- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2231 eaarRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAA 2310
Cdd:PRK02224 544 ----ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2311 DAEMEKHKKFAEQTLRqKAQVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSLRVQME 2385
Cdd:PRK02224 620 ELNDERRERLAEKRER-KRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVENELEELEELRE 698
|
570
....*....|.
gi 2124423178 2386 ELGKLKARIEA 2396
Cdd:PRK02224 699 RREALENRVEA 709
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1164-1749 |
3.08e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.28 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1164 RECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTLGKL-EQVRSLSAIYLEklktislvi 1242
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL----------EELLAELEAQLEELeEQAAEAVEQRSE--------- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1243 rsthgaeevLKAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpmfdalrdeLRGAQEVGERLQQRHgERDVEV 1321
Cdd:COG3096 583 ---------LRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA----------LADSQEVTAAMQQLL-EREREA 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1322 ERWRERVAQllerwqavlaqtdlRQRELEQLGRQLRYYRESADP--------LGAWL----------QDA----KRRQEQ 1379
Cdd:COG3096 643 TVERDELAA--------------RKQALESQIERLSQPGGAEDPrllalaerLGGVLlseiyddvtlEDApyfsALYGPA 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1380 IQAMVLADSRAVREQLRQEKALLEE---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKP 1450
Cdd:COG3096 709 RHAIVVPDLSAVKEQLAGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1451 KVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAAVEAALEKQRQlAEAHAQAK 1530
Cdd:COG3096 789 ELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQ 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1531 AQAEQEAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLR 1596
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQ 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1597 IEEEIRVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkRQAE 1661
Cdd:COG3096 946 AKEQQRRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ--VLAS 1023
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1662 AELAVRVKAE--AEAARE-KQRALQALEEFRLQAEEaERRLRQAEAERARQVQVALETAQRSAEVELQS--KRASFAEKT 1736
Cdd:COG3096 1024 LKSSRDAKQQtlQELEQElEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERD 1102
|
650
....*....|...
gi 2124423178 1737 AQLERTLQEEHVA 1749
Cdd:COG3096 1103 YKQEREQVVQAKA 1115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1880-2612 |
3.61e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1880 EEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLR---AL 1956
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIErqlAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1957 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAI-----GEATRLKTEaeiaLKEKEAENERLRRLAEDEAFQRRRLEEQA 2031
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEK----IGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2032 AQHKADIEERLAQLRKaSESELERQKglvedtlRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 2111
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEE-LEREIEEER-------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2112 AELEaMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALE-EVERLKAKVEEARRLRER------AEQESARQLQ 2184
Cdd:TIGR02169 397 LKRE-INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQlaadlsKYEQELYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2185 LAQDAAQKRLQA--EEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQ--VEE 2260
Cdd:TIGR02169 476 EEYDRVEKELSKlqRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNnvVVE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2261 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL---------------------------RQKQAADAE 2313
Cdd:TIGR02169 556 DDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIgfavdlvefdpkyepafkyvfgdtlvvEDIEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2314 MEK--------------------HKKFAEQTLRQKAQVEqELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV 2373
Cdd:TIGR02169 636 MGKyrmvtlegelfeksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2374 EEELFSLRVQMEELGKlKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARL-----SVAAQEAARLRELAEEDL 2448
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELeedlhKLEEALNDLEARLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2449 AQQRALAEKMlkEKMQAVQEATRLKAEAELlqQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAE 2528
Cdd:TIGR02169 794 PEIQAELSKL--EEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2529 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQsdhdaerLRQAIAELEREKEK 2608
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA-------LEEELSEIEDPKGE 942
|
....
gi 2124423178 2609 LKQE 2612
Cdd:TIGR02169 943 DEEI 946
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
187-288 |
3.67e-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: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 187 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 256
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 2124423178 257 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 288
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1867-2428 |
4.22e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1867 AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEASRFR 1944
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1945 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIA-----LKEKEAENERLRRLAE 2018
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieerIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2019 DEAFQRRRLEEQAAQHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILALKvsfekaaAGKAELE 2092
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKIT-------ARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2093 LELGRIRSNAEDTLRSK-----------EQAELEAMRQRQLAAEEeqrrreaeerVQKSLAAEEEAARQRKAALEEVERL 2161
Cdd:PRK03918 419 KEIKELKKAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKR----------IEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2162 KAKVEEARRLRERAEQESARQLQLAQDAAQKrlqAEEKAHAF-AVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEA 2240
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2241 eeareraereaaqsrRQVEE--AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHK 2318
Cdd:PRK03918 566 ---------------DELEEelAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2319 KFAEQTLRQKA--QVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLK 2391
Cdd:PRK03918 631 AFEELAETEKRleELRKELEELEKKYSEEEYEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
570 580 590
....*....|....*....|....*....|....*..
gi 2124423178 2392 ARIEAENRALilrdkDNTQRvLQEEAEKMKHVAEEAA 2428
Cdd:PRK03918 711 KELEKLEKAL-----ERVEE-LREKVKKYKALLKERA 741
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1517-1738 |
4.62e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.21 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1517 EKQRQLAEAHAQAKAQAEQEAQELQRRM---QEEVARREEAAVDAQQQKRSIQEELQhlrQSSEAEIQAKARQVEAAERS 1593
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQaaeQERLKQLEKERLAAQEQKKQAEEAAK---QAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1594 RLRieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELAVRVKAEA 1672
Cdd:PRK09510 146 KAK---------------------AEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1673 EAAREKQRALQAleefrlqAEEAErrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1738
Cdd:PRK09510 200 KKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1249-1439 |
5.03e-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: 62.46 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1249 EEVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPMFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1328
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1329 AQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADpLGAWLQDAKRRQEQIQamVLADSRAVREQLRQEKALLEEIERH 1408
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 2124423178 1409 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1439
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1828-2479 |
5.05e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1907
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLAS--------KARAEEESRSTsEKSKQRLEAEASRFRELAEeAARLRALAEEAKRQRQLAEEDAARQRAEAE 1979
Cdd:COG4913 322 REELDELEAQirgnggdrLEQLEREIERL-ERELEERERRRARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1980 RVLAEKLAAigEATRLKTEAEIALKEKEAENERLRR----LAEDEAFQRRRLEEQAAQHKADI----------------- 2038
Cdd:COG4913 400 LEALEEALA--EAEAALRDLRRELRELEAEIASLERrksnIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwr 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2039 -----------------EERLAQLRKASESELERQK---GLVEDTLR--QRRQVEEEILALKVSFEKAAAGkAELELELG 2096
Cdd:COG4913 478 gaiervlggfaltllvpPEHYAAALRWVNRLHLRGRlvyERVRTGLPdpERPRLDPDSLAGKLDFKPHPFR-AWLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2097 R----IRSNAEDTLRSKEQAeleAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEArrlr 2172
Cdd:COG4913 557 RrfdyVCVDSPEELRRHPRA---ITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEA---- 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2173 eraeQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLqqeqsmLERLRGEAEAARRAAEEAEEARERAEREAA 2252
Cdd:COG4913 630 ----EERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE------IAELEAELERLDASSDDLAALEEQLEELEA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2253 QSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVE 2332
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2333 QELTTLRLQLEET-------------DHQKSILD-----EELQRLKAEVTEAARQR------SQVEEELFSLRVQM-EEL 2387
Cdd:COG4913 780 ARLNRAEEELERAmrafnrewpaetaDLDADLESlpeylALLDRLEEDGLPEYEERfkellnENSIEFVADLLSKLrRAI 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2388 GKLKARIEAENRalILRDKD-NTQRVLQEEAEKMKHvaEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAV 2466
Cdd:COG4913 860 REIKERIDPLND--SLKRIPfGPGRYLRLEARPRPD--PEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSE 935
|
730
....*....|...
gi 2124423178 2467 QEATRLKAEAELL 2479
Cdd:COG4913 936 EEESDRRWRARVL 948
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
181-285 |
6.55e-10 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 59.74 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 181 ERDRvQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQI 252
Cdd:cd21300 4 EGER-EARVFTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 2124423178 253 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 285
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1856-2709 |
8.91e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 65.58 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1856 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1935
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1936 LEAEASRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEIAL-KEKEAENERL 2013
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2014 RRL---AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKglvedtlrQRRQVEEEILALKVSFEKAAAGKAE 2090
Cdd:pfam01576 162 SEFtsnLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK--------AKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2091 LELELGRirsnAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAE----EEAARQRKAALEEVERLKAKVE 2166
Cdd:pfam01576 234 LRAQLAK----KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESEraarNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2167 EA-------RRLRERAEQESARqlqlaqdaAQKRLQAEEKAHAFAVQQkeqelqqTLQQEQSMLERLRgeaeaarraaee 2239
Cdd:pfam01576 310 DTldttaaqQELRSKREQEVTE--------LKKALEEETRSHEAQLQE-------MRQKHTQALEELT------------ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2240 aeeareraereaaqsrRQVEEAERLKQSaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalrqkqaadaeMEKHKK 2319
Cdd:pfam01576 363 ----------------EQLEQAKRNKAN----------------------------------------------LEKAKQ 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2320 FAEQtlrQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENR 2399
Cdd:pfam01576 381 ALES---ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2400 ALilrDKD---------NTQRVLQEEAEKMKHVAeeaARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEAT 2470
Cdd:pfam01576 458 KL---SKDvsslesqlqDTQELLQEETRQKLNLS---TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2471 RLKAEAELLqqqkELAQEQARRLQEDKEQMAQQLEQETQGFQR---------------TLEAERQRQL------------ 2523
Cdd:pfam01576 532 KLEEDAGTL----EALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrlqqelddlLVDLDHQRQLvsnlekkqkkfd 607
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2524 EMSAEAERLKLRVA-EMSRAQARAEEDAQRFRKQAEEIGEKL-HRTELATQEKVTL----------------VQTLEIQR 2585
Cdd:pfam01576 608 QMLAEEKAISARYAeERDRAEAEAREKETRALSLARALEEALeAKEELERTNKQLRaemedlvsskddvgknVHELERSK 687
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2586 QQSDHDAERLRQAIAELEREKE-----KLKQEAKLLQLKSE---EMQTVQQEQLLQETQALQQsfLSEKDTLLQRERFIE 2657
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEDELQatedaKLRLEVNMQALKAQferDLQARDEQGEEKRRQLVKQ--VRELEAELEDERKQR 765
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2658 QE----KAKLEQLFQD---EVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREA 2709
Cdd:pfam01576 766 AQavaaKKKLELDLKEleaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI 824
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1488-1704 |
1.01e-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: 64.01 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1488 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1567
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1568 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEae 1644
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE-- 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 1645 rlRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF--RLQAEEAERRLRQAEA 1704
Cdd:COG4942 187 --RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1825-2202 |
1.12e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1904
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELE-AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1905 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE------EDAARQRAEA 1978
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEeeleqlENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1979 ERVLAEKLAAIGEATRLKTEAEIAL------------------------------KEKEAENERLRRLAEDEAFQRRRLE 2028
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSllsliltiagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2029 EQAAQHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEILALKVSFEKAAAGKAElelelgRIRSNAEDTLR 2107
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2108 SKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQL 2185
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQ 476
|
410
....*....|....*..
gi 2124423178 2186 AQDAAQKRLQAEEKAHA 2202
Cdd:COG4717 477 ELEELKAELRELAEEWA 493
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1676-2028 |
1.12e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.76 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1676 REKQRALQALEEFRLQaEEAERRLRqaEAERARQvqvaLETAQRSAEVELQSKRASFAEKtaqlERTLQEEHvavaqlre 1755
Cdd:pfam17380 287 RQQQEKFEKMEQERLR-QEKEEKAR--EVERRRK----LEEAEKARQAEMDRQAAIYAEQ----ERMAMERE-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1756 eaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEQAVRQRE 1835
Cdd:pfam17380 348 --------------------RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1836 LaeQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQ-QRQLLEEELARLQHEAAAATQKRQ-------ELEAELAKV 1907
Cdd:pfam17380 406 I--LEEERQRKIQQ--------QKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLASKARAEEESRSTSEKskqrlEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLAE 1984
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2124423178 1985 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 2028
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1836-2067 |
1.32e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.33 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1836 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAelakvraemevll 1915
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1916 askARAEEESRSTSEKSKQRLEAEASRfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAervlAEKLAaigEATRL 1995
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1996 KTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE----ERLAQLRKASESELERQKGLVEDTLRQR 2067
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1525-1984 |
1.39e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 64.65 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1525 AHAQAKAQAEQEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1604
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1605 RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQA 1684
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1685 LEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQ 1764
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1765 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1844
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1845 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1924
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1925 SRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1984
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1243-1979 |
1.89e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.59 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1243 RSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpmfdaLRDELRGAQEvGERLQQRHGERDVEVE 1322
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1323 RWRERvaqlLERWQAVLAQTDLRQRELEqlgRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVReQLRQEKALL 1402
Cdd:PRK04863 359 ELEER----LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1403 E----EIERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKK-------PKVQSGSESVIQEYVDLRT 1468
Cdd:PRK04863 431 GlpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1469 RYSELTTLTSQYikfisETLRRMEEEERLAEQQRAEERERL-------AAVEAALEKQRQLAEAHAQAKAQA-------E 1534
Cdd:PRK04863 511 LAEQLQQLRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1535 QEAQELQRRMQEEVARREE--AAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTE 1612
Cdd:PRK04863 586 QQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1613 rQRGGAEGE-LQALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QR 1656
Cdd:PRK04863 666 -QPGGSEDPrLNALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDS 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1657 KRQA-----EAELAVRVK-AEAE--------------AAREKQralqaLEEFRLQAEEAERRLRQAEAERaRQVQVALET 1716
Cdd:PRK04863 745 FDDSvfsveELEKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQA 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1717 AQR------------SAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlK 1784
Cdd:PRK04863 819 FSRfigshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA----D 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1785 ANEALRLRLQAEEVAQQkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQ--------------LAE 1849
Cdd:PRK04863 895 RVEEIREQLDEAEEAKR-FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDyQQAQQTQRDAKQqafaltevvqrrahFSY 973
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1850 GTAQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQHEAAAATQKRQELEAELAK--VRAEme 1912
Cdd:PRK04863 974 EDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPAD-- 1051
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1913 vllaskARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1979
Cdd:PRK04863 1052 ------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1824-2067 |
2.19e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.56 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 GKAEEQAVRQRelAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARlQHEAAAATQKRQELEAE 1903
Cdd:TIGR02794 46 GAVAQQANRIQ--QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1904 LAKVRAEMEVLLASKARAEeesRSTSEKSKQRLEAEAsrfreLAEEAARLRALAEEAKRQRqlaeEDAARQRAEAER-VL 1982
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAE---RKAKEEAAKQAEEEA-----KAKAAAEAKKKAEEAKKKA----EAEAKAKAEAEAkAK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1983 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVED 2062
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQ 270
|
....*
gi 2124423178 2063 TLRQR 2067
Cdd:TIGR02794 271 AIQQN 275
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1830-2598 |
2.28e-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: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1830 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEAAAATQK----RQ 1898
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1899 ELEAELAKVRAEMEVLLASkaraeEESRSTSEKSKQRLEAEASRFR-ELAE-----EAARLRALA--------EEAKRQR 1964
Cdd:COG3096 355 DLEELTERLEEQEEVVEEA-----AEQLAEAEARLEAAEEEVDSLKsQLADyqqalDVQQTRAIQyqqavqalEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1965 QL-------AEEDAARQRAEAERVLAEKLAAigeATRLkTEAEIALKEKEAENERLRRLAED----EAFQR-RRLEEQAA 2032
Cdd:COG3096 430 GLpdltpenAEDYLAAFRAKEQQATEEVLEL---EQKL-SVADAARRQFEKAYELVCKIAGEversQAWQTaRELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2033 QHKAdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEILALKVSFEKAAAGKAELELelgrirsnaedtlrskEQA 2112
Cdd:COG3096 506 SQQA-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEE----------------LLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2113 ELEAMRQRqlaaeeeqrrreaeervqksLAAEEEAARQRKAALE-EVERLKAKVEEarrLRERAEQESARQLQLAQDAAQ 2191
Cdd:COG3096 561 ELEAQLEE--------------------LEEQAAEAVEQRSELRqQLEQLRARIKE---LAARAPAWLAAQDALERLREQ 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2192 krlQAEEKAHAFAVQQkeqelqqtlqQEQSMLERLRGeaeaarraaeeaeeaRERAEREAAQSRRQVE-EAERLKQSAEE 2270
Cdd:COG3096 618 ---SGEALADSQEVTA----------AMQQLLERERE---------------ATVERDELAARKQALEsQIERLSQPGGA 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2271 QAQAQAQAQAAAE------------------------KLRKEAEQEAARRAQAEQAAL-----------RQKQAADA--- 2312
Cdd:COG3096 670 EDPRLLALAERLGgvllseiyddvtledapyfsalygPARHAIVVPDLSAVKEQLAGLedcpedlylieGDPDSFDDsvf 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2313 ---EMEK------------HKKFAEQTLRQKAQVEQELTTLRLQLEETD---HQKSILDEELQRL--------------- 2359
Cdd:COG3096 750 daeELEDavvvklsdrqwrYSRFPEVPLFGRAAREKRLEELRAERDELAeqyAKASFDVQKLQRLhqafsqfvgghlava 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2360 -----KAEVTEAARQRSQVEEELFSLRVQM----EELGKLKARIEAENRAL----ILRDKDNTQRVlqEEAEKMKHVAEE 2426
Cdd:COG3096 830 fapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETLADRL--EELREELDAAQE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2427 AAR-----------------------LSVAAQEAARLRELAEEDLAQQRALAekmLKEKMQ-----AVQEATRLKAEA-- 2476
Cdd:COG3096 908 AQAfiqqhgkalaqleplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFA---LSEVVQrrphfSYEDAVGLLGENsd 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2477 --ELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQrTLEAERQRQLEMSAEAERlklRVAEMS-RAQARAEEDAQRF 2553
Cdd:COG3096 985 lnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELEELGvQADAEAEERARIR 1060
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 2124423178 2554 RKqaeEIGEKLHRTElatQEKVTLVQTLEIQRQQSDHDAERLRQA 2598
Cdd:COG3096 1061 RD---ELHEELSQNR---SRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1472-1687 |
2.61e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 62.97 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1472 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAAVEAAlEKQRQLAEAHAQAKAQ------AEQEAqEL 1540
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREietariAEAEA-EL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1541 QRRMQEEVARREEAAVDAQQQKRsIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLETTERQRggAEG 1620
Cdd:COG2268 247 AKKKAEERREAETARAEAEAAYE-IAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKP--AEA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1621 ELQALRARAEeAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEE 1687
Cdd:COG2268 317 EKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK 382
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
669-858 |
2.64e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.54 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 669 LRYLQDLLAWVEENQRRVDGAEWGVDLPSVEAQLGSHRGLHHSIEEFRAKIERARTDEGQLSPATRGAY---RDCLGRLD 745
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 746 LQYAKLLNSSKGRLRSLE---SLYSFVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEI 822
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2124423178 823 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 858
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1860-2709 |
2.72e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1860 QELIRLRAETEQGEQQRQLLEE-----------ELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1928
Cdd:TIGR02169 198 QQLERLRREREKAERYQALLKEkreyegyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1929 SEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAaigEATRLKTEAEIALKEKEA 2008
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2009 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE---SELERQKGLVEDTLRQRRQVEEEILALKVSFEKAA 2085
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2086 AGKAELELEL-----------GRIRSNAEDtlRSKEQAELEAMRQRQlaaeeeqrrrEAEERVQKSLAAEEEAARQRKAA 2154
Cdd:TIGR02169 434 AKINELEEEKedkaleikkqeWKLEQLAAD--LSKYEQELYDLKEEY----------DRVEKELSKLQRELAEAEAQARA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2155 LEEVERLKAKVEEARRLRERAEQESARQL-------QLA-QDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLErL 2226
Cdd:TIGR02169 502 SEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryATAiEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLP-L 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2227 RGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRkeaeqeaarRAQAEQAALRQ 2306
Cdd:TIGR02169 581 NKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYR---------MVTLEGELFEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2307 KQAADAEMEKHKKFAEQTLRQKAQVEQelttLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEE 2386
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQR----LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2387 LGKlKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLsvaaqeaarlrelaEEDLAQ-QRALAEKMLKEKMQA 2465
Cdd:TIGR02169 728 LEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL--------------EEDLHKlEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2466 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2545
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2546 AEEDAQRFRKQAEEIGEKlhRTELATQEKVtlvqtLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2625
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKE--RDELEAQLRE-----LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2626 VQQEQllqetqalqqsfLSEKDTLLQRERfIEQEKAKLEQ---LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEA 2702
Cdd:TIGR02169 946 IPEEE------------LSLEDVQAELQR-VEEEIRALEPvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 2124423178 2703 RQRQREA 2709
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4534-4572 |
2.78e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.03 E-value: 2.78e-09
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 4534 FLEVQYLTGGLIEPDVPGRVPLDEALQRGTVDARTAQKL 4572
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2311-2842 |
3.05e-09 |
|
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: 63.83 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2311 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSLRVQMEELGKL 2390
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2391 KARIEAENRALILRDKdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELA----------EEDLAQQRALAEKMLK 2460
Cdd:TIGR00618 276 EAVLEETQERINRARK---AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkraahvkqQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2461 EKMQAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLEQETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMS 2540
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK------ELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2541 RAQARAEEDAQRFRKQAEEigekLHRTELATQEKVTLVQTLEIQrQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKS 2620
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2621 EEmQTVQQEQLLQETQALQQSFLSEKDT-LLQRerfIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVAsM 2699
Cdd:TIGR00618 501 EE-PCPLCGSCIHPNPARQDIDNPGPLTrRMQR---GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI-L 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2700 EEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALaHSEEIAASQATAVKALpngrda 2779
Cdd:TIGR00618 576 TQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL-HLQQCSQELALKLTAL------ 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2780 pdgpateaepehafdglrqkvpaqrlqevgilsTEELQRLVQGRTTVAELAQREDVRRYLQGR 2842
Cdd:TIGR00618 649 ---------------------------------HALQLTLTQERVREHALSIRVLPKELLASR 678
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1498-1696 |
3.35e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.52 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1498 AEQQRAEE-RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREeaavdAQQQKrsiQEELQHLRQSS 1576
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1577 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1656
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2124423178 1657 KRQAEAELAV-RVKAEAEAAREKQRALQALEEFRLQAEEAE 1696
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
306-408 |
3.83e-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: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 306 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 2124423178 385 PEDVDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4456-4493 |
4.75e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 4.75e-09
10 20 30
....*....|....*....|....*....|....*...
gi 2124423178 4456 QRLLEAQACTGGIIDPNTGERFPVTDAVNKGLVDKIMV 4493
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1581-1802 |
4.75e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1581 QAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQA 1660
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1661 EAELAVRVKAEAEAAREKQRA-LQALEEFRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1738
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1739 LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQK 1802
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1637-2157 |
5.04e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1637 RQAQEEAERLRRQVQ-----DETQRKRQAEAELAVRVKAEAEAAR--EKQRALQALEEfRLQAEEAERRLRQAEAERARQ 1709
Cdd:COG4913 238 ERAHEALEDAREQIEllepiRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEA-ELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1710 VQVALETAQRSAEVELQSkrasfaEKTAQLERtLQEEhvavaqlreeaerraqqqaeaerareeaereLERWQLKANEAL 1789
Cdd:COG4913 317 RLDALREELDELEAQIRG------NGGDRLEQ-LERE-------------------------------IERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1790 RLRLQAEEVAQQKSLAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1869
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1870 EQGEQQRQLLEEELARLQHEAAAATQ-KRQELE--AELAKVRAE-------MEVLLASKAR------------------- 1920
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrl 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1921 ---------------AEEESRSTSEKS-KQRLEAEASRFR-----ELAEEAARLRALAEEA------------------- 1960
Cdd:COG4913 509 hlrgrlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgngt 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1961 ----KRQRQLAEE-----DAARQRAEAERVLAEKLAAIGEATRLKTEAEialKEKEAENERLRRLAEDEAFQRRRLEEQA 2031
Cdd:COG4913 589 rhekDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALE---AELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2032 AQHK-ADIEERLAQLRKAS------ESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAED 2104
Cdd:COG4913 666 AEREiAELEAELERLDASSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2105 TLRskeqAELEAMRQRQLaaeeeqrRREAEERVQKSLAAEEEAARQRKAALEE 2157
Cdd:COG4913 746 ELR----ALLEERFAAAL-------GDAVERELRENLEERIDALRARLNRAEE 787
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1488-2102 |
5.14e-09 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 62.90 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1488 LRRMEEEERLAEQQRAEERERLAAVEAA-----LEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQK 1562
Cdd:PRK10246 259 ASRRQQALQQALAAEEKAQPQLAALSLAqparqLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1563 RSIQEELQHLRQSseaeiqakarqveAAERSRLRIEEEirvvrlqletterqrggaegELQALRARAEEAEAQKRQAQEE 1642
Cdd:PRK10246 339 AELQAQQQSLNTW-------------LAEHDRFRQWNN--------------------ELAGWRAQFSQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1643 AERLrrqvqDETQRKRQAEAELAVRVKA-EAEAAREKQRALQALEE--FRLQAEEAERRLRQAEAERARQvqvALETAQR 1719
Cdd:PRK10246 386 QQQL-----THAEQKLNALPAITLTLTAdEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVAIQ---NVTQEQT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1720 SAEVELQSKRASFAEKTAQLE--RTLQEEHVAVAQLrEEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEE 1797
Cdd:PRK10246 458 QRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDL-EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1798 vaQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1877
Cdd:PRK10246 537 --KEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLR 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1878 LLEEELArLQHEAAAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAEASRFRELAEEAA 1951
Cdd:PRK10246 614 LLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQRQNELTALQNRIQ 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1952 RLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAIGEATrLKTEAEIALKEKEAENERlRRLAE-----DEAFQRRR 2026
Cdd:PRK10246 693 QLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKaqaqfDTALQASV 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2027 LEEQAAQHKADIEE----RLAQLRKASESELERQKGLVEdtlrQRRQVEEEILALKVSFEKAAAGKAELELEL----GRI 2098
Cdd:PRK10246 763 FDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQIQQELaqlaQQL 838
|
....
gi 2124423178 2099 RSNA 2102
Cdd:PRK10246 839 RENT 842
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
301-403 |
6.64e-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: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 301 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 379
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 2124423178 380 TRLLDPEDVDVPQPDEKSIITYVS 403
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1486-1708 |
6.90e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.01 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQRAEERERLAAVE--AALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQqkr 1563
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1564 siQEELQHlrqssEAEIQAKARQVEAAERSRlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEE- 1642
Cdd:TIGR02794 145 --KEEAAK-----QAEEEAKAKAAAEAKKKA-----------------------EEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1643 ---AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAR 1708
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1599-2036 |
7.02e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1599 EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DETQRKRQAEAELAvrvkaeaeaar 1676
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELA----------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1677 EKQRALQALEEFRLQAEEAERRLRQAEAErarqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREE 1756
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAE--------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1757 AERRAQQQAEAERAREEAERELERWQLKA--NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1834
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEErlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1835 ELAEQELEKQRQLAEGTAQQRLaAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME-- 1912
Cdd:COG4717 295 REKASLGKEAEELQALPALEEL-EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEia 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1913 -VLLASKARAEEESRSTSEKSKQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQR-AEAERVLAEKLAAIG 1990
Cdd:COG4717 374 aLLAEAGVEDEEELRAALEQAEEYQELKE----ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2124423178 1991 EATRLKTEAEIALKEKEaENERLRRLAEDEAFQRRRLEEQAAQHKA 2036
Cdd:COG4717 450 ELREELAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2024-2751 |
7.13e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 62.68 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2024 RRRLEEQAA--QHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSN 2101
Cdd:pfam02463 155 RLEIEEEAAgsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2102 AEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2181
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2182 QLQLAQD---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLE-RLRGEAEAARRAAEEAEEARERAEREAAQSRRQ 2257
Cdd:pfam02463 315 KLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEElEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2258 VEEAERLKQSAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqaalrqKQAADAEMEKHKKFAEQTLRQKAQVEQELTT 2337
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEE-------------------KKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2338 LRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEA 2417
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQ----LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2418 EKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAvqeaTRLKAEAELLQQQKELAQEQARRLQEDK 2497
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK----LRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2498 EQMAQQLEQETQGFQRTLEAERQRQLEMSaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL 2577
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2578 VQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQalQQSFLSEKDTLLQRERFIE 2657
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ--KIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2658 QEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGvrrkqEELQLLEQQRQQQEKLLAEE 2737
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL-----EEEQLLIEQEEKIKEEELEE 837
|
730
....*....|....
gi 2124423178 2738 NQRLRERLQRLEEE 2751
Cdd:pfam02463 838 LALELKEEQKLEKL 851
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1623-2148 |
7.42e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 62.57 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1623 QALRARA-EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREkqRALQALEEFRLQAEEAERR--- 1698
Cdd:COG3899 714 RALARGAyAEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLE--RALAARALAALAALRHGNPpas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1699 ----------LRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAE 1768
Cdd:COG3899 792 arayanlgllLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1769 RAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1848
Cdd:COG3899 872 ALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAA 951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1849 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSt 1928
Cdd:COG3899 952 AALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAA- 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1929 sekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA 2008
Cdd:COG3899 1031 ------AAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAA 1104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2009 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGK 2088
Cdd:COG3899 1105 LALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLA 1184
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2089 AELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2148
Cdd:COG3899 1185 AAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1800-1995 |
7.85e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1800 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1879
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1880 EEELARLQHEAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEE 1959
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 2124423178 1960 AKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1995
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1409-2198 |
8.27e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.37 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1409 GEKVEECQ---RFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFis 1485
Cdd:TIGR00606 199 GQKVQEHQmelKYLKQYKEKACEIRDQITSKEAQLE---------SSREIVKSYENELDPLKNRLKEIEHNLSKIMKL-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 etlrrmeEEERLAEQQRAEERERLaaveaalekQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1565
Cdd:TIGR00606 268 -------DNEIKALKSRKKQMEKD---------NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1566 QEELQHLRQSS---EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRG----------------GAEGELQALR 1626
Cdd:TIGR00606 332 NKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfhtlvieRQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1627 ARAEEAEAQKRQAQEEAERLR-------RQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRlqaeEAERRL 1699
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRdekkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR----KAEREL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1700 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER---------TLQEEHVAVAQLREEAERRAQQQAEAERA 1770
Cdd:TIGR00606 488 SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqmeMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1771 REEAERELERWQLKANEAL-----RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRElaEQELEKQR 1845
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEInqtrdRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE--ESDLERLK 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1846 QLAEGTAQQR--LAAEQELIRLRAETEQGEQQ------------RQLLEEELARLQHEAAAATQKRQELEAELAKVRAEM 1911
Cdd:TIGR00606 646 EEIEKSSKQRamLAGATAVYSQFITQLTDENQsccpvcqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1912 EVLLA-SKARAEEESRSTSEKSKQRleaeaSRFRELAEEAARLRALAEEAKRQRQ--LAEEDAAR--------------Q 1974
Cdd:TIGR00606 726 DEMLGlAPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKvcltdvtimerfqmE 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1975 RAEAERVLAEKLAAIGEATRLKTEAEIAlKEKEAENERLRRLAEDEAFQRRRLEEQAAQ-------------HKADIEER 2041
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQiqhlksktnelksEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2042 LAQlRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELelelgrirSNAEDTLRSKEQAELEAMRQR- 2120
Cdd:TIGR00606 880 LQR-RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL--------ISSKETSNKKAQDKVNDIKEKv 950
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2121 -QLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2198
Cdd:TIGR00606 951 kNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE 1029
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1503-1723 |
8.44e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.43 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1503 AEERERLAAVEAALEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAvdAQQQKRSIQEELQhlRQSSEAEIQ 1581
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIAE--AEAELAKKKAEER--REAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1582 AKARQVEAAERSRlrieeeiRVVRLQLETTERQRggaEGELQalraraeEAEAQKRQAQEEAErlrrqvqdetqrkrqae 1661
Cdd:COG2268 264 AEAAYEIAEANAE-------REVQRQLEIAERER---EIELQ-------EKEAEREEAELEAD----------------- 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 1662 aelaVRVKAEAEAAREKQRALQALEEFRLQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1723
Cdd:COG2268 310 ----VRKPAEAEKQAAEAEAEAEAEAIRAKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
310-405 |
1.12e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.54 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 310 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 365
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 366 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 405
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1825-2032 |
1.26e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAel 1904
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1905 akvRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1983
Cdd:COG4942 119 ---QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423178 1984 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 2032
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1998-2447 |
1.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1998 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASEselerqkglVEDTLRQRRQVEEEILAL 2077
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2078 KVSFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEqrrreaeerVQKSLAAEEEAARQRKAALEE 2157
Cdd:COG4717 145 PERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEE---------LQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2158 VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAA 2237
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2238 EEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlRQKQAADAEMEKH 2317
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2318 KKFA------EQTLRQKAQVEQELTTLRLQLEETDHQ-KSILDEELQRLKAEVTEAARQR-SQVEEELFSLRVQMEELGK 2389
Cdd:COG4717 374 ALLAeagvedEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2390 LKARIEAENRALILRDK-DNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEED 2447
Cdd:COG4717 454 ELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1559-2103 |
1.39e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 61.20 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--TTERQRGGAEGELQALRARaeeaEAQK 1636
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1637 RQAQEEAERLRRQVQDETQRKRQAEAELAVrVKAE--------AEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAr 1708
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1709 QVQVALETAqRSAEVELQSKRASFA----EKTAQLERTLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLK 1784
Cdd:pfam05701 191 ATKESLESA-HAAHLEAEEHRIGAAlareQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1785 ANEALRLRLQAEEVAQQKSlaqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQE 1861
Cdd:pfam05701 254 TASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1862 LIRLRAETEQGEQQRQllEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeas 1941
Cdd:pfam05701 318 CLRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1942 rfrelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA--ENERLRRLAED 2019
Cdd:pfam05701 390 -----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2020 EAFQR-------------RRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKVSFEKAAA 2086
Cdd:pfam05701 465 EDSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKE 543
|
570
....*....|....*..
gi 2124423178 2087 GKAELELELGRIRSNAE 2103
Cdd:pfam05701 544 GKLAAEQELRKWRAEHE 560
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1489-1750 |
1.45e-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: 60.44 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1489 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQ 1566
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1567 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqletterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1646
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1647 RRQVQDETQR-KRQA-EAELAVRVKAEAEAARE--KQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1722
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 2124423178 1723 VELQSKRASFAEKTAQLERTLQEEHVAV 1750
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
301-408 |
1.66e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 301 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 379
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 2124423178 380 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1194-1687 |
1.70e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1194 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEaqaVPATLPELE 1273
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1274 ATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERL----QQRHG--ERDVEVERWRERVAQL------LERWQAVLAQ 1341
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLsrleEEINGieERIKELEEKEERLEELkkklkeLEKRLEELEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1342 TDLRQRELEQLGRQLRYYR-----ESADPLGAWLQDAKRRQEQIQ---AMVLADSRAVREQLRQEKALLEEIERHGEKVE 1413
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKkrltgLTPEKLEKELEELEKAKEEIEeeiSKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1414 ECQR---------FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTRYSELTTLTSQYIKFI 1484
Cdd:PRK03918 440 VCGRelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES---ELIKLKELAEQLKELEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1485 SETLRRMEEE-----ERLAE---QQRAEERE---------RLAAVEAAL-EKQRQLAEAHAQAKAQAEQEAQELQRRMQ- 1545
Cdd:PRK03918 517 LEELEKKAEEyeklkEKLIKlkgEIKSLKKElekleelkkKLAELEKKLdELEEELAELLKELEELGFESVEELEERLKe 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1546 -EEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEE------EIRVVRLQLETTERQRgga 1618
Cdd:PRK03918 597 lEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkysEEEYEELREEYLELSR--- 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1619 egELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELAVRVKAEAEAAREKQRALQALEE 1687
Cdd:PRK03918 674 --ELAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1894-2045 |
1.72e-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: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1894 TQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEASRFRELAEEAARLRAlaEEAKRQRQLAEEDAAR 1973
Cdd:COG2268 215 AIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEIAER 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1974 QR------AEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 2045
Cdd:COG2268 289 EReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKL 366
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1825-2045 |
2.37e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEkQRQLAEgtaQQRLAA-EQELIRLRAETEQGEQQRQLLEEElarlQHEAAAATQKrqELEAE 1903
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQ-QKQAAE---QERLKQlEKERLAAQEQKKQAEEAAKQAALK----QKQAEEAAAK--AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1904 LAKVRAEMEVLLASKARAEEESrstseksKQRLEAEAsrfRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVlA 1983
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEA-------KKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-A 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 1984 EKLAAIGEATRLKTEAEIALKEKEAEnerlrrlAEDEAFQRRRLEEQAAQHKADIEERLAQL 2045
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAA-------AEKAAAAKAAEKAAAAKAAAEVDDLFGGL 266
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1643-2099 |
2.46e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1643 AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQAleefRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1722
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1723 VELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1802
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1803 SLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1882
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1883 LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKR 1962
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1963 QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERL 2042
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2043 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIR 2099
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1506-1975 |
2.52e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1506 RERLAAVEAALEKQRQLAEAHAqakAQAEQEAQELQRRMQEEVARREEAAVDaqqqkrSIQEELQHLRQSSEAEIqakAR 1585
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYL---ALAERAAAELRGPDQLAWLARLDAEHD------NLRAALRWALAHGDAEL---AL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1586 QVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1665
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1666 VRvkAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1745
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1746 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1825
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1826 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1905
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1906 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1975
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2314-2617 |
2.69e-08 |
|
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: 60.42 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2314 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKAR 2393
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2394 IEAENRAL------ILRDKDNTQRVLQEEAEKMKHVAEEAarlsvaaqeaarlRELAEE--DLAQQRALaekmLKEKMQa 2465
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2466 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaerqrqlemsaeaeRLKLRVAEMSRAQAR 2545
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 2546 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQ 2617
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1375-1753 |
3.45e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1375 RRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQS 1454
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1455 GSESVIQEYVDLRTRYSELTTLtsqyikfiSETLRRMEEEERLAEQQRAEERERL-AAVEAALEKQRQLAEAHAQAKAQA 1533
Cdd:COG4717 140 ELAELPERLEELEERLEELREL--------EEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1534 EQEAQELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAE---------------------------------- 1579
Cdd:COG4717 212 EEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllall 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1580 --IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQR 1656
Cdd:COG4717 290 flLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLeLLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1657 KRQAEAELAVRVKAEaEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT 1736
Cdd:COG4717 370 QEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410
....*....|....*..
gi 2124423178 1737 AQLERTLQEEHVAVAQL 1753
Cdd:COG4717 449 EELREELAELEAELEQL 465
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1308-1615 |
3.75e-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: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1308 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdlRQRELEqlgRQLRYYRESAdplgawlQDAKRRQEQIQAMVLAD 1387
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1388 SRAVREQLRQEKALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1460
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1461 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEaalEKQRQLAEAHAQAKAQAEQEAQEL 1540
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1541 QRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVeAAERSRLRIEEEIRVVRLQLETTERQR 1615
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2354-2764 |
4.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2354 EELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAL-ILRDKDNTQRVLQEEAEKMKHVAEEAARLSV 2432
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2433 AAQEAARLRELAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQ 2512
Cdd:COG4717 161 LEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2513 RTLEAERQRQLEMSAE----------------------AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2570
Cdd:COG4717 238 AAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2571 TQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQtvqqeqllqETQALQQSFLSEKDTLL 2650
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---------IAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2651 QRERFIEQEKAKLEQLfqdEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVrrkqeelqlleqqrqqq 2730
Cdd:COG4717 389 AALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL----------------- 448
|
410 420 430
....*....|....*....|....*....|....
gi 2124423178 2731 ekllaeenQRLRERLQRLEEEHRaALAHSEEIAA 2764
Cdd:COG4717 449 --------EELREELAELEAELE-QLEEDGELAE 473
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1673-2116 |
4.68e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1673 EAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQ 1752
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1753 LreeaerraqqqaeaERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAeaekqkeeaerearrrgKAEEQAVR 1832
Cdd:COG4717 151 L--------------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-----------------EELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1833 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME 1912
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1913 VLLASKARAeeeSRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1992
Cdd:COG4717 280 FLVLGLLAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1993 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR-RQ 2069
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEE 436
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2124423178 2070 VEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEA 2116
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKA 483
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2395-2622 |
4.83e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2395 EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLS-----VAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEA 2469
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2470 TRLKAEAELLQQQK-ELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2548
Cdd:COG4913 319 DALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 2549 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAE-LEREKEKLKQEAKLLQLKSEE 2622
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1295-2120 |
5.84e-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: 59.58 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1295 ALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAV-----LAQTDLRQREleQLGRqlryYRESADPLGAW 1369
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1370 LQdakrrqeqIQAMVLADSRAVREQLRQEKALLE-EIERHG-------EKVEECQRFAKQYINAIKDYE-LQLVTYKAQL 1440
Cdd:COG3096 363 LE--------EQEEVVEEAAEQLAEAEARLEAAEeEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1441 EPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEERER-------LAAV 1512
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1513 EAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER 1592
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1593 -SRLRIEEEI-RVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDETQRKRQAEAELAVR 1667
Cdd:COG3096 594 iKELAARAPAwLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELaarKQALESQIERLSQPGGAEDPR 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1668 VKAEAE---------------------------------------AAREKQRAL--------------QALEEFRLQAEE 1694
Cdd:COG3096 674 LLALAErlggvllseiyddvtledapyfsalygparhaivvpdlsAVKEQLAGLedcpedlyliegdpDSFDDSVFDAEE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1695 AERRL------RQAEAER----------ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE---EHVAVAqlre 1755
Cdd:COG3096 754 LEDAVvvklsdRQWRYSRfpevplfgraAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgGHLAVA---- 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1756 eaerRAQQQAEAERAREEAERELERWQLKANEAL-RLRLQAEEVAQQKSLAQAEAEKQKEEaerearrrgkAEEQAVRQR 1834
Cdd:COG3096 830 ----FAPDPEAELAALRQRRSELERELAQHRAQEqQLRQQLDQLKEQLQLLNKLLPQANLL----------ADETLADRL 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1835 ELAEQELEKQRQLAEGTAQQRLAAEQ---ELIRLRAETEQGEQQRQLLEEELARLQheaaaatQKRQELEAeLAKVRAEM 1911
Cdd:COG3096 896 EELREELDAAQEAQAFIQQHGKALAQlepLVAVLQSDPEQFEQLQADYLQAKEQQR-------RLKQQIFA-LSEVVQRR 967
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1912 EVLLASKARAE-EESRSTSEKSKQRLEAeasrfrelaeeaarlralAEEAKRQRQLAEEDAARQRAEAERVLAEklaaig 1990
Cdd:COG3096 968 PHFSYEDAVGLlGENSDLNEKLRARLEQ------------------AEEARREAREQLRQAQAQYSQYNQVLAS------ 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1991 eatrLKTEAEIA---LKEKEAENERLRRLAEDEAfqrrrlEEQAAQHKADIEERLAQLRkASESELERQKGLVE---DTL 2064
Cdd:COG3096 1024 ----LKSSRDAKqqtLQELEQELEELGVQADAEA------EERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSL 1092
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2065 RQR-RQVEEEILALKVSFEKAAAGKAELeLELGRiRSNAEDTLRSKEQAELEAMRQR 2120
Cdd:COG3096 1093 QKRlRKAERDYKQEREQVVQAKAGWCAV-LRLAR-DNDVERRLHRRELAYLSADELR 1147
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
186-290 |
5.99e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 54.04 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 186 QKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHR 260
Cdd:cd21299 5 EERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQL 77
|
90 100 110
....*....|....*....|....*....|
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILH 290
Cdd:cd21299 78 KFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1485-2200 |
6.40e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1485 SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKaQAEQEAQELQRRMQEEVARREEAAVDAQQQKRS 1564
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLPDLTADNAEDWLEEFQAKEQE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1565 IQEELQHLRQS-SEAeiQAKARQVEAAERSRLRIEEEI------RVVRLQLETTERQRGGAEgELQALRARAEEAEaQKR 1637
Cdd:PRK04863 454 ATEELLSLEQKlSVA--QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAE-QLQQLRMRLSELE-QRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1638 QAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREkqRALQALEEFRLQAEEAERRLRQAEAERARQvqvaleTA 1717
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELE-QLQEELEARLE--SLSESVSEARERRMALRQQLEQLQARIQRL------AA 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1718 QRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW-QLKANEALRLRLQAE 1796
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLsQPGGSEDPRLNALAE 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1797 EV--------------------------AQQ----KSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1846
Cdd:PRK04863 681 RFggvllseiyddvsledapyfsalygpARHaivvPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVV 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1847 LAEGTAQQRLAAEQELIRL-RAETEQGEQQRQLLEEELARLQHEAAAATQKRQEL--------------------EAELA 1905
Cdd:PRK04863 761 VKIADRQWRYSRFPEVPLFgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLhqafsrfigshlavafeadpEAELR 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1906 KVRA---EMEVLLASKARAEEESRSTSEKSKQR---LEAEASRFRELAEE--AARLRALAEEAKRQRQlAEEDAARQRAE 1977
Cdd:PRK04863 841 QLNRrrvELERALADHESQEQQQRSQLEQAKEGlsaLNRLLPRLNLLADEtlADRVEEIREQLDEAEE-AKRFVQQHGNA 919
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1978 AERVlaEKLAAI-----GEATRLKTEAEIALKEKEAENERLRRLAedEAFQRRR--LEEQAAQ---HKADIEERLAQLRK 2047
Cdd:PRK04863 920 LAQL--EPIVSVlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALT--EVVQRRAhfSYEDAAEmlaKNSDLNEKLRQRLE 995
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2048 ASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELG----RIRSNAEDTLRSKE---QAELEAMRQR 2120
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAEERARARRdelHARLSANRSR 1075
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2121 QlaaeeeqrrreaeERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQD-AAQKRLQAEEK 2199
Cdd:PRK04863 1076 R-------------NQLEKQLTFCEAEMDNLTKKLRKLER---DYHEMREQVVNAKAGWCAVLRLVKDnGVERRLHRREL 1139
|
.
gi 2124423178 2200 A 2200
Cdd:PRK04863 1140 A 1140
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2427-2624 |
6.81e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2427 AARLSVAAQEAARLREL------AEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2500
Cdd:COG4942 16 AAQADAAAEAEAELEQLqqeiaeLEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2501 AQQLEQetqgfQRTLEAERQRQLEMSAEAERLKL-----------RVAEMSRAQARA-EEDAQRFRKQAEEIGEKLHRTE 2568
Cdd:COG4942 96 RAELEA-----QKEELAELLRALYRLGRQPPLALllspedfldavRRLQYLKYLAPArREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2569 LATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQ 2624
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1301-1726 |
7.02e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1301 RGAQEvgERLQQRHGERDVEVERWRERVA--QLLERW--------------------QAVLAQTDLR----QRELEQLGR 1354
Cdd:PRK04863 781 RAARE--KRIEQLRAEREELAERYATLSFdvQKLQRLhqafsrfigshlavafeadpEAELRQLNRRrvelERALADHES 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1355 QLRYYRESADPLGAWLQDAkrRQEQIQAMVLADsravrEQLRQEkalLEEIERHGEKVEECQRFAKQYINAIkdyelqlv 1434
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSAL--NRLLPRLNLLAD-----ETLADR---VEEIREQLDEAEEAKRFVQQHGNAL-------- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1435 tykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAeereR 1508
Cdd:PRK04863 921 ---AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLNEKLRQ----R 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1509 LAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHL--RQSSEAEIQAKARq 1586
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA-----------KRQMLQELKQELQDLgvPADSGAEERARAR- 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1587 veaaersRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDETQRKRQ 1659
Cdd:PRK04863 1062 -------RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRLVKDNGVERRL 1134
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1660 AEAELAVRVKAEAEAAREKqrALQALeefrlqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1726
Cdd:PRK04863 1135 HRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
180-291 |
7.37e-08 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 53.75 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 180 DERDRVQ--KKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIA 253
Cdd:cd21222 9 EAPEKLAevKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLA 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 2124423178 254 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21222 84 LELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1514-1746 |
7.94e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1514 AALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLR--QSSEAEIQAKARQVEAA 1590
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEArAAKDKDAVAAALARVKakKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1591 ERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKA 1670
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1671 EAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1746
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4187-4223 |
8.35e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 8.35e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 4187 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4223
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1527-1741 |
8.64e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1527 AQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRvvrl 1606
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1607 qletterqrggaegelQALRARAEEAEAQKRQAQEEAERlrrQVQDETQRKRQAEAelavRVKAEAEAAREKQRALQALE 1686
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1687 EFRLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1741
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1834-2206 |
8.78e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1834 RELAEQELEKQR-QLAEGTAQQRLAAEQELIRLRAETEQGEQQrqllEEELARLQHEAAAATQKRQELEAELAKVRAEME 1912
Cdd:COG4717 44 RAMLLERLEKEAdELFKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1913 VLlaSKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1992
Cdd:COG4717 120 KL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1993 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqhKADIEERLAQLRKASESELERQkGLVEDTLRQRRQVEE 2072
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARLLLLIAAALL-ALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2073 EILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK 2152
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2153 AALEEVERLKAKVEEARR--LRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQ 2206
Cdd:COG4717 355 EAEELEEELQLEELEQEIaaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2463-2608 |
9.45e-08 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 58.88 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2463 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLEQetQGFQRTLEAERQRQLEMSAEAERLK 2533
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2534 LRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlRQAIAELEREKEK 2608
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1917-2188 |
9.74e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1917 SKARAEEESRSTSEKSKQRLEAEASRF-RELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1995
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREARHKK-AAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1996 KTEAEIALKEKEAENERLRRLAEDEAfqrrrleEQAAQHKADIEERL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 2073
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAA-------AAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2074 ILALKVsfEKAAAGKAELELElgrIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKA 2153
Cdd:PRK05035 586 IARAKA--KKAAQQAASAEPE---EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423178 2154 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQD 2188
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1974-2337 |
1.06e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1974 QRAEAERVLAEKLAAIgEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasESEL 2053
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2054 ERQKglVEDTLRQRRQVEEEILALKVSFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAMRQRQLAAEEEQRRRE 2132
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2133 AEERVQKSLAAEEEAARQRKAALEEVERLKakveEARRLRERaEQESARQLQ-LAQDAAQKRLQAEEKAHAfAVQQKEQE 2211
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAR----EMERVRLE-EQERQQQVErLRQQEEERKRKKLELEKE-KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2212 LQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklRKEAEQ 2291
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER----------------------RKQQEM 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2124423178 2292 EAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLR-QKAQVEQELTT 2337
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVEsEKARAEYEATT 595
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1837-2052 |
1.10e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1837 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1916
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1917 SKARAEE---------ESRSTSE--KSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1985
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1986 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESE 2052
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1486-1722 |
1.22e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.24 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1565
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1566 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1645
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1646 LRrqvqdetqRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1722
Cdd:pfam13868 206 LR--------AKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE 274
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1873-2064 |
1.26e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1873 EQQRQLLEEELAR-LQHEAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEASRFR----ELA 1947
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1948 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 2026
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 2124423178 2027 LEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTL 2064
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
188-287 |
1.36e-07 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 52.72 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 188 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQ 261
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARG 75
|
90 100
....*....|....*....|....*.
gi 2124423178 262 VKLVNIRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21286 76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1486-1734 |
1.53e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 56.97 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQRAEERERL--AAVEAALEKQRQ---LAEAHAQAKAQAEQEAQELQRRMqeevarrEEAAVDAQQ 1560
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLerARQEAEQRKQCQeqrLKEKEEELQALREQNSLQLQERL-------EEACHKRQL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1561 QKRSIQEELQHLRQSSEAEIQAKARQVE---AAERSRLRIEEEIRVVRLQlettERQRGGAEGELQALRARAEEAEAQKR 1637
Cdd:pfam15558 161 KEREEQKKVQENNLSELLNHQARKVLVDcqaKAEELLRRLSLEQSLQRSQ----ENYEQLVEERHRELREKAQKEEEQFQ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1638 QAQEEAERLRRQvQDETQRKRQAEAELAVRvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQ----AEAERARQVQVA 1713
Cdd:pfam15558 237 RAKWRAEEKEEE-RQEHKEALAELADRKIQ-QARQVAHKTVQDKAQRARELNLEREKNHHILKLkvekEEKCHREGIKEA 314
|
250 260
....*....|....*....|.
gi 2124423178 1714 LETAQRSAEVELQSKRASFAE 1734
Cdd:pfam15558 315 IKKKEQRSEQISREKEATLEE 335
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1559-1740 |
1.64e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqletterqrggaegelqalraraEEAEAQKRQ 1638
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1639 AQeEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAER---ARQVQVALE 1715
Cdd:PRK09510 120 AE-EAAKQAALKQKQAEEAAAKAAAAA-KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAA 197
|
170 180
....*....|....*....|....*
gi 2124423178 1716 TAQRSAEVELQSKRASFAEKTAQLE 1740
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1824-2066 |
1.65e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.65 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheaaaATQKRQEL 1900
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1901 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeasrfrelaEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1980
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1981 VLAEKlaaigeatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASESELERQKGL 2059
Cdd:pfam15709 447 AEAEK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 2124423178 2060 VEDTLRQ 2066
Cdd:pfam15709 516 AQEQARQ 522
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2328-2753 |
1.93e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2328 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSLRVQMEELGKLKAriEAENRALILRDKD 2407
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2408 NTQ-RVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2482
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2483 ----KELAQEQARRLQEDKEQMaQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQAE 2558
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2559 EIGEKLHRTElatQEKVTLVQTleiqRQQSDHDAERLRQAIAELE----REKEKLKQEAKLLQLKSEEMQTVQQEQLLQE 2634
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQA----REKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2635 TQALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEvakaqKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVR 2714
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIE-----NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
410 420 430
....*....|....*....|....*....|....*....
gi 2124423178 2715 RKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2753
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1880-2198 |
3.38e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1880 EEELARLQHEAAAATQKRQ-ELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE 1958
Cdd:pfam02029 4 EEEAARERRRRAREERRRQkEEEEPSGQVTESVEP--NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1959 EAKRQRQLAEEDA---------ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN----ERLRRLAEDEAFQRR 2025
Cdd:pfam02029 82 ALERQKEFDPTIAdekesvaerKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnkwsTEVRQAEEEGEEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2026 RLEEQAAQHKADIEERLAQLRKASE---------SELERQKGLVE--------DTLRQRRQVEEEILALKVSFEKAAAGK 2088
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKekkvkyeskVFLDQKRGHPEvksqngeeEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2089 AELELE--LGRIR-SNAEdtlrsKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEaaRQRKAalEEVERLKAKV 2165
Cdd:pfam02029 242 VFLEAEqkLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEE--QRRKQ--EEAERKLREE 312
|
330 340 350
....*....|....*....|....*....|...
gi 2124423178 2166 EEARRLRERAEQESArqlqlaqDAAQKRLQAEE 2198
Cdd:pfam02029 313 EEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1935-2121 |
3.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1935 RLEAEASRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 2010
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2011 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVS 2080
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2124423178 2081 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQ 2121
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1492-1657 |
3.68e-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: 55.62 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1492 EEEERLAEQQRAEERERLAAVEAAleKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1571
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1572 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLETTERQRGGAEGELQALRARAEEAEAQK------RQAQ 1640
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 2124423178 1641 EEAERLRRQVQDETQRK 1657
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2304-2767 |
4.11e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELF 2378
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2379 SLRVQMEELG-----KLKARIEAENRALilRDKDNTQRVLQEEAEKMKH-VAEEAARLSVAAQEAARLRELAEEDLAQQR 2452
Cdd:COG4913 327 ELEAQIRGNGgdrleQLEREIERLEREL--EERERRRARLEALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2453 ALAEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARRL----------------------QEDKE-QMAqqLEQ 2506
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDAlaealgldeaelpfvgelievrPEEERwRGA--IER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2507 ETQGFQRTL--EAERQRQLEMSAEAERLKLR-----VAEMSRAQARAEEDAQRFrkqAEEIGEKLH------RTELATQE 2573
Cdd:COG4913 483 VLGGFALTLlvPPEHYAAALRWVNRLHLRGRlvyerVRTGLPDPERPRLDPDSL---AGKLDFKPHpfrawlEAELGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2574 KVTLVQTLEIQRQQS-------------------DHDA---------------ERLRQAIAELEREKEKLKQEAKLLQLK 2619
Cdd:COG4913 560 DYVCVDSPEELRRHPraitragqvkgngtrhekdDRRRirsryvlgfdnraklAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2620 SEEMQTvqqeqLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQL--FQDEVAKAQKLREEQQRQQKQMEEEKQQLVA 2697
Cdd:COG4913 640 LDALQE-----RREALQRLAEYSWDEIDVASAERE-IAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKG 713
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2698 SMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEEnQRLRERLQRLEEEHRAALAHSEEIAASQA 2767
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEERIDALRARL 782
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2306-2491 |
4.92e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 56.19 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2306 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSLRVQME 2385
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2386 ELGKLKARIEaenRAL-ILRDKDNT----QRVLQEEAEKMKHVAE--EAARLSVAAqEAARLREL-AEEDLAQQRALAE- 2456
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIE-EYRALKEAkSNKEDESQRKLEEi 456
|
170 180 190
....*....|....*....|....*....|....*..
gi 2124423178 2457 KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2491
Cdd:pfam05667 457 KELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1590-1715 |
5.69e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.05 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1590 AERSRLRIEEEIRVVRLQLETTERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDET---QRKRQAEAELAV 1666
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2124423178 1667 rVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERArQVQVALE 1715
Cdd:COG1566 160 -AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1482-1709 |
5.91e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.92 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1482 KFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQ 1561
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1562 KRSIQEELQHLRQSSEAEIQAKARQVEAAE---------RSRLRIEEEIRVVRLQLETTERQRggAEGELQALRARAEEA 1632
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQdekaerdelRAKLYQEEQERKERQKEREEAEKK--ARQRQELQQAREEQI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1633 EAQKRQAQEEAER--------------LRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERR 1698
Cdd:pfam13868 246 ELKERRLAEEAEReeeefermlrkqaeDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
250
....*....|.
gi 2124423178 1699 LRQAEAERARQ 1709
Cdd:pfam13868 326 ERRERIEEERQ 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1828-2227 |
6.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1905
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1906 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED--------------- 1970
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1971 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASE 2050
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2051 SELERQKGLVE-DTLRQRRQVEEEILALKVSFEKAAAGKAElelelgRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQR 2129
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2130 RREAEERVQKSLAAEEEAARQRKAALEEveRLKAKVEEARRLRERAEQesarqLQLAQDAAQKRLQAEEKahafavqqke 2209
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEE--ELEELREELAELEAELEQ-----LEEDGELAELLQELEEL---------- 481
|
410
....*....|....*...
gi 2124423178 2210 qelqqtlqqeqsmLERLR 2227
Cdd:COG4717 482 -------------KAELR 486
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3868-3903 |
6.10e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 6.10e-07
10 20 30
....*....|....*....|....*....|....*.
gi 2124423178 3868 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3903
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1778-2178 |
6.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1778 LERWQLKANEA------LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGT 1851
Cdd:COG4717 104 LEELEAELEELreelekLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1852 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE---------------LAKVRAEMEVLLA 1916
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleaaaleerlkearlLLLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1917 SKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLK 1996
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1997 TEAEIALKEKEAENERLRRLAEDEAFQRRR--LEEQAAQHKADIEERLAQLRKAseSELERQKGLVEDTLRQRRQVEEEI 2074
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEEL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2075 LalkvsfekAAAGKAELELELGRIRSNAEDTlrskeQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAA 2154
Cdd:COG4717 422 L--------EALDEEELEEELEELEEELEEL-----EEELEELREELAELEAELEQLEEDGELAELLQELEELKAELREL 488
|
410 420
....*....|....*....|....
gi 2124423178 2155 LEEVERLKAKVEEARRLRERAEQE 2178
Cdd:COG4717 489 AEEWAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1839-2239 |
6.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1839 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EAAAATQKRQELEAELAKVRAEMEvlla 1916
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1917 sKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLK 1996
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1997 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVE 2061
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2062 DTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQrrreaeerVQKSL 2141
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2142 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2220
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410
....*....|....*....
gi 2124423178 2221 SMLERLRGEAEAARRAAEE 2239
Cdd:COG4717 461 ELEQLEEDGELAELLQELE 479
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1493-1677 |
7.35e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1493 EEERLAEQQR--AEERERLaaveAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ 1570
Cdd:PRK09510 93 QQKQAAEQERlkQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1571 HLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlettERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqv 1650
Cdd:PRK09510 169 KKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA------- 230
|
170 180
....*....|....*....|....*..
gi 2124423178 1651 qdETQRKRQAEAELAVRVKAEAEAARE 1677
Cdd:PRK09510 231 --AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1499-1678 |
7.36e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1499 EQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRrmqeEVARREEAAVDAQQQKRSIQEELQHLRqsSEA 1578
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1579 EIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAqkrQAQEEAERLRRQVQDETQRKR 1658
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAERE 166
|
170 180
....*....|....*....|
gi 2124423178 1659 QAEAELAVRVKAEAEAAREK 1678
Cdd:COG1579 167 ELAAKIPPELLALYERIRKR 186
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3609-3645 |
7.57e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.57e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 3609 IRLLEAQIATGGIIDPVHSHRVPVEVAYQRGYFDEEM 3645
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1952-2762 |
7.75e-07 |
|
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: 55.75 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1952 RLRALAEEAKRQRQLAEEDAARQRAEAERVLAeklaaiGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRrrleeQA 2031
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLG------TKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGR-----IL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2032 AQHKADIEERLAQLRKASESELERQKGLvedtlrqrRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 2111
Cdd:TIGR00618 122 AAKKSETEEVIHDLLKLDYKTFTRVVLL--------PQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2112 AELEAMRQR-QLAAEEEQRRREAEERVQKSLAAEEEAARqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQDAA 2190
Cdd:TIGR00618 194 GKAELLTLRsQLLTLCTPCMPDTYHERKQVLEKELKHLR------EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2191 Q-KRLQAEEKAHAfavqqkeqelqqtlqqeqsmlerlrgeaeaarraaeeaeeARERAEREAAQSRRQVEEAERLKQSAE 2269
Cdd:TIGR00618 268 RiEELRAQEAVLE----------------------------------------ETQERINRARKAAPLAAHIKAVTQIEQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2270 EQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQK--QAADAEMEKHKKFAEQTLRQKAQVEQElTTLRLQLEETDH 2347
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2348 QKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKdNTQRVLQEEAEKMKHVAEEA 2427
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA-AITCTAQCEKLEKIHLQESA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2428 ARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQedKEQMAQQLEQE 2507
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR--GEQTYAQLETS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2508 TQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgekLHRTELATQEKVTLVQTLEIQRQQ 2587
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2588 SDHDAERLRQAIAELEREKEKLKQEAKLLQLKSE---EMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE 2664
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2665 Q---LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVR-----------RKQEELQLLEQQRQQQ 2730
Cdd:TIGR00618 701 QcqtLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlkarteahfNNNEEVTAALQTGAEL 780
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423178 2731 EKLLAEENQRLRER------LQRLEEEHRAALAHSEEI 2762
Cdd:TIGR00618 781 SHLAAEIQFFNRLReedthlLKTLEAEIGQEIPSDEDI 818
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2146-2490 |
8.14e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.51 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2146 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQDAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2217
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2218 qeqsmLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaAEKLRKEAEQEAARRA 2297
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR------------------KVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2298 QAEQAALRQKQAADAEmekhkkfaEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEElqrlkaevtEAARQRSQVEeel 2377
Cdd:pfam17380 419 KVEMEQIRAEQEEARQ--------REVRRLEEERAREMERVRLEEQERQQQVERLRQQ---------EEERKRKKLE--- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2378 fslrvqMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2457
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
330 340 350
....*....|....*....|....*....|....*..
gi 2124423178 2458 MLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2490
Cdd:pfam17380 553 RIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4290-4318 |
8.95e-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: 8.95e-07
10 20
....*....|....*....|....*....
gi 2124423178 4290 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4318
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1510-1731 |
1.01e-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: 54.47 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1510 AAVEAALEKQRQ----LAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR 1585
Cdd:TIGR02794 46 GAVAQQANRIQQqkkpAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1586 QVEAAERSRlriEEEIRVVRLQLETTERQrggAEGElqalrARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1665
Cdd:TIGR02794 126 AKQAAEAKA---KAEAEAERKAKEEAAKQ---AEEE-----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1666 vrvKAEAEAAREKQRAlqaleEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAS 1731
Cdd:TIGR02794 195 ---KAKAEAAKAKAAA-----EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGA 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2326-2620 |
1.05e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2326 RQKAQVEQELTTLRLQLeeTDHQKSiLDEE-------------LQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKlkA 2392
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQQA-LDVQqtraiqyqqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2393 RIEAENRaliLRDKDNTQRVLQEEAEKMKHVAEEAARlSVAAQEAarlRELaEEDLAQQRALAEKM---------LKEKM 2463
Cdd:PRK04863 458 LLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVA---REL-LRRLREQRHLAEQLqqlrmrlseLEQRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2464 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQEtqgfqrtLEAERQRQLEMSAEAERLKLRVAE-MSRA 2542
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2543 QA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLRQAIAELEREKEKLKQ-----EA 2613
Cdd:PRK04863 603 PAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQpggseDP 673
|
....*..
gi 2124423178 2614 KLLQLKS 2620
Cdd:PRK04863 674 RLNALAE 680
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1629-1745 |
1.19e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.49 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1629 AEEAEAQKRQAQEEAERLRRQvqdETQRKRQAEAELAVRVKaEAEAAREKQRAlqaleefRLQAEEAerrLRQAEAERAR 1708
Cdd:COG2268 212 TEIAIAQANREAEEAELEQER---EIETARIAEAEAELAKK-KAEERREAETA-------RAEAEAA---YEIAEANAER 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 1709 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1745
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1839-1996 |
1.35e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.02 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1839 QELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqhEAAAATQKRQELEAELAKVRAemevllAS 1917
Cdd:PTZ00491 647 DSLQKSVQLAiEITTKSQEAAARHQAELLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES------SG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1918 KARAEEESRSTSEKSKQRLEAEASRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLK 1996
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI-EATKFE 791
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2411-2767 |
1.44e-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: 54.98 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2411 RVLQEEAEKMKHVAEEAARLSVAAQEaaRLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2490
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2491 RRLQEDKEQMAQQLEQETQGFQRTLE---AERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2567
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2568 ELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQ-EAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEK 2646
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2647 DTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEgvrrkqeelqlleQQ 2726
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE-------------DL 473
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2124423178 2727 RQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQA 2767
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2311-2772 |
1.52e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2311 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2379
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2380 LRvqmeeLGKLKARIeaeNRALILRDKDNTQRVLQEEAEKMKHVAEEA-ARLSVAAQEAARLRELAEEDLAQQRaLAEKM 2458
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2459 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLE 2524
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2525 MSAEAERLKLRVAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLR 2596
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2597 QAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE-------QLFQD 2669
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgakaelKALET 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2670 EVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLE 2749
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
490 500
....*....|....*....|....
gi 2124423178 2750 EEHRAALAHSE-EIAASQATAVKA 2772
Cdd:pfam12128 835 ADTKLRRAKLEmERKASEKQQVRL 858
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4073-4110 |
1.55e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.48 E-value: 1.55e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2124423178 4073 QKFLEGTSCIAGVFVDSTKERLSVYQAMKKGIIRPGTA 4110
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1456-1744 |
1.67e-06 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 54.46 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1456 SESVIQEyvDLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAAVEAALEKQRQL-----AEAHAQ-A 1529
Cdd:pfam15450 219 AESSLRE--ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1530 KAQAEQE-AQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVE------AAERSRLRIEEEir 1602
Cdd:pfam15450 295 KGQLEESqAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1603 VVRLQLETTERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAarekqra 1681
Cdd:pfam15450 373 TLGLKLSEAKKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKA------- 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1682 lqalEEFRLQAeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1744
Cdd:pfam15450 446 ----REFEVEA------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1863-2168 |
1.71e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.57 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1863 IRLRA-ETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1935
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1936 LEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlaeklaaigeatrlkteAEIALKEKEAENERLRR 2015
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2016 LAEDEAFQRRrleeqaaqhkadieerlAQLRKASESELERQKGLVEDTLRQRRQVEEEILAlkvsfeKAAAGKAELELEL 2095
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA------RAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2096 grIRSNAEDTLRSKEQAELEAMRQRQLAAeeeqrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 2168
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2950-2986 |
1.83e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 1.83e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 2950 IRLLEAQIATGGVIDPVHSHRVPVEVAYQRGYFDEEM 2986
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2450-2773 |
1.90e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2450 QQRALAEKMLKEKMQavqeatrlKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLEQETQGfqrTLEAERQR-QLEMSA 2527
Cdd:pfam17380 280 HQKAVSERQQQEKFE--------KMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQA---AIYAEQERmAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2528 EAERLKLRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTELATQEKVTLV-QTLEIQRQQSDHDAERLRQaIAELEREK 2606
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVrQELEAARKVKILEEERQRK-IQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2607 EKLKQEAKllQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE-QLFQDEVAKAQKLR-----EE 2680
Cdd:pfam17380 423 EQIRAEQE--EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLElEKEKRDRKRAEEQRrkileKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2681 QQRQQKQMEEEKQQ---LVASMEEAR------QRQREAEEgvRRKQEELQLLEQQRQQQEKLLAEENQRL------RERL 2745
Cdd:pfam17380 501 LEERKQAMIEEERKrklLEKEMEERQkaiyeeERRREAEE--ERRKQQEMEERRRIQEQMRKATEERSRLeamereREMM 578
|
330 340
....*....|....*....|....*...
gi 2124423178 2746 QRLEEEHRaalAHSEEIAASQATAVKAL 2773
Cdd:pfam17380 579 RQIVESEK---ARAEYEATTPITTIKPI 603
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2429-2595 |
2.03e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2429 RLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQ-----EDKEQM 2500
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNELQKLEKRLLQkeenlDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2501 AQQLEQETQGFQRTLEAERQRQLEMSAEAERLK-------LRVAEMSRAQAR----------AEEDAQRFRKQAEEIGEk 2563
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKeillekveeeARHEAAVLIKEIEEEAK- 183
|
170 180 190
....*....|....*....|....*....|...
gi 2124423178 2564 lhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2595
Cdd:PRK12704 184 ----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
181-293 |
2.11e-06 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 50.00 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 181 ERDRVQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIA 253
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423178 254 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1567-1939 |
2.34e-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: 53.75 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1567 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1646
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1647 RRQVQDETQRKRQAEAELAVRVKA-EAEAAREKQRALQA---LEEFRLQAEEAERRLRQAEAERaRQVQVALETAQ---R 1719
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLEReteLERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1720 SAEVELQSKRASFAEKTAQLERtLQEEhvaVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1799
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-LQDT---ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1800 QQKSlaqaeaekqkeeaerearrRGKAEEQAVRQR--ELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRq 1877
Cdd:pfam07888 265 AQRD-------------------RTQAELHQARLQaaQLTLQLADASLALREGRA--RWAQERETLQQSAEADKDRIEK- 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1878 lLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAE 1939
Cdd:pfam07888 323 -LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASlrvAQKEKEQLQAE 386
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1857-1952 |
2.39e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 54.19 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1857 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1936
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 2124423178 1937 EAEASRFrELAEEAAR 1952
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1113-1652 |
2.50e-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: 54.20 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1113 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIA-EQQKAQAEVEGLGKGVARLS 1191
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1192 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRSTHGAEEVLKAHEEQLKEAQAVpaTLPE 1271
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1272 LEATKAALKKLRAQAEAQQPMFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1342
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1343 DLRQRELEQLGRQLRYYRESADPLGAWLQDAKR---RQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQrfa 1419
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1420 kQYINAIKDYELQLvTYKAQLEPVASPAKKPKVQsgSESVIQEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEERLAE 1499
Cdd:TIGR00618 643 -LKLTALHALQLTL-TQERVREHALSIRVLPKEL--LASRQLALQKMQSEKEQLTYWKEM-LAQCQTLLRELETHIEEYD 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1500 QQRAEERERLAAVEAALEKQRQLA-----EAHAQAKAQAEQEAQELQRRMQEEVA-----RREEAAVDAQQQKRSIQEEL 1569
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAAREDALnqslkELMHQARTVLKARTEAHFNNNEEVTAalqtgAELSHLAAEIQFFNRLREED 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1570 QHLRQSSEAEIQAKARQVEAAersRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1649
Cdd:TIGR00618 798 THLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
...
gi 2124423178 1650 VQD 1652
Cdd:TIGR00618 875 SDK 877
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1509-1921 |
2.93e-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: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1509 LAAVEAALEKQRQLAEAHAQAKaqaeqEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1577
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1578 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1649
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1650 VQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1729
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1730 ASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1809
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1810 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1889
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 2124423178 1890 AAAATQKRQELEAELAKVRAEMEVLLASKARA 1921
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2431-2709 |
3.04e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 54.07 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2431 SVAAQEAARLRELAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLEqETQG 2510
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2511 FQRTLEAERQRQLEMSAEAERlklrvaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2590
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2591 DAE---RLRQAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSflsekDTLLQRErfiEQEKAKLEQ 2665
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKS-----EAGVAQG---EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2124423178 2666 LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQR-QREA 2709
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2353-2559 |
3.13e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2353 DEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALIlRDKDNTQRVLQEEAEKMKHVAEEAARLSV 2432
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2433 AAQEAARLRELAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2504
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 2505 EQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2559
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2313-2750 |
3.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2313 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSLRVQMEE 2386
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2387 LGKLKARIEAENRALilrdkdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAE--EDLAQQRALAEKMLKEKmq 2464
Cdd:PRK03918 312 IEKRLSRLEEEINGI--------EERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2465 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2539
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2540 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKL-KQEAKL 2615
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2616 LQLKSEemqtvqqeqllqetqalqqsfLSEKDTLLQRERFIEQEKAKLEQlfqdEVAKAQKLREEQQRQQKQMEEEKQQL 2695
Cdd:PRK03918 542 KSLKKE---------------------LEKLEELKKKLAELEKKLDELEE----ELAELLKELEELGFESVEELEERLKE 596
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 2696 VASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEE 2750
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3278-3314 |
3.26e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.26e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 3278 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3314
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1467-1600 |
3.45e-06 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 51.91 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1467 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQeaqelqR 1542
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1543 RMQEEVARREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKARQVEAA-----ERSRLRIEEE 1600
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1511-1684 |
3.75e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1511 AVEAALEKQRQLAEAHAQAkAQAEQEAQELQRR---MQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQV 1587
Cdd:COG1579 1 AMPEDLRALLDLQELDSEL-DRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1588 EAAER--SRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELa 1665
Cdd:COG1579 76 KKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL- 154
|
170
....*....|....*....
gi 2124423178 1666 vrvKAEAEAAREKQRALQA 1684
Cdd:COG1579 155 ---EAELEELEAEREELAA 170
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2304-2768 |
3.88e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQA-ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDhqksILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2382
Cdd:PRK02224 211 LESELAeLDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2383 QMEELGK------------------LKARIEA-ENRALILRDKDNTQRV------------------LQEEAEKMKhvaE 2425
Cdd:PRK02224 287 RLEELEEerddllaeaglddadaeaVEARREElEDRDEELRDRLEECRVaaqahneeaeslredaddLEERAEELR---E 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2426 EAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE 2505
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2506 ---------------QETQGFQR--TLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE------DAQRFRKQAEEIGE 2562
Cdd:PRK02224 444 eaealleagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2563 KLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQlksEEMQTVQQEQLLQETQALQQSF 2642
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERIESLERIRTLLAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2643 LSEKDTLLQRERfieqekAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQqlvASMEEARQRQREAEEGVRRKQEELQL 2722
Cdd:PRK02224 601 IADAEDEIERLR------EKREALAELNDERRERLAEKRERKRELEAEFDE---ARIEEAREDKERAEEYLEQVEEKLDE 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 2723 LEQQRQQQEKLLA------EENQRLRERLQRLEEEHRAALAHSEEIAASQAT 2768
Cdd:PRK02224 672 LREERDDLQAEIGavenelEELEELRERREALENRVEALEALYDEAEELESM 723
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1451-1665 |
3.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1451 KVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHA 1527
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1528 QAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlq 1607
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALK------ 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1608 letTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1665
Cdd:COG4942 195 ---AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1828-2052 |
4.22e-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: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1904
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1905 AKVRAEMEVLLASKARAEEESrstsekskQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1984
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRA--------QLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1985 klaAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESE 2052
Cdd:COG3206 318 ---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1494-1749 |
4.22e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1494 EERLAEQQRaEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE--EVARREEAAVDAQQQKrsiQEELQH 1571
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkEELRQSREKHEELEEK---YKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1572 LRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1651
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIK-------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1652 DETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKR 1729
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLG 257
|
250 260
....*....|....*....|
gi 2124423178 1730 ASFAEKTAQLERTLQEEHVA 1749
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQA 277
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1498-1941 |
4.35e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.99 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1498 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1577
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1578 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1657
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1658 RQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1737
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1738 QLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1817
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1818 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKR 1897
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2124423178 1898 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1941
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2328-2711 |
4.51e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2328 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIE--AENRALILR 2404
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2405 DKDNtqrvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQ 2480
Cdd:PRK02224 273 EREE----LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2481 QQKELAQEQARRLQEDkeqmAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEI 2560
Cdd:PRK02224 349 EDADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2561 GEKLH--RTELAT-QEKVTLVQTL-----------EIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTV 2626
Cdd:PRK02224 425 REREAelEATLRTaRERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2627 QQEQllqetqalqqsflSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEqqrqqkqmeeeKQQLVASMEEARQRQ 2706
Cdd:PRK02224 505 VEAE-------------DRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAA 560
|
....*
gi 2124423178 2707 REAEE 2711
Cdd:PRK02224 561 AEAEE 565
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1242-1801 |
4.55e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.27 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1242 IRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAAL--KKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGER-- 1317
Cdd:PRK10246 250 TRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRar 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1318 --------------------------------DVEVERWRERVAQL------LERWQAVLAqTDLRQRE----------- 1348
Cdd:PRK10246 330 irhhaakqsaelqaqqqslntwlaehdrfrqwNNELAGWRAQFSQQtsdreqLRQWQQQLT-HAEQKLNalpaitltlta 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1349 ------LEQLGRQlRYYRESADPLGAWLQDAKRRQEQIQAMVladSRAVREQLRQEKALLEEIERHGEKVEE-------C 1415
Cdd:PRK10246 409 devaaaLAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQVAI---QNVTQEQTQRNAALNEMRQRYKEKTQQladvktiC 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1416 QRFAKqyinaIKDyelqLVTYKAQLEPvASPAkkPKVQSGSESVIQEYVDLRtryselttltsqyikfISETLRRMEEEE 1495
Cdd:PRK10246 485 EQEAR-----IKD----LEAQRAQLQA-GQPC--PLCGSTSHPAVEAYQALE----------------PGVNQSRLDALE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1496 RLAEQQRAEERERLAAVEaALEKQRQLAEAHAQAKAQAEQ----EAQEL------QRRMQEEVARREEAAVDAQQQKRSI 1565
Cdd:PRK10246 537 KEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQEEQaltqQWQAVcaslniTLQPQDDIQPWLDAQEEHERQLRLL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1566 QEelQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEEIRVVRLQLEtterqrggAEGELQA-LRARAEEAeAQKRQAQEEA 1643
Cdd:PRK10246 616 SQ--RHELQGQIAAHNQQIIQYQQQiEQRQQQLLTALAGYALTLP--------QEDEEASwLATRQQEA-QSWQQRQNEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1644 ERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQaEAERARQVQVALETAqrsaev 1723
Cdd:PRK10246 685 TALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVL-EAQRLQKAQAQFDTA------ 757
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1724 eLQSKRasFAEKTAQLERTLQEEhvAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQ 1801
Cdd:PRK10246 758 -LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQE 830
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1473-1710 |
4.56e-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: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1473 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAAVEAALEKQRQlAEAHAQAKAQAEQEAQELQRrMQEEVAR 1550
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1551 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRggAEGELQALRAR-A 1629
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1630 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEaAREKQRALQALEEfrlQAEEAERRLRQAEAERARQ 1709
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARE---LYESLLQRLEEARLAEALT 384
|
.
gi 2124423178 1710 V 1710
Cdd:COG3206 385 V 385
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1450-1643 |
4.59e-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: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1450 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQ- 1528
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1529 -AKAQAEQEAQELQRRMQEEVARREE---AAVDAQQQKRS----IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEE 1600
Cdd:COG3206 263 pVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAAlraqLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2124423178 1601 IRV---VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1643
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2110-2626 |
4.77e-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: 53.22 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2110 EQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA------ARQRKAALEEVERLKAKVEEARRLRERAEQESARQL 2183
Cdd:pfam07111 63 QQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmeldalAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQREL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2184 QLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVE---- 2259
Cdd:pfam07111 143 EEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTlves 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2260 --------------------EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA-EMEKHK 2318
Cdd:pfam07111 223 lrkyvgeqvppevhsqtwelERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSlEPEFPK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2319 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT-----EAARQRS------QVEEELFSLR-VQMEE 2386
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTsqsqeQAILQRAlqdkaaEVEVERMSAKgLQMEL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2387 LGKLKARIEAENRA--------LILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKM 2458
Cdd:pfam07111 383 SRAQEARRRQQQQTasaeeqlkFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2459 LK-----------------EKMQAVQEATRLKAE----AELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT--- 2514
Cdd:pfam07111 463 QEscpppppappvdadlslELEQLREERNRLDAElqlsAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlas 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2515 ----LEAERQRQLEMSAEAERLKLRVAEMSRA-----QARAEEDAQRFRKQAEEIGEKLHRTEL---------------A 2570
Cdd:pfam07111 543 vgqqLEVARQGQQESTEEAASLRQELTQQQEIygqalQEKVAEVETRLREQLSDTKRRLNEARReqakavvslrqiqhrA 622
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2571 TQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKE----KLKQEAKLLQLKSEEMQTV 2626
Cdd:pfam07111 623 TQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLLSRYKQQRLLAV 682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2518-2842 |
4.95e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2518 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2578
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2579 QTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEKDTLLQRERFIEQ 2658
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2659 EKAKLEQLfQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRkqeeLQLLEQQRQQQEKLLAEEN 2738
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2739 QRLRERLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDApDGPATEAEPEHAFDGLRQKVPAQRLQEvgilsTEELQR 2818
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERLEEALEELREEL-----EEAEQA 476
|
330 340
....*....|....*....|....
gi 2124423178 2819 LVQGRTTVAELAQREDVRRYLQGR 2842
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQEN 500
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1488-1968 |
4.97e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.82 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1488 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1567
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1568 ELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIR--VVRLQLET-------TERQRGGAEGELQALRARAEEA 1632
Cdd:pfam05557 133 ELEELQERLDllkakaSEAEQLRQNLEKQQSSLAEAEQRIKelEFEIQSQEqdseivkNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1633 EAQKRQAQEEAERLRRQVQDETQRKRQAEaelavrvKAEAEAAR---EKQRALQALEEFRLQAEEAERRLRQAEAERARQ 1709
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREE-------KYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1710 VQValetaqRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQLK 1784
Cdd:pfam05557 286 EQL------QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkERDGYR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1785 AN-EALRLRLQAEEVAQQKSLAQAEAE----KQKEEAEREARRRGKAEEQAVRQRELA---EQELEKQRQlAEGTAQQRL 1856
Cdd:pfam05557 360 AIlESYDKELTMSNYSPQLLERIEEAEdmtqKMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQALRQ-QESLADPSY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1857 AAE------QELIRLRAETEQGEQQRQLLEEELAR--------------LQHEAAAATQKRQELEAELAKVRAEMEvlla 1916
Cdd:pfam05557 439 SKEevdslrRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIE---- 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1917 skaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEA-KRQRQLAE 1968
Cdd:pfam05557 515 ---RLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAeLKNQRLKE 564
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1547-1712 |
5.01e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.84 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1547 EVARR----EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRggaegel 1622
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1623 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelavrvKAEAEAAREKQRALQALEEfRLQAEEAERRLRQ 1701
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 2124423178 1702 AEAERARQVQV 1712
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1485-1706 |
5.16e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1485 SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK----------AQAEQEAQELQRRMQEEVARREEA 1554
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKesvaerkennEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1555 AV----------DAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQA 1624
Cdd:pfam02029 132 ETeirekeyqenKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1625 ---------------------LRARAEEAEAQKrQAQEEAERLRRQVQD------ETQRKRQAEAELAVrvkAEAEAARE 1677
Cdd:pfam02029 212 geeevtklkvttkrrqgglsqSQEREEEAEVFL-EAEQKLEELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKRE 287
|
250 260
....*....|....*....|....*....
gi 2124423178 1678 KQRALQALEEFRLQAEEAERRLRQAEAER 1706
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREEEEKR 316
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1097-1649 |
5.75e-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: 52.81 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1097 DRLQAEREYGSCSHHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRLPLDK---EPARECAQRIAE 1172
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLRRELDDrnmEVQRLEALLKAM 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1173 QQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTLGKLEQVrslsaiyLEKLKTISLVIRSTHGAEEVL 1252
Cdd:pfam15921 439 KSECQGQMERQMAAIQGKNESLEKV----------SSLTAQLESTKEMLRKV-------VEELTAKKMTLESSERTVSDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1253 KAHEEQLKEAqavpatlpeLEATKAALKKLRAQAEAQQPMFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVA 1329
Cdd:pfam15921 502 TASLQEKERA---------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1330 QLLE-------RWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1402
Cdd:pfam15921 573 NMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1403 EEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyik 1482
Cdd:pfam15921 653 QERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN---- 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1483 fiseTLRRMEEEERlaeqqraeererlAAVEAALEKQRQLAEAHAQAKAqaeqeaqelqrrMQEEVARREEAAVDAQQQK 1562
Cdd:pfam15921 714 ----TLKSMEGSDG-------------HAMKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEK 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1563 RSIQEELQHLRQssEAEIQAKARQVEAAERSRLRIEEEirvvRLQLETTERQRGGAEGELQAlrarAEEAEAQKRQAQEE 1642
Cdd:pfam15921 765 HFLKEEKNKLSQ--ELSTVATEKNKMAGELEVLRSQER----RLKEKVANMEVALDKASLQF----AECQDIIQRQEQES 834
|
....*..
gi 2124423178 1643 AeRLRRQ 1649
Cdd:pfam15921 835 V-RLKLQ 840
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1559-1745 |
6.34e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETT--ERQRGGAEGELQALRARAEEAEAQK 1636
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKllLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1637 RQAQEEAERLRRQVQD-----ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEfrlQAEEAERRLRQAEAERARQVQ 1711
Cdd:COG3206 243 AALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA---QIAALRAQLQQEAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|....
gi 2124423178 1712 VALETAQRSAEvELQSKRASFAEKTAQLERTLQE 1745
Cdd:COG3206 320 AELEALQAREA-SLQAQLAQLEARLAELPELEAE 352
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2416-2575 |
7.47e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2416 EAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2495
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2496 DKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2575
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1834-2556 |
7.59e-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: 52.43 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1834 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQHEA--AAATQKRQELEAELAKVR 1908
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHFRSlgSAISKILRELDTEISYLK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1909 AEM----EVLLASKARAEEESRSTSEKSKQRLEAEASR----FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1980
Cdd:pfam15921 238 GRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEheveITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1981 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASESELERQKGLV 2060
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKELS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2061 EDTLRQRRQVEEEIlalkvsfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAMRQrqlaaeeeqrrrEAEERVQKS 2140
Cdd:pfam15921 395 LEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQGQ 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2141 LAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQLAqdaAQKRLQAEEKAhafAVQQKEQELQQTLQQE 2219
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLE---SSERTVSDLTA---SLQEKERAIEATNAEI 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2220 QSMLERLRgeaeaarraaeeaeeareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLrkeaeqeaaRRAQA 2299
Cdd:pfam15921 520 TKLRSRVD----------------------------LKLQELQHLKNEGDHLRNVQTECEALKLQM---------AEKDK 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2300 EQAALRQKQAADAEM-EKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----E 2374
Cdd:pfam15921 563 VIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagS 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2375 EELFSLRVQMEELGKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQ---EAAR--LRELAEED 2447
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQselEQTRntLKSMEGSD 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2448 -------LAQQRALAEK-----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEqetqgfqrT 2514
Cdd:pfam15921 723 ghamkvaMGMQKQITAKrgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE--------V 794
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2124423178 2515 LEAERQRQLE----MSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2556
Cdd:pfam15921 795 LRSQERRLKEkvanMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
301-408 |
7.64e-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: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 301 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 379
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 2124423178 380 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1622-1896 |
7.75e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1622 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQAleefrlQAEEAERRLRQ 1701
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQ------ELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1702 AEAERARqvqvaletaqrsAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW 1781
Cdd:COG4942 88 LEKEIAE------------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1782 QLKANEALRLRLQAEEVAQQKSLAQaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaqqrlaAEQE 1861
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALL--------------------AELEEERAALEALKAERQKLLAR--------LEKE 207
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423178 1862 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1896
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1828-2614 |
8.05e-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: 52.42 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR-----LQHEAAAATQKRQELEA 1902
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1903 ElakvraemevllaskaraEEESRSTSEKSKQRLEAEASRFRELAEEAARLR-----ALAEEAKRQRQLaEEDAARQRAE 1977
Cdd:pfam05483 177 E------------------REETRQVYMDLNNNIEKMILAFEELRVQAENARlemhfKLKEDHEKIQHL-EEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1978 AERVLAEKLAAIGEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRRLEeQAAQHKADIEERLAQLRKASESELERQK 2057
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2058 GLVED---TLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSkEQAELEAmRQRQLAAEEEQrrreae 2134
Cdd:pfam05483 314 ALEEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRT-EQQRLEK-NEDQLKIITME------ 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2135 erVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQDAAQKRLQAEEK-AHAFAVQqkeqe 2211
Cdd:pfam05483 386 --LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ----- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2212 lqqtlqqeqsmlerlrgeaeaarraaeeaeearerAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQ 2291
Cdd:pfam05483 459 -----------------------------------LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2292 EAARRAQAEQAALRQKQaadaEMEKHKKFAEQTLRQKAQVEQELTTLRLQLE--------ETDHQKSILD---EELQRLK 2360
Cdd:pfam05483 504 LTQEASDMTLELKKHQE----DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIE 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2361 AEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALilrDKDNTQRVLQEEAEKMKhVAEEAARLSVAAQEAARL 2440
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL---KKKGSAENKQLNAYEIK-VNKLELELASAKQKFEEI 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2441 RELAEEDLAQQRALAEKMLKEkmqaVQEATRLKAEAELLQQQKELaqeqarRLQEDKEQMAQQLEQETQGFQRTLEaERQ 2520
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEE----VEKAKAIADEAVKLQKEIDK------RCQHKIAEMVALMEKHKHQYDKIIE-ERD 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2521 RQLEMSAEAERlklrvaEMSRAQARAEEDAQRFRkqaeeigeklhrtelatQEKVTLVQTLEIQRQqsdhdaerlrqaia 2600
Cdd:pfam05483 725 SELGLYKNKEQ------EQSSAKAALEIELSNIK-----------------AELLSLKKQLEIEKE-------------- 767
|
810
....*....|....
gi 2124423178 2601 elerEKEKLKQEAK 2614
Cdd:pfam05483 768 ----EKEKLKMEAK 777
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2393-2558 |
8.29e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2393 RIEAENRALILRDKdntqRVLQEEAEKMKHVAE-----EAARLSVAAQEAARLRELAEEDLAQQ--RALAEKMLKEKMQA 2465
Cdd:COG2268 199 RDARIAEAEAERET----EIAIAQANREAEEAEleqerEIETARIAEAEAELAKKKAEERREAEtaRAEAEAAYEIAEAN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2466 VQEATRLKAEAELLQQQKELAqeQARRLQEDKEQMAQQLEQetqgfqrtLEAERQRQLEmSAEAErlklrvAEMSRAQAR 2545
Cdd:COG2268 275 AEREVQRQLEIAEREREIELQ--EKEAEREEAELEADVRKP--------AEAEKQAAEA-EAEAE------AEAIRAKGL 337
|
170
....*....|...
gi 2124423178 2546 AEedAQRFRKQAE 2558
Cdd:COG2268 338 AE--AEGKRALAE 348
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1509-1603 |
8.81e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.26 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1509 LAAVEAALEKQRQLAEAHAQAKAQAEQEAqelqRRMQEEVARREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKARQV 1587
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 2124423178 1588 EAAERSRLRI---EEEIRV 1603
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3497-3532 |
9.68e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 9.68e-06
10 20 30
....*....|....*....|....*....|....*.
gi 2124423178 3497 LLQGSGCLAGIYLEESKEKVTIYEAMRRGLLRPSTA 3532
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1523-1738 |
9.87e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1523 AEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1602
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1603 VVRLQLETTERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1662
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1663 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1738
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
768-858 |
1.07e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.94 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 768 FVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVESFQAAL 847
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEEL 82
|
90
....*....|.
gi 2124423178 848 QTQWSWMLQLC 858
Cdd:smart00150 83 NERWEELKELA 93
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1489-1662 |
1.17e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1489 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE----QEAQELQRRMQEEVARreEAAVDAQQQKRS 1564
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEerqrQEEEERKQRLQLQAAQ--ERARQQQEEFRR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1565 IQEELQHLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEae 1644
Cdd:pfam15709 431 KLQELQRKKQQEEAE--------RAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE-- 496
|
170
....*....|....*...
gi 2124423178 1645 rlRRQVQDETQRKRQAEA 1662
Cdd:pfam15709 497 --RRQKEEEAARLALEEA 512
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2424-2875 |
1.18e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 51.89 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2424 AEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2503
Cdd:COG4995 10 LAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2504 LEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2583
Cdd:COG4995 90 LAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2584 QRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKL 2663
Cdd:COG4995 170 LALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2664 EQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRE 2743
Cdd:COG4995 250 LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2744 RLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQRLVQGR 2823
Cdd:COG4995 330 LALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLL 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2824 TTVAELAQREDVRRYLQGRSSIAGLLLKP--ANEKLSIYTALRRQLLSPGTALI 2875
Cdd:COG4995 410 RLLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4075-4113 |
1.23e-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: 1.23e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 4075 FLEGTSCIAGVFVDSTKERLSVYQAMKKGIIRPGTAFEL 4113
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2404-2559 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2404 RDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2480
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2481 QQKELAQEQARRLQEDKEqmaQQLEQETQgfqrtLEAERQRQLEMsAEAERLKLRvAEMSRAQARAEEDAQRFRKQAEE 2559
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQ---RQKELEMQ-----LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKEEE 503
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3497-3535 |
1.30e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.30e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3497 LLQGSGCLAGIYLEESKEKVTIYEAMRRGLLRPSTATVL 3535
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1416-1747 |
1.41e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.55 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1416 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1494
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1495 ERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQ----------ELQRRMQE-EVARREEAAVDAQQQKR 1563
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1564 SIQEELQHLRQSSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA----EAQKRQA 1639
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGvlgePATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1640 QEEAERLRRQVQDET-------QRKRQAEAELAV-RVKAEAEAAREKQR---ALQALEEFRLQAEEAERRLRQAEA---- 1704
Cdd:NF033838 280 ENDAKSSDSSVGEETlpspslkPEKKVAEAEKKVeEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAELelvk 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2124423178 1705 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1747
Cdd:NF033838 360 EEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2398-2770 |
1.46e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2398 NRALILRDKDNTQRvlQEEAEKMKHVAEEAARLSVAAQEAARLRElAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2472
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2473 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGF--QRTLEAERQRQLEMSAEAERLkLRVAE 2538
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2539 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQL 2618
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2619 KSEEMQtvqqeqllqetqalqqsflsekdtlLQRERFIEQEKAKLEQLFQdEVAKAQKLREEQQRQQKQMEEEKQQLVAS 2698
Cdd:COG3096 505 RSQQAL-------------------------AQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2699 MEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSEEIAASQATAV 2770
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLL 636
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1825-2041 |
1.51e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.76 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQE 1899
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEESRAVTKELTTLAQGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1900 LEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEASRF----RELAEEAARLRALAEEAKRQRQLAE 1968
Cdd:NF012221 1632 LDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAGVAQGEQNQANAE 1709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1969 EDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2041
Cdd:NF012221 1710 QDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNR 1782
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1664-1912 |
1.58e-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: 50.53 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1664 LAVRVKAEAEAAREKQRALQALEEfRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1743
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1744 QEEHVAVAQLREEAERRAQQQAEAerareeaerelerWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1823
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlaaeqeliRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1903
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 2124423178 1904 LAKVRAEME 1912
Cdd:COG4942 229 IARLEAEAA 237
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1916-2115 |
1.58e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1916 ASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAIGEATRL 1995
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1996 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 2075
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2124423178 2076 ALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 2115
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1249-1965 |
1.60e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.29 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1249 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpmfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1327
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1328 VAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESAdplGAWLQDAKRRQEQIQAMVladsRAVREQLRQEKALLEEIER 1407
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRKQL----SKTQEELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1408 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTSQY 1480
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1481 IKFISETLRRMEEEE-RLAEQQRAEERERLAAVEaalEKQRQLAEAHAQAKAQAEQEAQeLQRRMQEEVARREEAAVDAq 1559
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDKAAEVEVERMSA- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1560 qqkRSIQEELQhlrQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1639
Cdd:pfam07111 376 ---KGLQMELS---RAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1640 QEEAER--LRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF--RLQAEEAERRLRQAEAERARQVQVALE 1715
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVAQQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1716 TAQrsaevELQSKRASFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1795
Cdd:pfam07111 529 LEQ-----ELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1796 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1870
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1871 QGEQQR-----QLLEEE----LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1936
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 2124423178 1937 EAEASRFRELAEEAARLRALAEEAKRQRQ 1965
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1782-2200 |
1.62e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.06 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1782 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1861
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1862 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1941
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1942 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA 2021
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2022 FQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSN 2101
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2102 AEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2181
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 2124423178 2182 QLQLAQDAAQKRLQAEEKA 2200
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2304-2833 |
1.64e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILdeelqRLKAEVTEAARQRSQVEEELFSLRVQ 2383
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2384 MEELGKLKARIEA--ENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAA---RLRELAEE---DLAQQRALA 2455
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2456 EKMLKEKMQAVQEATRLKAEAELlQQQKELAQEQARRLQEDKEQMAQQLEQETQ-----------GFQRTLEAERQ---- 2520
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihlqeSAQSLKEREQQlqtk 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2521 -----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERL 2595
Cdd:TIGR00618 479 eqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2596 RQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQeqllqetqaLQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQ 2675
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN---------ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2676 KLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEE-----------NQRLRER 2744
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltywkemlaqcQTLLREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2745 LQRLEEEHR-------AALAHSEEIAASQATAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQ 2817
Cdd:TIGR00618 710 ETHIEEYDRefneienASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF 789
|
570
....*....|....*.
gi 2124423178 2818 RLVQGRTTVAELAQRE 2833
Cdd:TIGR00618 790 FNRLREEDTHLLKTLE 805
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2304-2606 |
1.64e-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: 50.84 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSLRVQ 2383
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2384 MEELGKLKARIEAENRALILRDKDNTQRVLQEEAEkmkhvaeeaarlsVAAQEAARLRELAEEDLAQQRALAEKM-LKEK 2462
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2463 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLEQETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEM 2539
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2540 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLRqaiAELEREK 2606
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLK---EELQRER 384
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1794-1970 |
1.91e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1794 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1869
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1870 EQGEQQRQLLEEELArlQHEAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRfr 1944
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA-- 236
|
170 180
....*....|....*....|....*.
gi 2124423178 1945 elAEEAARLRALAEEAKRQRQLAEED 1970
Cdd:PRK09510 237 --AAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1609-1746 |
1.94e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.23 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1609 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEeaerlrRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF 1688
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1689 RLQAEEAERRlRQAEAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1746
Cdd:TIGR02794 124 AKAKQAAEAK-AKAEAEAERK---AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEA 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1550-1903 |
2.34e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1550 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1629
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1630 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQ 1709
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1710 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1789
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1790 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1869
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 2124423178 1870 EQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1903
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1678-2577 |
2.37e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1678 KQRALQALEEFRLQAEEAERRLRQAEAERARQ----------VQVALETAQ--RSAEVELQSKRASFAEKTA-QLERTLQ 1744
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQkfylrqsvidLQTKLQEMQmeRDAMADIRRRESQSQEDLRnQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1745 EEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlkanEALRLRLQAEEVAQQKslaqaeAEKQKEEAEREARRRG 1824
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKK------IYEHDSMSTMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRqrelaeqELEKQRQLAEGtaqQRLAAEQELIRLRAETEQG-----EQQRQLLEEELARLQHEAAAATQKRQE 1899
Cdd:pfam15921 220 SAISKILR-------ELDTEISYLKG---RIFPVEDQLEALKSESQNKielllQQHQDRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1900 LEAELAKVRAEMEVLlaskaraEEESRSTSE---KSKQRLEAEASRFRELAEEAARL-RALAEEAKRQRQLAEEDAARQR 1975
Cdd:pfam15921 290 ARSQANSIQSQLEII-------QEQARNQNSmymRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1976 AEAERVLAEKLAAIGEATRL-----KTEAEIALkEKEaENER--------------LRRLAEDEAFQRRRLEEQAAQHKA 2036
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKLladlhKREKELSL-EKE-QNKRlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2037 D----IEERLAQLRKASESeLERQKGL---VEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTlrsk 2109
Cdd:pfam15921 441 EcqgqMERQMAAIQGKNES-LEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT---- 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2110 eQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEV-ERLKAKVEEARRL-RERAEQESARQL---Q 2184
Cdd:pfam15921 516 -NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKViEILRQQIENMTQLvGQHGRTAGAMQVekaQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2185 LAQDAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSMLE----RLRGEAEAARRAAEEAEEARERAEREAAQSRRQV-- 2258
Cdd:pfam15921 595 LEKEINDRRLELQEFK---ILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELns 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2259 --EEAERLKQSaeeQAQAQAQAQAAAEKLrKEAEQEAARRAQAEQAALRQKQAADAE-MEKHKKFAEQTLRQKAQV---E 2332
Cdd:pfam15921 672 lsEDYEVLKRN---FRNKSEEMETTTNKL-KMQLKSAQSELEQTRNTLKSMEGSDGHaMKVAMGMQKQITAKRGQIdalQ 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2333 QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEaenralILRDKDNTQrv 2412
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME------VALDKASLQ-- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2413 LQEEAEKMKHVAEEAARLSVaaQEAARLRELAEEDLAQQRALAEKMLKEKmqavqEATRLKAEAELLQQQKELAQEQARR 2492
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKL--QHTLDVKELQGPGYTSNSSMKPRLLQPA-----SFTRTHSNVPSSQSTASFLSHHSRK 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2493 ---LQEDKEQMAQQLEQETQ---GFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLhr 2566
Cdd:pfam15921 893 tnaLKEDPTRDLKQLLQELRsviNEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKS-- 970
|
970
....*....|.
gi 2124423178 2567 TELATQEKVTL 2577
Cdd:pfam15921 971 SETCSREPVLL 981
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1520-1647 |
2.40e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 50.05 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1520 RQLAEAHAQAKAQ-----AEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSR 1594
Cdd:COG1566 79 TDLQAALAQAEAQlaaaeAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1595 LRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1647
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1499-1722 |
2.42e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1499 EQQRAEERERLAAveaalEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE---ELQHLRQS 1575
Cdd:PRK07735 3 PEKDLEDLKKEAA-----RRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAakaKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1576 SEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE-----AEAQKRQAQEEAERLRRQV 1650
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAaakakAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 1651 QDETQRKRQAEAELAVRVKAeaeAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1722
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKA---AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQG 226
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1320-1560 |
2.43e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1320 EVERWRERVAQLLERWQAVLAQTDLRQREL------EQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVRE 1393
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFdptiadEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1394 QLRQ-----EKALLEEIERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEPVASPAK---------KPKVQSGSESV 1459
Cdd:pfam02029 140 YQENkwsteVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVfldqkrghpEVKSQNGEEEV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1460 IQEYVDLRTRYSELTTL--TSQYIKFISETLRRMEEEERLAEQQRAEERERL------AAVEAAL-----EKQRQLAEAH 1526
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSqeREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrqkqqeAELELEElkkkrEERRKLLEEE 296
|
250 260 270
....*....|....*....|....*....|....*...
gi 2124423178 1527 AQAKAQAEQEAQ----ELQRRMQEEVARREEAAVDAQQ 1560
Cdd:pfam02029 297 EQRRKQEEAERKlreeEEKRRMKEEIERRRAEAAEKRQ 334
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1271-1741 |
2.47e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1271 ELEATKAALKKLRAQAEAQQPMFDALRDELrgaqevgERLQQRHGERDVEVERWRERVAQLLERWQAVlaqtDLRQRELE 1350
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKEL-------EEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1351 QLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVladsravrEQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYE 1430
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1431 LQLVTYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSELTTltsqYIKFISETLRRMEEEERLAEQQRAEERERL 1509
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKElEEKEERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1510 AAVEAALEKqrqlaeahaqAKAQAEQEAQELQRR---MQEEVARREEAAVDAQQQK-------RSIQEE--LQHLRQSSE 1577
Cdd:PRK03918 390 EKELEELEK----------AKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1578 --AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRAR-----AEEAEAQKRQAQEEAERLR--- 1647
Cdd:PRK03918 460 elKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKlkkynLEELEKKAEEYEKLKEKLIklk 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1648 ---RQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQA-EEAERRLRQAE--------AERARQVQVALE 1715
Cdd:PRK03918 539 geiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEpfyneyleLKDAEKELEREE 618
|
490 500
....*....|....*....|....*.
gi 2124423178 1716 TAQRSAEVELQSKRASFAEKTAQLER 1741
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEE 644
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1828-2149 |
2.53e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1907
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1987
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1988 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR 2067
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2068 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2147
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 2124423178 2148 AR 2149
Cdd:COG4372 368 AD 369
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2425-2766 |
2.60e-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: 50.74 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2425 EEAARLSVAAQEAARLRELAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2504
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2505 EQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQ 2579
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2580 TLEIQRQQSDHDAERLRQAIAELEREKeKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQE 2659
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2660 KAKLEQLFQdEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQ 2739
Cdd:pfam02463 397 LELKSEEEK-EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|....*..
gi 2124423178 2740 RLRERLQRLEEEHRAALAHSEEIAASQ 2766
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1485-1967 |
2.73e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.52 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1485 SETLRRMEEEERLAEQQRAEE--RERLAAVEAALEKQRQLAEA-----HAQAKAQAEQEAQELQRR-MQEEVARREEAAV 1556
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAEllRKQLSKTQEELEAQVTLVESlrkyvGEQVPPEVHSQTWELERQeLLDTMQHLQEDRA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1557 DAQQQKRSIQ---EELQHLRQSSEAEIQAKARQVEAAE-------RSRL-RIEEEIRVVRLQLETTERQRggaEGELQAL 1625
Cdd:pfam07111 260 DLQATVELLQvrvQSLTHMLALQEEELTRKIQPSDSLEpefpkkcRSLLnRWREKVFALMVQLKAQDLEH---RDSVKQL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1626 RARAEEAEAQKRQAQEEAERLRRQVQDETqrkrqaeAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAeAE 1705
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKA-------AEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFV-VN 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1706 RARQVQVALETA-----QRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER 1780
Cdd:pfam07111 409 AMSSTQIWLETTmtrveQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1781 WQLKANEALRL-------------------RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL 1841
Cdd:pfam07111 489 ERNRLDAELQLsahliqqevgrareqgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1842 EKQRQLAeGTAQQRLAAEQElIRLRAETEQGEQQRQLLEEELAR-------LQHEAAAATQKRQELEaelakvraemevl 1914
Cdd:pfam07111 569 TQQQEIY-GQALQEKVAEVE-TRLREQLSDTKRRLNEARREQAKavvslrqIQHRATQEKERNQELR------------- 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1915 laskaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLA 1967
Cdd:pfam07111 634 -----RLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLA 681
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1465-1745 |
2.85e-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: 50.28 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1465 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLaEAHAQAKAQAEQEAQELQRRM 1544
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1545 QEEVARREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGE 1621
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1622 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA 1695
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1696 --ERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1745
Cdd:pfam07888 316 dkDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1824-1946 |
2.86e-05 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 49.05 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQH-----EAAAATQKR 1897
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 1898 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEASRFREL 1946
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2145-2618 |
2.96e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2145 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEekahAFAVQQKEQELQQTLQQEQSMLE 2224
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ----LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2225 RLRgeaeaarraaeeaeeareraereaaQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2304
Cdd:COG4717 150 ELE-------------------------ERLEELRELEE--------------------ELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2305 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA-EVTEAARQRSQVEEELFSLRVQ 2383
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2384 MEELGKLKARI------EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2457
Cdd:COG4717 265 GGSLLSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2458 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQrtlEAERQRQLEMSAEAERLKLRVA 2537
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE---LKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2538 EMSRAQARAEEDAQRFRKQAEEIGEKL--HRTELATQEkvtlvqtLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKL 2615
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEEELeeLREELAELE-------AELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
...
gi 2124423178 2616 LQL 2618
Cdd:COG4717 495 LKL 497
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1495-1980 |
3.12e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1495 ERLAEQQRAEERERlAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1574
Cdd:COG3064 2 QEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1575 SSEAEIQAKARQVeAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDET 1654
Cdd:COG3064 81 EAEKAAAEAEKKA-AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1655 QRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1734
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1735 KTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKE 1814
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1815 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAT 1894
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1895 QKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQ 1974
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 2124423178 1975 RAEAER 1980
Cdd:COG3064 480 LLLLGG 485
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1553-1759 |
3.36e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.46 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1553 EAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvvrlqletTERQRGGAEGELQALRARAEEA 1632
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK--------------ELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1633 EAQKRQAQEEAErlrrqvQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERrlrQAEAERArqvqv 1712
Cdd:TIGR02794 115 EEKQKQAEEAKA------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK---KAEAEAK----- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2124423178 1713 ALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAER 1759
Cdd:TIGR02794 181 AKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2306-2514 |
3.60e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2306 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSLRVQ 2383
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2384 MEELGKLKARIEAENRaLILRDKD--NTQRVLQEEAEKMKH-VAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLK 2460
Cdd:COG3883 111 SESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKAeLEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2461 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT 2514
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2423-2625 |
3.67e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.46 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2423 VAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2502
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2503 QLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQTLE 2582
Cdd:TIGR02794 128 QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2124423178 2583 IQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2625
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1941-2187 |
3.75e-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: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1941 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDE 2020
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2021 AFQRRRLEEQAAQHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELE 2094
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2095 LGRIRSnaedtlrSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEE--AARQRKAALEE-VERLKAKVEEARRL 2171
Cdd:pfam07888 194 FQELRN-------SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrSLQERLNASERkVEGLGEELSSMAAQ 266
|
250
....*....|....*..
gi 2124423178 2172 RERAEQESAR-QLQLAQ 2187
Cdd:pfam07888 267 RDRTQAELHQaRLQAAQ 283
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2395-2512 |
3.91e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 49.11 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2395 EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEaarlRELAEEDLAQQRALAE--KMLKEKMQavQEATRL 2472
Cdd:cd16269 180 EAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEKME--EERENL 253
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2124423178 2473 KAEAELLQQQKElaQEQARRLQEDKEQMAQQLEQETQGFQ 2512
Cdd:cd16269 254 LKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4283-4311 |
4.06e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.06e-05
10 20
....*....|....*....|....*....
gi 2124423178 4283 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4311
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1570-1858 |
4.26e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1570 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqletteRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1649
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1650 VQDETQRKRQAEAELAVRVKAeAEAAREKQRALQALEEFRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVEL--- 1725
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKA-KKAAATQPIVIKAGARPDNSAVIAAREARKAQArARQAEKQAAAAADPKKAAVAAaia 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1726 --QSKRASFAEKTAQLERTLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1803
Cdd:PRK05035 556 raKAKKAAQQAANAEAEEEVDPKKAAVAA-AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1804 LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1858
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1626-1747 |
4.59e-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: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1626 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQralQALEEFRLQAEEAER-- 1697
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1698 -RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1747
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ 465
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2410-2710 |
4.59e-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: 49.15 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2410 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2489
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2490 ARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2569
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2570 ATQEKvtlvqtleIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMqtvqqeqllqetqaLQQSFLSEkdtL 2649
Cdd:pfam13868 191 AQQEK--------AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQE--------------LQQAREEQ---I 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2650 LQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQL---VASMEEARQRQREAE 2710
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHrreLEKQIEEREEQRAAE 309
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1489-1708 |
5.02e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.21 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1489 RRMEEEERLAEQQRAEER--ERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1566
Cdd:PRK07735 29 KHGAEISKLEEENREKEKalPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1567 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1646
Cdd:PRK07735 109 AKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1647 RRQVQDETQR-KRQAEAELAVRVKAEAeAAREKQRALQ----ALEEFRLQAEEAERRLRQAEAERAR 1708
Cdd:PRK07735 189 GEGTEEVTEEeKAKAKAKAAAAAKAKA-AALAKQKASQgngdSGDEDAKAKAIAAAKAKAAAAARAK 254
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1832-2056 |
5.14e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.76 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1832 RQRELAEQELEKQRQLAEGTAQQRLAAEQEL---------IRLRAETEQGEqqRQLLEEELARLQHEAAAATQKRQELEA 1902
Cdd:pfam00038 47 RLYSLYEKEIEDLRRQLDTLTVERARLQLELdnlrlaaedFRQKYEDELNL--RTSAENDLVGLRKDLDEATLARVDLEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1903 elaKVRAEMEVLLASKARAEEESRSTSEKSKQR---LEAEASRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEA 1978
Cdd:pfam00038 125 ---KIESLKEELAFLKKNHEEEVRELQAQVSDTqvnVEMDAARKLDLTSALAEIRAQYEEiAAKNREEAEEWYQSKLEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1979 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERL--------RRLAEDEAfqrrRLEEQAAQHKADIEERLAQLRKASE 2050
Cdd:pfam00038 202 QQAAARNGDALRSAKEEITELRRTIQSLEIELQSLkkqkasleRQLAETEE----RYELQLADYQELISELEAELQETRQ 277
|
....*.
gi 2124423178 2051 sELERQ 2056
Cdd:pfam00038 278 -EMARQ 282
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1233-1740 |
5.21e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.84 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1233 EKLKTISLVIRSTHGAeevLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQ-QPMFDALRDELRGAQEvgeRLQ 1311
Cdd:pfam12128 251 NTLESAELRLSHLHFG---YKSDETLIASRQE------ERQETSAELNQLLRTLDDQwKEKRDELNGELSAADA---AVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1312 QRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAV 1391
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1392 REQLRQEKAL-LEEIERHGEKVEECQRFA-KQYINAIKDYELQLvtykaqlepvASPAKKPKVQSGSESVIQEyvdlrtr 1469
Cdd:pfam12128 399 LAKIREARDRqLAVAEDDLQALESELREQlEAGKLEFNEEEYRL----------KSRLGELKLRLNQATATPE------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1470 yseltTLTSQYIKfiSETLRRMEEEErlaeQQRAEERERLAAVEAALEKQRQLA-EAHAQAKAQAEQEAQELQRRMQEEV 1548
Cdd:pfam12128 462 -----LLLQLENF--DERIERAREEQ----EAANAEVERLQSELRQARKRRDQAsEALRQASRRLEERQSALDELELQLF 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1549 AR--------REEAAVDAQQQKRSIQEELQH-------------------------LRQ-------SSEAEIQAKARQVE 1588
Cdd:pfam12128 531 PQagtllhflRKEAPDWEQSIGKVISPELLHrtdldpevwdgsvggelnlygvkldLKRidvpewaASEEELRERLDKAE 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1589 AA---ERSRL-RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRrqvqdeTQRKRQAEAEl 1664
Cdd:pfam12128 611 EAlqsAREKQaAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAL------AERKDSANER- 683
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1665 avRVKAEAEAAREKQRALQALEEFRLQAEEAerrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1740
Cdd:pfam12128 684 --LNSLEAQLKQLDKKHQAWLEEQKEQKREA----RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE 753
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1945-2180 |
5.34e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1945 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRlaedeafQR 2024
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2025 RRLEEQAAQHKADIEERLAQLRKASESE----LERQKGlVEDTLRQRRQVEEEILALKVSFEKAAAGKAELElelgRIRS 2100
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPplalLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELA----ALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2101 NAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2180
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1828-2094 |
5.37e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQH-------EAAAATQKRQEL 1900
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1901 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEASRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1979
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1980 rvlaEKLAAIGEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SESELERQ 2056
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270
....*....|....*....|....*....|....*....
gi 2124423178 2057 KGLVEDTLRQRRQVEEEILALKVSFEKAAAG-KAELELE 2094
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQANRRlKEELQRE 383
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1825-2040 |
5.69e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1896
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1897 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE--EAKRQRQLAEEDAARQ 1974
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARakAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1975 RAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 2040
Cdd:PRK05035 607 VAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1484-1689 |
6.05e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1484 ISETLRRMEEEERLAEQQRAEERERLAAVEAALekqrqlaeahAQAKAQAEQEAQELqRRMQEEVARREEAAVDAQQQKR 1563
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1564 siqeelQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1637
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1638 -----QAQEEAERLRRQVqDETQRKRQAEAELAVR--VKAEAEAAREKQRALQALEEFR 1689
Cdd:COG1842 157 gidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1991-2625 |
6.11e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.82 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1991 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 2070
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2071 EEEIlaLKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ----------AELEAMRQRQLAAEEEQRRREAEERVQKS 2140
Cdd:NF041483 103 TQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2141 LAAEEEA------ARQRKAALEEVERLKAK--VEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQEL 2212
Cdd:NF041483 181 AAARAEAerlaeeARQRLGSEAESARAEAEaiLRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2213 QQTLQQEQSMLERLR-----GEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRK 2287
Cdd:NF041483 261 RAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2288 EAEQEAARRAQAEQAALRQKQAAdAEMEKHKKFAEQTLrQKAQVEQELTTlRLQLEETDHQKSILDEELQRLKAEVTEAA 2367
Cdd:NF041483 341 AEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVL-TKASEDAKATT-RAAAEEAERIRREAEAEADRLRGEAADQA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2368 RQ-RSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAAR-----LSVAAQEAARLR 2441
Cdd:NF041483 418 EQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADADELR 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2442 ELAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQ 2520
Cdd:NF041483 498 STATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQAEAA 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2521 RQLE-MSAEAERlKLRVAEMSRAQARAEedAQRFRKQAEEIGEKLhRTELAtqEKVTLVQtleiqrQQSDHDAERLR--- 2596
Cdd:NF041483 575 EELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--ERIRTLQ------AQAEQEAERLRtea 642
|
650 660 670
....*....|....*....|....*....|....*.
gi 2124423178 2597 -----QAIAELEREKEKLKQEA--KLLQLKSEEMQT 2625
Cdd:NF041483 643 aadasAARAEGENVAVRLRSEAaaEAERLKSEAQES 678
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
183-287 |
6.12e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 45.34 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 183 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHR 260
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAK 84
|
90 100
....*....|....*....|....*..
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1481-1721 |
6.22e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1481 IKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQ 1560
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1561 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR-------AraeEAE 1633
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1634 AQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA 1713
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....*...
gi 2124423178 1714 LETAQRSA 1721
Cdd:COG3883 255 AGAAAGSA 262
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1674-1986 |
6.34e-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: 48.76 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1674 AAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEEHVAVAQL 1753
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEERE-QKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1754 REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1833
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1834 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAatQKRQELEAELAKVRAEMEV 1913
Cdd:pfam13868 188 RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE--LKERRLAEEAEREEEEFER 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1914 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKL 1986
Cdd:pfam13868 266 MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1498-1659 |
6.35e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 49.52 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1498 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1577
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1578 AEIQAKARQVEAAERSRLRIEEEirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1657
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 2124423178 1658 RQ 1659
Cdd:PRK12678 216 EE 217
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2331-2711 |
7.01e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2331 VEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKL-KARIEAENRALILRDKDNT 2409
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLlDEKKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2410 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLR------ELAEEDL--AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2481
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEvedlktELEKEKLknIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2482 -------QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaERQRQLEMSAE-AERLKLRVAEMSRAQARAEEDAQRF 2553
Cdd:pfam05483 521 diinckkQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD-EVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNL 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2554 RKQAEEIG---EKLHRTELATQEKVTL----VQTLEIQRQQSDHDAERLRQAIAEL------EREKEKLKQEAKLLQLKS 2620
Cdd:pfam05483 600 KKQIENKNkniEELHQENKALKKKGSAenkqLNAYEIKVNKLELELASAKQKFEEIidnyqkEIEDKKISEEKLLEEVEK 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2621 EEMQTVQQEQLLQETQALQQSFLSEKDTLL-----QRERFIEQEKAKL---EQLFQDEVAKAQKLREEQQRQQKQMEEEK 2692
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMekhkhQYDKIIEERDSELglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
410
....*....|....*....
gi 2124423178 2693 QQLVASMEEARQRQREAEE 2711
Cdd:pfam05483 760 KQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1337-1596 |
7.05e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1337 AVLAQTDLR---QRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVE 1413
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1414 ECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESVIQEYvdlrtRYSELTTLTSQYIKFISETLRRMEE 1493
Cdd:COG4942 94 ELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1494 EERLAEQQRAEERERLAAVEAALEKQRqlaeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR 1573
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 2124423178 1574 QSSEAEIQAKARQVEAAERSRLR 1596
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3944-3980 |
7.38e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.38e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 3944 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3980
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1575-1788 |
7.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1575 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1652
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1653 -ETQRKRQAEAELAV------------RVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAErARQVQVALETAQR 1719
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1720 saevELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1788
Cdd:COG3883 172 ----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1348-1663 |
8.02e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1348 ELEQLGR---QLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQL----RQEKALLEEIERHGEKV-------- 1412
Cdd:PLN03188 892 EITQLNRlvqQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFLEEELaslmHEHKLLKEKYENHPEVLrtkielkr 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1413 --EECQRFAKQY--------INAIKDYELQLVTYkaqLEPVASPAKKpkvqsgSESVIQ-EYVDLRTRYSELTTLT---- 1477
Cdd:PLN03188 972 vqDELEHYRNFYdmgerevlLEEIQDLRSQLQYY---IDSSLPSARK------RNSLLKlTYSCEPSQAPPLNTIPestd 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1478 -SQYIKFISETLRRMEEEER---LAEQQRAEererLAAVEAALEKQRQLAEAH---AQAKAQAEQEAQELQRRMQEEVAR 1550
Cdd:PLN03188 1043 eSPEKKLEQERLRWTEAESKwisLAEELRTE----LDASRALAEKQKHELDTEkrcAEELKEAMQMAMEGHARMLEQYAD 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1551 REEAAVDAQQQKRSIQEELQHLRQsseAEIQAKARQVE-------AAERSRLRIEEEIRVVRLQLETTERQ---RGGAE- 1619
Cdd:PLN03188 1119 LEEKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVEREKERRYLRDENKSLQaqlRDTAEa 1195
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1620 ----GELQALRARAEEA--EAQKR--QAQEEA-------ERLRRQVQDETQRKRQAEAE 1663
Cdd:PLN03188 1196 vqaaGELLVRLKEAEEAltVAQKRamDAEQEAaeaykqiDKLKRKHENEISTLNQLVAE 1254
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1499-1600 |
8.04e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 47.96 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1499 EQQRAEERERLAAVEAALEKQRQLAEAHAQAkaqaeqEAQELQRRMQEEVARREEaaVDAQQQKRSIQEELQHLRQSSEA 1578
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 2124423178 1579 EIQAKARQVEAAERSRLRIEEE 1600
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1971-2202 |
9.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1971 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE 2050
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2051 SELERQKGLVEDTLRQR-RQVEEEILALKVSFEKAAAGKAELEL--ELGRIRSNAEDTLRsKEQAELEAMRQRQLAAeee 2127
Cdd:COG4942 97 AELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELR-ADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 2128 qrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHA 2202
Cdd:COG4942 173 ----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
186-298 |
9.15e-05 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 45.80 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 186 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDY 256
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNS 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2124423178 257 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 298
Cdd:cd21323 104 ASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2088-2564 |
9.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2088 KAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERvQKSLAAEEEAARQRKAALEEVERLKAKVEE 2167
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2168 ARRLRERAEQESARqlqlaqdaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERA 2247
Cdd:COG4717 134 LEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2248 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKK-------- 2319
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2320 ----FAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAArqrsqveEELFSLRVQMEELGKLKARIE 2395
Cdd:COG4717 285 llalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2396 -AENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLkekmqAVQEATRLKA 2474
Cdd:COG4717 358 eLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2475 EAELLQQQKELAQEQARRLQEDKEQMAQQLEQ-ETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEED 2549
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKaelrELAEEWAALKLALELLEEAREEYREE 512
|
490
....*....|....*.
gi 2124423178 2550 AQ-RFRKQAEEIGEKL 2564
Cdd:COG4717 513 RLpPVLERASEYFSRL 528
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1505-1726 |
9.46e-05 |
|
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: 47.83 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1505 ERERLAAVEAALEKQRQLAEAHAQAKAQAEQ---EAQELQRRMQEEVarreeaavdaqqqkRSIQEELQHLRQSSEAEIQ 1581
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQlrtELQELEAQQQEEA--------------ESSREQLQELEEQLATERS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1582 AKarqvEAAERSRLRIEEEIRVVRLQLETTERQRggaegelqalraraeeaEAQKRQAQEEAERLRRQVQDETQRKRQaE 1661
Cdd:pfam09787 108 AR----REAEAELERLQEELRYLEEELRRSKATL-----------------QSRIKDREAEIEKLRNQLTSKSQSSSS-Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1662 AELAVRVKAEAEAAREKQRALQALEEFR----LQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1726
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKnslvLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLR 234
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1830-2198 |
9.91e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1830 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--HEAAAATQKRQELEA 1902
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1903 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAsRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvl 1982
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1983 aEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA--DIEERLAQLRKASESELERqkglv 2060
Cdd:PRK04863 418 -QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahSQFEQAYQLVRKIAGEVSR----- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2061 EDTLRQRRQVEEEILALKVSFEKAAAGKAELElELGRirsnaedtlRSKEQAELEAMRQRqlaaeeeqrrreAEERVQKS 2140
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLS-ELEQ---------RLRQQQRAERLLAE------------FCKRLGKN 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2141 LAAEEEAARQRKAALEEVERLKAKVEEArrlRERAEQESARQLQLAQDAAQKRLQAEE 2198
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1926-2074 |
1.03e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1926 RSTSEKSKQRLEAEASRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 2004
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 2005 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 2074
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1540-2173 |
1.08e-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: 48.56 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1540 LQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAE 1619
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1620 gELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELavRVKAEaeaarekqralQALEEFRLQAEEAERRL 1699
Cdd:pfam05483 159 -LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAE-----------NARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1700 RQAEAERARQV-----QVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVAVAQLREEAERRAQQQAEAERAREEA 1774
Cdd:pfam05483 225 QHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1775 ERELERwqlkaneaLRLRLQaEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRELAEQELEKQR---QLAEGT 1851
Cdd:pfam05483 295 TKELED--------IKMSLQ-RSMSTQKALEEDLQIAT------------KTICQLTEEKEAQMEELNKAKaahSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1852 AQQRLAAEQELIRLRAET-EQGEQQRQLLEEELARLQHEAAAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESR 1926
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRlEKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1927 STSEKSKQRLEAEASRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLkteaeialkek 2006
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL----------- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2007 eaENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEILA 2076
Cdd:pfam05483 500 --ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARS 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2077 LKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKsLAAEEEAARQR----- 2151
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfeeii 656
|
650 660 670
....*....|....*....|....*....|....*.
gi 2124423178 2152 --------------KAALEEVERLKAKVEEARRLRE 2173
Cdd:pfam05483 657 dnyqkeiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2417-2602 |
1.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2417 AEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELaqEQARRLQED 2496
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2497 KEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2576
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*.
gi 2124423178 2577 LVQTLEIQRQQSDHDAERLRQAIAEL 2602
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERA 792
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2319-2773 |
1.10e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2319 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAEN 2398
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2399 RALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2478
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2479 LQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2558
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2559 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQAL 2638
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2639 QQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQE 2718
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 2719 ELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKAL 2773
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
168-299 |
1.10e-04 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 45.43 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 168 LASPGPEPAPATDErdrvqKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR--- 237
Cdd:cd21325 12 LSSEGTQHSYSEEE-----KYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDErai 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 238 -EKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 299
Cdd:cd21325 84 nKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2322-2579 |
1.10e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2322 EQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS------QVEEELFSLRVQmeeLGKLKA 2392
Cdd:PRK11281 66 EQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQ---LQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2393 RIEAENRALIlrdkdnTQRVLQEEAEkmkhvaeeaARLSVAAQEAARLRELAEEDLAQQRALAEKmLKEKMQAVQEATrl 2472
Cdd:PRK11281 143 DLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALRPS-QRVLLQAEQALL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2473 kaEAELLQQQKELA-----QE--QARRlqEDKEQMAQQLEQETQGFQrtlEAERQRQLEMSAEAerlklrVAEMSRAQAR 2545
Cdd:PRK11281 205 --NAQNDLQRKSLEgntqlQDllQKQR--DYLTARIQRLEHQLQLLQ---EAINSKRLTLSEKT------VQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423178 2546 AEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVQ 2579
Cdd:PRK11281 272 ARIQANPLVAQELEINLQLSQRLLkATEKLNTLTQ 306
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1861-2174 |
1.16e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1861 ELIRLRAETEQGEQQ--RQLLEEELARLQHEAAAATQKRQeLEAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR 1935
Cdd:pfam05557 3 ELIESKARLSQLQNEkkQMELEHKRARIELEKKASALKRQ-LDRESDRNQElqkRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1936 LEAEASRFRELAEEAARLRALAE----------EAKRQRQLAEEDAARQRAEAERV---LAEKLAAIGEATRLKTEAEIA 2002
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREvisclknelsELRRQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2003 LKEKEAENERLRRLAedeafQRRRLEEQAAQHKADIEERLAQLRKAsESELERQKGLVE---DTLRQRRQVEEEILALKV 2079
Cdd:pfam05557 162 QSSLAEAEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPEL-EKELERLREHNKhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2080 S---FEKAAAGKAELELELGRIRS----------NAEDTLRSKE--QAELEAMRQRQLAAEEE----QRRREAEERVQKS 2140
Cdd:pfam05557 236 KlerEEKYREEAATLELEKEKLEQelqswvklaqDTGLNLRSPEdlSRRIEQLQQREIVLKEEnsslTSSARQLEKARRE 315
|
330 340 350
....*....|....*....|....*....|....
gi 2124423178 2141 LaaEEEAARQRKAALEEVERLKAKVEEARRLRER 2174
Cdd:pfam05557 316 L--EQELAQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2310-2551 |
1.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2310 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfslRVQMEELGK 2389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2390 LkARIEAENRALIlrdkDNTQRVLQEEaekmkHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMlkekmqavQEA 2469
Cdd:COG3883 91 R-ARALYRSGGSV----SYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKK--------AEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2470 TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQEtqgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEED 2549
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE----EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
..
gi 2124423178 2550 AQ 2551
Cdd:COG3883 229 AA 230
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1550-1681 |
1.21e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.74 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1550 RREEAAVD-AQQQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQletteRQRGGAEGELQAL 1625
Cdd:COG1566 79 TDLQAALAqAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1626 RARAEEAEAQKRQAQEEAERLRRQVQDETQrKRQAEAELavrvkAEAEAAREKQRA 1681
Cdd:COG1566 154 RAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQAEL 203
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4113-4147 |
1.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.22e-04
10 20 30
....*....|....*....|....*....|....*
gi 2124423178 4113 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4147
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1519-1652 |
1.35e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1519 QRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1597
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1598 EEEIRVVRLQLETTERQRGGaegelqalRARAEEAEAQKRQAQEEAERLRRQVQD 1652
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLRE--------EEELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1498-1612 |
1.35e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1498 AEQQRAEERERLAAVEAALEKQRQLAEAHAQ---AKAQAEQEAQELQRRM---------QEEVARREEAAVDAQQQKRSI 1565
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2124423178 1566 QEELQHLRQSSEAEiqakaRQVEAAERSRLRIEEEIRVVRLQLETTE 1612
Cdd:COG1566 168 QAQLAQAQAGLREE-----EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2348-2766 |
1.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2348 QKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALilrdKDNTQRVLQEEA--EKMKHVAE 2425
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA----SDHLNLVQTALRqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2426 EAARLSVAAQEAARLRELAEEDLAQQRALAEkmlkekmQAVQEATRLKA------EAELLQQQKELAQEQARRLQEDKEQ 2499
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSqladyqQALDVQQTRAIQYQQAVQALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2500 MAQ--QLEQET-QGFQRTLEAERQRQLEMSAEAERlKLRVAEMSRAQAraEEDAQRFRKQAEEIGEklhrtELATQEKVT 2576
Cdd:PRK04863 429 LCGlpDLTADNaEDWLEEFQAKEQEATEELLSLEQ-KLSVAQAAHSQF--EQAYQLVRKIAGEVSR-----SEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2577 LVQTLEIQRQQSDHdAERLRQAIAELEREkekLKQEAKLLQLKSEEMQtvqqeqllqetqALQQSFLSEKDTllqrERFI 2656
Cdd:PRK04863 501 LLRRLREQRHLAEQ-LQQLRMRLSELEQR---LRQQQRAERLLAEFCK------------RLGKNLDDEDEL----EQLQ 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2657 EQEKAKLEQLfQDEVAKAQKLREEQQRQQKQMeeekQQLVASMEEARQRQREAEEGVRRKQEELQLLEqqrqqqekllaE 2736
Cdd:PRK04863 561 EELEARLESL-SESVSEARERRMALRQQLEQL----QARIQRLAARAPAWLAAQDALARLREQSGEEF-----------E 624
|
410 420 430
....*....|....*....|....*....|
gi 2124423178 2737 ENQRLRERLQRLEEEHRAALAHSEEIAASQ 2766
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARK 654
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3907-3943 |
1.48e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.48e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 3907 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPAEEA 3943
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1825-1984 |
1.60e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEA 1902
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1903 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1978
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....*.
gi 2124423178 1979 ERVLAE 1984
Cdd:COG1842 207 EDELAA 212
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1250-1894 |
1.68e-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: 48.18 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1250 EVLKAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAE-AQQPMFDALRDELRGAQEVGERLQQRHGERDVEV------ 1321
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAEnARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliq 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1322 ---------------ERWRERVAQLLERwqavlaqTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLA 1386
Cdd:pfam05483 249 itekenkmkdltfllEESRDKANQLEEK-------TKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1387 DSRAVREQLRQEKALLEEIERHGE--------------KVEECQRFAKQYINAIKDyELQLVTYKAQlepvaspakkpKV 1452
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAahsfvvtefeattcSLEELLRTEQQRLEKNED-QLKIITMELQ-----------KK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1453 QSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETlrrmEEEERLAEQQRAEERErLAAVEAALEKQRQLAEAHAQAKAQ 1532
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK----KQFEKIAEELKGKEQE-LIFLLQAREKEIHDLEIQLTAIKT 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1533 AEQ----EAQELQRRMQEEVARREEaaVDAQQQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRlrieEEIRVVRlQL 1608
Cdd:pfam05483 465 SEEhylkEVEDLKTELEKEKLKNIE--LTAHCDKLLL-ENKELTQEASDMTLELKKHQEDIINCKK----QEERMLK-QI 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1609 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEef 1688
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH-- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1689 rlQAEEAERRLRQAEAERARqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLreeaerraqqqaeae 1768
Cdd:pfam05483 615 --QENKALKKKGSAENKQLN----AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL--------------- 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1769 rareeaERELERWQLKANEALRLRLQAEEVAQQKslaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1848
Cdd:pfam05483 674 ------LEEVEKAKAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2124423178 1849 EGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAT 1894
Cdd:pfam05483 737 QSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4422-4455 |
1.70e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....
gi 2124423178 4422 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4455
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2343-2625 |
1.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2343 EETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDntqrvLQEEAEKMKH 2422
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS-----KRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2423 VAEeaarlsvaaqeaaRLRELAEEdlaqqralaEKMLKEKmqaVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2502
Cdd:PRK03918 264 LEE-------------RIEELKKE---------IEELEEK---VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2503 qLEQETQGFQRTL-EAErqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFrkqaEEIGEKLHRTElatqekvtlvqtl 2581
Cdd:PRK03918 319 -LEEEINGIEERIkELE-----EKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELE------------- 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2124423178 2582 EIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2625
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1528-1684 |
1.81e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.03 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1528 QAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER---------SRLRIE 1598
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAqlaqaqidlARRRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1599 EEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ-VQDETQRKRQAEAELAvrvKAEAEAAR 1676
Cdd:pfam00529 133 APIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEAEAELK---LAKLDLER 209
|
....*...
gi 2124423178 1677 EKQRALQA 1684
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1559-1710 |
1.85e-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: 46.46 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG--ELQALRARAEEAE 1633
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1634 AQKRQAQEEAERLRRQVQdetqrkrQAEAELAvrvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV 1710
Cdd:COG1579 103 RRISDLEDEILELMERIE-------ELEEELA---ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3831-3867 |
1.90e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.90e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 3831 RYLYGTGCVAGVYVPGSRQTLTIYQALKKGLLSAEVA 3867
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1632-1752 |
1.97e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1632 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQ 1711
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423178 1712 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVAVAQ 1752
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKK 178
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
328-405 |
2.02e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 43.45 E-value: 2.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 328 DNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 405
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1487-1726 |
2.21e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 46.95 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1487 TLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQ-EAQELQRRMQEEVARRE------EAAVDAQ 1559
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQaRAQLAQAEAQLAQARNAlalllgLPPPAPL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1560 QQKRSIQEELQHLRQSSEAEIQAKAR--QVEAAERSRLRIEEEIRVVRLQL----------ETTERQRGGAEGELQ---- 1623
Cdd:COG1538 164 DLPDPLPPLPPLPPSLPGLPSEALERrpDLRAAEAQLEAAEAEIGVARAAFlpslslsasyGYSSSDDLFSGGSDTwsvg 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1624 -----------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQ-ALEEFR-- 1689
Cdd:COG1538 244 lslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAEEALElARARYRag 323
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2124423178 1690 ----LQAEEAERRLRQAEAERarqvqVALETAQRSAEVELQ 1726
Cdd:COG1538 324 laslLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1489-1659 |
2.28e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1489 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQlAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1568
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1569 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLETTERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRR 1648
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 2124423178 1649 QVQDETQRKRQ 1659
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2146-2758 |
2.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2146 EAARQRKAALEEV----ERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEqs 2221
Cdd:COG4913 245 EDAREQIELLEPIrelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR-- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2222 mlERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVE-EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEqeaarraqae 2300
Cdd:COG4913 323 --EELDELEAQIRGNGGDRLEQLEREIERLERELEERErRRARLEALLAALGLPLPASAEEFAALRAEAA---------- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2301 qaalRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEEL--- 2377
Cdd:COG4913 391 ----ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAELpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2378 -------------------------FSLRVQMEELGKLKARIEAENRALILRdkdnTQRVLQEEAEKMKHVAEE---AAR 2429
Cdd:COG4913 464 gelievrpeeerwrgaiervlggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdslAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2430 LSVAAQEAarlRELAEEDLAQQRALA----EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE 2505
Cdd:COG4913 540 LDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2506 QETQGFQRTLEAERQRQLEMSAEAERL--KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlVQTLEI 2583
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD----LAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2584 QRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFlsekDTLLQRERFIEQEKAKL 2663
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2664 EQLfQDEVAKAQKLREEQQrqqkqmeeekQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEEN-QRLR 2742
Cdd:COG4913 769 ENL-EERIDALRARLNRAE----------EELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeERFK 837
|
650
....*....|....*.
gi 2124423178 2743 ERLQRLEEEHRAALAH 2758
Cdd:COG4913 838 ELLNENSIEFVADLLS 853
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1848-2344 |
2.40e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.55 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1848 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV----------RAEMEVLLAS 1917
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1918 KARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1997
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1998 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 2077
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2078 KVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE 2157
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2158 VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAA 2237
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2238 EEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2317
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 2124423178 2318 KKFAEQTLRQKAQVEQELTTLRLQLEE 2344
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
181-294 |
2.41e-04 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 43.82 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 181 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQ 251
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCN 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2124423178 252 IALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21329 73 YAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1486-1675 |
2.48e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQRAEERERLAAVEAALekqrqlaeAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1565
Cdd:PRK05035 524 EARKAQARARQAEKQAAAAADPKKAAVAAAI--------ARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1566 QEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAE 1644
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE 670
|
170 180 190
....*....|....*....|....*....|.
gi 2124423178 1645 rlrrqvQDETQRKRQAEAELAvRVKAEAEAA 1675
Cdd:PRK05035 671 ------EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1825-2018 |
2.55e-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: 46.84 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1904
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1905 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1984
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 2124423178 1985 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAE 2018
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
526-1475 |
2.63e-04 |
|
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: 47.36 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 526 EREKQLRSEFERLERLQRIVSKLqmeaglcEEQLNqadallqsdvRLLAAGKAPQRAGEVERDLDKADsmIRLLFNDVQT 605
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNEL-------ERQLK----------SLERQAEKAERYKELKAELRELE--LALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 606 LKDGRhpqgeqmyrrvyrlhERLVAIRTEYNLRLKAGVAAPVTQVTQVTlQSTQRRPELEDSTLRYLQDLLAWVEENQRr 685
Cdd:TIGR02168 237 LREEL---------------EELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELYALANEISR- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 686 vdgaewgvdlpsveaqlgshrgLHHSIEEFRAKIERARTDEGQLSpatrgAYRDCLGRLDLQYAKLLNSSKGRLRSLESL 765
Cdd:TIGR02168 300 ----------------------LEQQKQILRERLANLERQLEELE-----AQLEELESKLDELAEELAELEEKLEELKEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 766 YSFVAAATKELMWL---SEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVES 842
Cdd:TIGR02168 353 LESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 843 FQ-AALQTQwswmlqlcccIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKytcdrsitVTRLEDLLQDAQDERDQL 921
Cdd:TIGR02168 433 AElKELQAE----------LEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQLQARLDSL 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 922 NEYRGHLSGLARRAKAIvqLKPRNPAHPVRGRVPLLAVCD--YKQVEVTVHKGDECQLVGPAQPSHWKVVSSSgSEAAVP 999
Cdd:TIGR02168 495 ERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVDegYEAAIEAALGGRLQAVVVENLNAAKKAIAFL-KQNELG 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1000 SVCFLVPPPNQEAQEAITRLEA-QHQALVTLWHQLHVDMKSllawqSLSRDVQLIRSWSLVTfrtmkpEEQRQALRSLEL 1078
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREIlKNIEGFLGVAKDLVKFDP-----KLRKALSYLLGGVLVV------DDLDNALELAKK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1079 HYQAFLRDSQD----------AGGFGPED--RLQAEREYGSCSHHYQQLLQSLEQGEQeesrcqrcisELKDIRLQLEAC 1146
Cdd:TIGR02168 641 LRPGYRIVTLDgdlvrpggviTGGSAKTNssILERRREIEELEEKIEELEEKIAELEK----------ALAELRKELEEL 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1147 ETRTVHRLRLPLDKEpaRECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRS 1226
Cdd:TIGR02168 711 EEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTE-------------LEAEIEELEERLEEAEE 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1227 LSAIYLEKLKTISLVIRsthGAEEVLKAHEEQLKEAQAVPATLPELEATKA-ALKKLRAQAEAQQPMFDALRDELRGAQE 1305
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANLReRLESLERRIAATERRLEDLEEQIEELSE 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1306 VGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLgawLQDAKRRQEQIQAMVL 1385
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL---RRELEELREKLAQLEL 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1386 ADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakkpkvqsgSESVIQEYVD 1465
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV------------NLAAIEEYEE 997
|
970
....*....|
gi 2124423178 1466 LRTRYSELTT 1475
Cdd:TIGR02168 998 LKERYDFLTA 1007
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2304-2711 |
2.65e-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: 47.41 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAadaEMEKHKKFAEQTLR--QKAQVEQELTTLRLQLE------------ETDHQKSILDEELQRLKAEVTEAARQ 2369
Cdd:pfam05483 101 LKQKEN---KLQENRKIIEAQRKaiQELQFENEKVSLKLEEEiqenkdlikennATRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2370 RSQVEEELFSLRVQMEE--LGKLKARIEAENRALILRDKdntqrvLQEEAEKMKHVAEEAARlsvaaqeaarlrelAEED 2447
Cdd:pfam05483 178 REETRQVYMDLNNNIEKmiLAFEELRVQAENARLEMHFK------LKEDHEKIQHLEEEYKK--------------EIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2448 LAQQRALAEKMLKEKMQAVQEATRLkaeaellqqqkelaqeqarrLQEDKEQmAQQLEQETQGFQRTLEAERQRQLEMSA 2527
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFL--------------------LEESRDK-ANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2528 EAERLKLRVAEMSRAQARAEEDAQRFRK-----------QAEEIGEKLHRTELATQEKVTLVQTLE----IQRQQSDHDA 2592
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEellrTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2593 ERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVqqeqllqetqalqQSFLSEKDTLLqrerfieQEKAKLEQLFQDEVA 2672
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEEL-------------KKILAEDEKLL-------DEKKQFEKIAEELKG 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 2124423178 2673 KAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEE 2711
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2307-2522 |
2.80e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2307 KQAADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2369
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2370 RSQVEEElfslRVQMEELGKlKARIEAENRAL--ILRDKDNTQRVLQE--EAEKMKHVAEEA-ARLSVAAQEAA-----R 2439
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKqlADAKQRHVDNQQkVKDAVAKSEAGvaqgeQ 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2440 LRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeqmAQQLEQETQGFQRTLEAER 2519
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK---ANQAQADAKGAKQDESDKP 1780
|
...
gi 2124423178 2520 QRQ 2522
Cdd:NF012221 1781 NRQ 1783
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3535-3568 |
2.89e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.89e-04
10 20 30
....*....|....*....|....*....|....
gi 2124423178 3535 LLEAQAATGFLVDPVRNQRLYVHEAVKAGIVGPE 3568
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2442-2566 |
2.91e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.42 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2442 ELAEEDLAQQRALAEKMLK-----EKMQAVQEATRLKAEAEllQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLE 2516
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILQadqalTEKEKEIEAERAKAEAA--EQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKME 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2517 AERQRQLEmsaEAERLklrVAEMSRAQARAEEdaQRFRKQAEEIGEKLHR 2566
Cdd:cd16269 248 EERENLLK---EQERA---LESKLKEQEALLE--EGFKEQAELLQEEIRS 289
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1824-1971 |
2.97e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEAAAATQKRQELEA 1902
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1903 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEASRF-RELAEEAARLRALAEEAKRQRQLAEEDA 1971
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLEH 506
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2325-2665 |
2.98e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2325 LRQKAQVEQ---ELTTLRLQLEEtdhQKSILDEelqrLKAEVTEAARQRSQVEEELFSLRVQMEELgkLKARIEAENRAL 2401
Cdd:PRK04863 344 LRQQEKIERyqaDLEELEERLEE---QNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADY--QQALDVQQTRAI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2402 ILRdkdNTQRVLqEEAEKMKHVAEEAARLSVAAQEAARlrelAEEDLAQQRALaekMLKEKMQAVQEATRLKAEA-ELLQ 2480
Cdd:PRK04863 415 QYQ---QAVQAL-ERAKQLCGLPDLTADNAEDWLEEFQ----AKEQEATEELL---SLEQKLSVAQAAHSQFEQAyQLVR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2481 Q-----QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEmsAEAERLKLRVAEMSRAQARAEEDAQRFRK 2555
Cdd:PRK04863 484 KiagevSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2556 QAEEigeklhRTELATQEKVTLVQTLEIQRQQsdhdAERLRQAIAELE-REKEKLKQEAKLLQLKSEEMQTVQQEQLLQE 2634
Cdd:PRK04863 562 ELEA------RLESLSESVSEARERRMALRQQ----LEQLQARIQRLAaRAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
330 340 350
....*....|....*....|....*....|....*
gi 2124423178 2635 TQALQQ----SFLSEKDTLLQRERFIEQEKAKLEQ 2665
Cdd:PRK04863 632 YMQQLLererELTVERDELAARKQALDEEIERLSQ 666
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2304-2665 |
3.00e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.53 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTT---LRLQLEET--DHQKSILDEELQRLKAEVTEAARQRSQVEEELF 2378
Cdd:pfam12128 451 LRLNQATATPELLLQLENFDERIERAREEQEAANaevERLQSELRqaRKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2379 S--------LRVQM----EELGKLKARieaenrALILRDKDNTQRVLQEEAEKMK------HVAEEAARLSVAAQEAARL 2440
Cdd:pfam12128 531 PqagtllhfLRKEApdweQSIGKVISP------ELLHRTDLDPEVWDGSVGGELNlygvklDLKRIDVPEWAASEEELRE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2441 R-ELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaER 2519
Cdd:pfam12128 605 RlDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ER 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2520 QRQLEmsAEAERLKLRVAEMSRAQAR--AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQ 2597
Cdd:pfam12128 684 LNSLE--AQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLA 761
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2598 AIAELEREKEKLKQEAKLLQLKSEEMQtVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQ 2665
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIERIA-VRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ 828
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1510-1707 |
3.18e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 46.57 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1510 AAVEAALEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVAR--REEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKAR 1585
Cdd:COG1538 4 ELIERALANNPDLRAARARvEAARAQLRQARAGLLPSQELDLggKRRARIEaAKAQAEAAEADLRAARLDLAAEVAQAYF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1586 QVEAAERSRLRIEEEIRVVRLQLETTERQR---GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1662
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYeagLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNALALLLGLPPPAPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2124423178 1663 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERA 1707
Cdd:COG1538 164 DLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAEAEIG 208
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1467-1753 |
3.30e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1467 RTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE 1546
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1547 EVARREEAavdaQQQKRSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR 1626
Cdd:COG4372 92 AQAELAQA----QEELESLQEEAEELQE-----------ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1627 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAER 1706
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2124423178 1707 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1753
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2145-2678 |
3.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2145 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHA--FAVQQKEQELQQTLQQEQSM 2222
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrlWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2223 LERLRGEAEAARRAAEEAEEARERAEREAAQS-RRQVEEAER----LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRA 2297
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEReierLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2298 QAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEEL 2377
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2378 ----------------------------FSLRVQMEELGKLKARIEAENRALILRdkdnTQRVLQEEAEKMKHVAEE--- 2426
Cdd:COG4913 461 pfvgelievrpeeerwrgaiervlggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdsl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2427 AARLSVAAQEAarlRELAEEDLAQQRALA----EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2502
Cdd:COG4913 537 AGKLDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2503 QLEQETQGFQRTLEAERQRQLEMSAEAERL--KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlVQT 2580
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD----LAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2581 LEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFlsekDTLLQRERFIEQEK 2660
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVER 765
|
570
....*....|....*...
gi 2124423178 2661 AKLEQLfQDEVAKAQKLR 2678
Cdd:COG4913 766 ELRENL-EERIDALRARL 782
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3241-3277 |
3.52e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.52e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 3241 KLLSAEKAVTGYKDPYSGKSVSLFQALKKGLIPKEQG 3277
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1488-1677 |
3.76e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.53 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1488 LRRMEEEERLAEQQRAEERERLAAVEAA-LEKQRQLAEAHAqakaqaEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1566
Cdd:pfam05262 203 LKERESQEDAKRAQQLKEELDKKQIDADkAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1567 EELQHLRQSSEAEIQAKARQVEAAERsrlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRqaQEEAERL 1646
Cdd:pfam05262 277 ENQKREIEKAQIEIKKNDEEALKAKD-------------------------HKAFDLKQESKASEKEAEDK--ELEAQKK 329
|
170 180 190
....*....|....*....|....*....|..
gi 2124423178 1647 RRQVQDETQR-KRQAEAElavrVKAEAEAARE 1677
Cdd:pfam05262 330 REPVAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2259-2606 |
3.77e-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: 46.07 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2259 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKhkkfAEQTLRQKAQVEQELTTL 2338
Cdd:pfam13868 3 ENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEE----EEKEEERKEERKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2339 RLQLEETDHQKSILDEELQRLKAEVTEAARQrsqveeelfslrVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAE 2418
Cdd:pfam13868 79 EEQIEEREQKRQEEYEEKLQEREQMDEIVER------------IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2419 KMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAlAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2498
Cdd:pfam13868 147 KEEEREEDERILEYLKEKAEREEEREAEREEIEEE-KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2499 QMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE----DAQRFRKQAEEIGEKLHRTELATQEK 2574
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEieqeEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
330 340 350
....*....|....*....|....*....|..
gi 2124423178 2575 VTLVQTLEIQRQQSDHDAERLRQAIAELEREK 2606
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1815-1978 |
3.94e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.40 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1815 EAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQElirlrAETEQGEQQRQL-LEEELARLQHEAAAA 1893
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA-----YEIAEANAEREVqRQLEIAEREREIELQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1894 TQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEedAA 1972
Cdd:COG2268 296 EKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IA 370
|
....*.
gi 2124423178 1973 RQRAEA 1978
Cdd:COG2268 371 EAAAKP 376
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1513-2013 |
4.04e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1513 EAALEKQRQLAEAhAQAKAQAEQeAQELQRRMQEeVARREEAAVDAQQQKRSIQE---ELQHLRQSSEAEiqakarqvea 1589
Cdd:PRK10929 25 EKQITQELEQAKA-AKTPAQAEI-VEALQSALNW-LEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1590 aersrlriEEEIRVVRLQLETterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRrQVQDETQRKRQAEAElAVRVK 1669
Cdd:PRK10929 92 --------RDEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAR-EISDSLSQLPQQQTE-ARRQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1670 AEAEaarekqRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSA--EVELQSKRASFAEK-TAQLERTLQee 1746
Cdd:PRK10929 154 NEIE------RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1747 hvavaqlreeaerraqqqaeaerareeaerelerwqlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgka 1826
Cdd:PRK10929 226 -----------------------------------------ALRNQLNSQ------------------------------ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1827 eeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQHEAAAATQK-RQELEA--- 1902
Cdd:PRK10929 235 -----RQRE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlre 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1903 ---ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEASRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAE 1977
Cdd:PRK10929 308 qsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAE 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1978 AERVLAEKLAA---------------IGEATRLK---TEAEIALKE-KEAENERL 2013
Cdd:PRK10929 377 QNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1123-1753 |
4.51e-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: 46.89 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1123 EQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPE 1202
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1203 PSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKL 1282
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1283 RAQAEAQQPMFDALRDELRGAQE-------VGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQ 1355
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1356 LRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQR---FAKQYINAIKDYELQ 1432
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvVEGILKDTELTKLKE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1433 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERlaEQQRAEERERLAAV 1512
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK--KEQREKEELKKLKL 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1513 EAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEA------AVDAQQQKRSIQEELQHLRQSSEAEIQAKARQ 1586
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeekeeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1587 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDETQRKRQAEAEL 1664
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEELLQELLLKEE 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1665 AVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1744
Cdd:pfam02463 878 ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
|
....*....
gi 2124423178 1745 EEHVAVAQL 1753
Cdd:pfam02463 958 EEERNKRLL 966
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1865-2119 |
4.57e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1865 LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAemevlLASKARAEEEsrstsekskqrLEAEasrfR 1944
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA-----AALQPGEEEE-----------LEEE----R 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1945 ELAEEAARLRALAEEAkrQRQLAEED--AARQRAEAERVLaEKLAAIGE-----ATRLkTEAEIALKEKEAEnerLRRLA 2017
Cdd:COG0497 216 RRLSNAEKLREALQEA--LEALSGGEggALDLLGQALRAL-ERLAEYDPslaelAERL-ESALIELEEAASE---LRRYL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2018 EDEAFQRRRLEEqaaqhkadIEERLAQLRKaseselerqkglvedtLRQRRQVE-EEILALkvsfekaaagKAELELELG 2096
Cdd:COG0497 289 DSLEFDPERLEE--------VEERLALLRR----------------LARKYGVTvEELLAY----------AEELRAELA 334
|
250 260
....*....|....*....|...
gi 2124423178 2097 RIrSNAEDTLRSKEQAELEAMRQ 2119
Cdd:COG0497 335 EL-ENSDERLEELEAELAEAEAE 356
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1517-1648 |
4.57e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.88 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1517 EKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1594
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 1595 LRIEEEIRVVRLQLETTERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1648
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3164-3201 |
4.68e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.68e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2124423178 3164 RQALRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVA 3201
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2384-2551 |
4.81e-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: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2384 MEELGKLKARIEAENRALILRDKdntqRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKM 2463
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQK----KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2464 QAVQEATR-LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRvAEMSRA 2542
Cdd:TIGR02794 125 KAKQAAEAkAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK-AEAAKA 203
|
....*....
gi 2124423178 2543 QARAEEDAQ 2551
Cdd:TIGR02794 204 KAAAEAAAK 212
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2838-2876 |
4.83e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.39 E-value: 4.83e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 2838 YLQGRSSIAGLLLKPANEKLSIYTALRRQLLSPGTALIL 2876
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1249-2072 |
4.96e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1249 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRER 1327
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1328 VAQLLERWQAvlAQTDLRQRELEQLGRQLRYYREsadplgawlqdAKRRQEQIQAMvlaDSRAVREQLRQEKALLEE--- 1404
Cdd:TIGR00606 324 CQRELEKLNK--ERRLLNQEKTELLVEQGRLQLQ-----------ADRHQEHIRAR---DSLIQSLATRLELDGFERgpf 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1405 IER-----HGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTRYSELTTLT 1477
Cdd:TIGR00606 388 SERqiknfHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1478 --SQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREeaa 1555
Cdd:TIGR00606 468 gsSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK--- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1556 VDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI---EEEIRVVRLQLETTERQRGGAEGELQALRAR---- 1628
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQlssy 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1629 ---------AEEAEAQKRQAQEEAERLRRQVQ-------------DETQRKRQAEAELAVRV-KAEAEAAREKQRALQAL 1685
Cdd:TIGR00606 625 edklfdvcgSQDEESDLERLKEEIEKSSKQRAmlagatavysqfiTQLTDENQSCCPVCQRVfQTEAELQEFISDLQSKL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1686 EEFRLQAEEAERRLRQAEAERARQVQVAletAQRSAEVELQSKR-ASFAEKTAQLERTLQEEHVAVAQlREEAERRAQQQ 1764
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMLGLA---PGRQSIIDLKEKEiPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPE 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1765 AEAERAREEAERELERWQLKANEALRlrlqaeEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1844
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQMELKDVER------KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1845 RQLAEGTAQQRLaaeQELIRLRAETEQGEQQRQLLEEELARLQHEA----AAATQKRQE---LEAELAKVRAEMEVLLAS 1917
Cdd:TIGR00606 855 QQEQIQHLKSKT---NELKSEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISS 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1918 K----ARAEEESRSTSEKSKQRLEAEASRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE----- 1977
Cdd:TIGR00606 932 KetsnKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqk 1011
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1978 -AERVLAEKLaaigeaTRLKTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASESELERQ 2056
Cdd:TIGR00606 1012 iQERWLQDNL------TLRKRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQ 1077
|
890
....*....|....*.
gi 2124423178 2057 KGLVEDTLRQRRQVEE 2072
Cdd:TIGR00606 1078 KGYEKEIKHFKKELRE 1093
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1512-1711 |
5.03e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1512 VEAALEKQRQL----AEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQV 1587
Cdd:PRK12678 52 IAAIKEARGGGaaaaAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1588 EAAERSRLRieeeirvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElavr 1667
Cdd:PRK12678 132 ERGEAARRG-------------AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRRE---- 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423178 1668 vkaeaEAAREKQRALQaleefRLQAEEAERRLRQAEAERARQVQ 1711
Cdd:PRK12678 195 -----ERGRDGDDRDR-----RDRREQGDRREERGRRDGGDRRG 228
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2308-2527 |
5.06e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.52 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2308 QAADAEMEKHKKFAEQTLRQKAQVEQEL------------TTLRLQLEETDHQKSILDEELQRLKAEV----TEAARQRS 2371
Cdd:pfam09787 3 ESAKQELADYKQKAARILQSKEKLIASLkegsgvegldssTALTLELEELRQERDLLREEIQKLRGQIqqlrTELQELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2372 QVEEELFSLRvqmEELGKLKARIEAENRAliLRDKDNTQRVLQEEaekMKHVAEEAARLSVAAQEAARLRELAEEDLAQQ 2451
Cdd:pfam09787 83 QQQEEAESSR---EQLQELEEQLATERSA--RREAEAELERLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2452 raLAEKMLKEKMQAVQEAtRLKAEAELLQQQkelaQEQARRLQEDKEQMAQQLEQ-ETQGFQRTLEAERQRQLEMSA 2527
Cdd:pfam09787 155 --LTSKSQSSSSQSELEN-RLHQLTETLIQK----QTMLEALSTEKNSLVLQLERmEQQIKELQGEGSNGTSINMEG 224
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1934-2048 |
5.27e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.48 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1934 QRLEAEASRFRELAEEAARLRALAEEAKRQRQlaeedaarqraeAERVLAEKLAAIGEATRLKTEAEIA-LKEKEAENER 2012
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQ------------QELVALEGLAAELEEKQQELEAQLEqLQEKAAETSQ 212
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2124423178 2013 LRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA 2048
Cdd:PRK11448 213 ERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKA 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1213-1429 |
5.51e-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: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1213 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPM 1292
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1293 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdlrQRELEQLGRQLRYYRESADPLGAWLQD 1372
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1373 AKRRQEQIQAMVladsRAVREQLRQE-KALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1429
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1825-2060 |
5.54e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 46.21 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQ-RQLLEEELARLqHEAAAATQKRQEleae 1903
Cdd:pfam05911 10 KVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKI-HDVVLKKTKEWE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1904 laKVRAEMEVLLAskaraeeesrstsEKSKQRLEAEasrfrelAEEAARLRALAEEAKRQRQLAEEdaaRQRAEAE-RVL 1982
Cdd:pfam05911 85 --KIKAELEAKLV-------------ETEQELLRAA-------AENDALSRSLQERENLLMKLSEE---KSQAEAEiEAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1983 AEKL-AAIGEATRLKTEAEIALKEKEAENErlrrlaEDEaFQRRRLEEQAAQHKADIeERLAQLrkasESELERQKGLV 2060
Cdd:pfam05911 140 KSRLeSCEKEINSLKYELHVLSKELEIRNE------EKN-MSRRSADAAHKQHLESV-KKIAKL----EAECQRLRGLV 206
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1559-1728 |
6.14e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1559 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL-------RIE-EEIRVVRLQLETTerqrgGAEGELQAlRARAE 1630
Cdd:PTZ00491 647 DSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLerqkmhdKAKaEEQRTKLLELQAE-----SAAVESSG-QSRAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1631 -EAEAQKRQAQEEAErlrrqVQdetQRKRQAEAElavRVKAEAEAAREKQRALQALEEFRLQAE---EAERRLRQAEAER 1706
Cdd:PTZ00491 721 aLAEAEARLIEAEAE-----VE---QAELRAKAL---RIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATK 789
|
170 180
....*....|....*....|....*.
gi 2124423178 1707 ARQVQVAL--ET--AQRSAEVELQSK 1728
Cdd:PTZ00491 790 FERIVEALgrETliAIARAGPELQAK 815
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4532-4569 |
6.16e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.16e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2124423178 4532 QRFLEVQYLTGGLIEPDVPGRVPLDEALQRGTVDARTA 4569
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2315-2666 |
6.19e-04 |
|
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: 46.17 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2315 EKHKKFAEQTLRQKAQVEQ---ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLK 2391
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2392 ARI-EAENRALILRD-KDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQqralAEKMLKEKMQAVQEa 2469
Cdd:TIGR04523 218 SQIsELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQLNQ- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2470 trLKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLEQETQGFQRTLE------AERQRQL-EMSA 2527
Cdd:TIGR04523 293 --LKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTnsesenSEKQRELeEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2528 EAERLKlrvaemsRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKE 2607
Cdd:TIGR04523 371 EIEKLK-------KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2608 KLKQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQL 2666
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDN-TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1630-1709 |
6.45e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1630 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL------AVRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQA 1702
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqqeLVALEGLAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 2124423178 1703 EAERARQ 1709
Cdd:PRK11448 218 RKEITDQ 224
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1522-1701 |
6.53e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.61 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1522 LAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKarqveaaersrlrieeei 1601
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1602 rvvrlQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR-----KRQAEAELAV---RVKAEAE 1673
Cdd:COG3524 222 -----LIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARltgasGGDSLASLLAeyeRLELERE 296
|
170 180
....*....|....*....|....*....
gi 2124423178 1674 -AAREKQRALQALEEFRLqaeEAERRLRQ 1701
Cdd:COG3524 297 fAEKAYTSALAALEQARI---EAARQQRY 322
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
186-298 |
6.64e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 43.07 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 186 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIAL 254
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2124423178 255 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 298
Cdd:cd21324 102 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2339-2569 |
6.66e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2339 RLQLEETDHQKSildEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAlilrdkdntqrvlQEEAE 2418
Cdd:PRK09510 66 RQQQQQKSAKRA---EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA-------------KQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2419 KMKHVAEEAARLSVAAQEAARLRELAEEDLAQQrALAEKMLKEKMQAVQeatrlKAEAEllqQQKELAQEQARRLQEDKE 2498
Cdd:PRK09510 130 KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAK-----KAAAE---AKKKAEAEAAAKAAAEAK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423178 2499 QMAQQleqetqgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2569
Cdd:PRK09510 201 KKAEA------------EAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1829-2771 |
6.71e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1829 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAeLAKVR 1908
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1909 AEMEVLLAS-KARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1980
Cdd:TIGR00606 279 KQMEKDNSElELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1981 VLAEKLAAIGEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---AQHKADIEERLAQLRKASESELERQK 2057
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2058 GLVEDTLRQRRQVEEEILALKVSFEK----AAAGKAELELELGRIRSNAEDTLrSKEQAELEAMRQRQLAAEEEQRRREA 2133
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKElqqlEGSSDRILELDQELRKAERELSK-AEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2134 EErvqKSLAAEEEAARQRKAALEEVERL-KAKVEEARRLRERAEQESARQLQLAQDAAQKRlQAEEKAHAFAVQQKEqel 2212
Cdd:TIGR00606 516 KL---RKLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKSKEINQ--- 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2213 qqtlqqeqsMLERLRgeaeaarraaeeaeeARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAeklrkeaeqe 2292
Cdd:TIGR00606 589 ---------TRDRLA---------------KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS---------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2293 aarraqaeqaalrqkQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2372
Cdd:TIGR00606 635 ---------------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2373 VEEELFSLRVQMEELGKLKARIEAEnRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSvaaqeaarlRELAEE--DLAQ 2450
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKR-RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN---------RDIQRLknDIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2451 QralaEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEA 2529
Cdd:TIGR00606 770 Q----ETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2530 ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLeiqrQQSDHDAERLRQAIAELEREKEKL 2609
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV----QSLIREIKDAKEQDSPLETFLEKD 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2610 KQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTllqrERFIEQEKAKLEQLFQDEVAKaqklreeqqrqqkqme 2689
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI----ENKIQDGKDDYLKQKETELNT---------------- 981
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2690 eekqqLVASMEEARQRQREAEEGVRrkqeeLQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATA 2769
Cdd:TIGR00606 982 -----VNAQLEECEKHQEKINEDMR-----LMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQ 1051
|
..
gi 2124423178 2770 VK 2771
Cdd:TIGR00606 1052 MK 1053
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2325-2622 |
6.88e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2325 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIeaenralil 2403
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2404 RDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2483
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2484 ELAQEQARRLQEDKEQMA--QQLEQETQGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2561
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILelEGYEMDYNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2562 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLRQAIAELEREKEKL 2609
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 2124423178 2610 KQEAKllQLKSEE 2622
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1492-1753 |
7.13e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1492 EEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEE-------VARREEAAVDAQQQKRS 1564
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1565 IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEI--RVVRLQLETTE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1641
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1642 EAERLRRQV-QDETQRKRQAEAELAVRVKAEAEAAREK---QRALQALEEFRLQAEEAERRLRQaeAERARQVQVALETA 1717
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpEVKSQNGEEEVTKLKVTTKRRQG--GLSQSQEREEEAEV 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 2124423178 1718 QRSAEVELQSKRASFAEKTAQ-LERTLQEEHVAVAQL 1753
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEeFEKLRQKQQEAELEL 279
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1296-1664 |
7.43e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1296 LRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLgrqLRYYRESADPLGAWLQDAKR 1375
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1376 RQEQIQAMVLADSRAVREQLRQEKALLEEI----ERHGEKVEECQRF---AKQYINAIKDYELQLVTYKAQLEPVASPAK 1448
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIktltQRVLERETELERMkerAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1449 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAeERERLAAVEAALEKQRQLAEAH 1526
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQK----LTTAHRKEAENEALLEELRS-LQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1527 AQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEiRVVRL 1606
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1607 QLETT-ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL 1664
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1852-2198 |
7.58e-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: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1852 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAA----TQKRQELEAELAKVRAEME----VLLASKARAEE 1923
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErlaeLEAKRQAEEEAREAKAEAEqraaELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1924 ESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA 1999
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKaeeaKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2000 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKV 2079
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2080 SFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVE 2159
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 2124423178 2160 RLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2198
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALA 359
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1465-1737 |
7.71e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1465 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE---QEAQELQ 1541
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1542 RRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSS----------EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETT 1611
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRkqleaqiaelQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1612 ERQRggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQ 1691
Cdd:COG4372 177 SEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2124423178 1692 AEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1737
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2419-2594 |
8.01e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 45.63 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2419 KMKHvAEEAARLSV--AAQEAARLRELAEEDLAQQRALAEKMLKEK-----MQAVQEAT--RLKAEAELLQQQKELAQEQ 2489
Cdd:PRK00106 25 KMKS-AKEAAELTLlnAEQEAVNLRGKAERDAEHIKKTAKRESKALkkellLEAKEEARkyREEIEQEFKSERQELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2490 AR---------RLQED---KEQMAQQLEQETQGFQRTLEaERQRQLEMSAEAERLKL-RVAEMSRAQARAEEDAQRFRKQ 2556
Cdd:PRK00106 104 SRlteratsldRKDENlssKEKTLESKEQSLTDKSKHID-EREEQVEKLEEQKKAELeRVAALSQAEAREIILAETENKL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423178 2557 AEEIGEKLHRTELATQEKVT------LVQTLeiQRQQSDHDAER 2594
Cdd:PRK00106 183 THEIATRIREAEREVKDRSDkmakdlLAQAM--QRLAGEYVTEQ 224
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1499-1606 |
8.52e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1499 EQQRAEERERLAAVEAALE-----------KQRQLAEAHAQAKAQAEQEAQELQRRMQEEVA------RREEAAVDAQQQ 1561
Cdd:PRK00409 526 EELERELEQKAEEAEALLKeaeklkeeleeKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2124423178 1562 KRSIQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1606
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2321-2574 |
8.59e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2321 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSLRVQMEELGK 2389
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2390 LKARIEAENRALI-LRDKDNTQRVLQEEAEKMK-HVAEEAARLSVAAQEAARLRELAEE--------------------- 2446
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPLQYDcwwekvenlqdlldratnqve 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2447 ----DLAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTL----E 2516
Cdd:PLN02939 318 kaalVLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklkE 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2517 AERQRQLEMSAEA------ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2574
Cdd:PLN02939 398 ESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1171-1740 |
9.02e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1171 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRSTHGAEE 1250
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1251 VLKAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1330
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1331 LLERWQavlaqtdlrqrELEQLGRQLRYYRESADPLGAWLQDAKRR-QEQIQ-AMVLADSRAVREQLRQEKALLEEIERH 1408
Cdd:pfam05557 144 LKAKAS-----------EAEQLRQNLEKQQSSLAEAEQRIKELEFEiQSQEQdSEIVKNSKSELARIPELEKELERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1409 GEKVEECQRFAKQYINAIKDYELQLVTY-KAQLEPVASPAKKPKVQS---GSESVIQEY-VDLRTRyselTTLTSQYIKF 1483
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREeKYREEAATLELEKEKLEQelqSWVKLAQDTgLNLRSP----EDLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1484 ISETLRRMEEEERLAEQQRAEERErlaaveaalekQRQLAEAHAQAKAQAEQEAQELQRrmQEEVARReeaavdAQQQKR 1563
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKA-----------RRELEQELAQYLKKIEDLNKKLKR--HKALVRR------LQRRVL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1564 SIQEELQHLRQ---------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGG-------AEGELQALRA 1627
Cdd:pfam05557 350 LLTKERDGYRAilesydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGykqqaqtLERELQALRQ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1628 RAEEAEAQkrQAQEEAERLRRQVQD---ETQRKRQAEAELAVRV-----KAEAEAAREKQRALQ---ALEEFRLQAEEAE 1696
Cdd:pfam05557 430 QESLADPS--YSKEEVDSLRRKLETlelERQRLREQKNELEMELerrclQGDYDPKKTKVLHLSmnpAAEAYQQRKNQLE 507
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2124423178 1697 RrlRQAEAERAR----QVQVALETAQRSAEVELQSKRASFAEKTAQLE 1740
Cdd:pfam05557 508 K--LQAEIERLKrllkKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2324-2678 |
9.22e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 45.44 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2324 TLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT-EAARQRSQVEEELFSlrvqmEELGKLKARIEAENRAL- 2401
Cdd:pfam13166 94 IQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLdECWKKIKRKKNSALS-----EALNGFKYEANFKSRLLr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2402 -ILRDKDNTQRVLQEEAEKmkhvAEEAARLSVAAQEAARLRE-LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2479
Cdd:pfam13166 169 eIEKDNFNAGVLLSDEDRK----AALATVFSDNKPEIAPLTFnVIDFDALEKAEILIQKVIGKSSAIEELIKNPDLADWV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2480 QQQKELAQE--------QARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEA-ERLKLRVAEMSRAQArAEEDA 2550
Cdd:pfam13166 245 EQGLELHKAhldtcpfcGQPLPAERKAALEAHFDDEFTEFQNRLQKLIEKVESAISSLlAQLPAVSDLASLLSA-FELDV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2551 QRFRKQAEEIGEKLHrtelatqekvTLVQTLEIQRQQSDHDAErLRQAIAELEREKEKLKQEAKLLQlKSEEMQTVQQEQ 2630
Cdd:pfam13166 324 EDIESEAEVLNSQLD----------GLRRALEAKRKDPFKSIE-LDSVDAKIESINDLVASINELIA-KHNEITDNFEEE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 2631 LLQETQALQQSFLSEKDTLLQRE----RFIEQEKAKLEQLFQDEVAKAQKLR 2678
Cdd:pfam13166 392 KNKAKKKLRLHLVEEFKSEIDEYkdkyAGLEKAINSLEKEIKNLEAEIKKLR 443
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1113-1538 |
9.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1113 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1192
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1193 EAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTislvirsthgAEEVLKAHEEQLKEAQAVPATLPEL 1272
Cdd:COG4717 178 ELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1273 EATKAALKKLRAQA-----EAQQPMFDALRDELRGAQEVGERLQQRHGERDVeveRWRERVAQLLERWQAVLAQTDLRQR 1347
Cdd:COG4717 243 ERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1348 ELEQLGRQLRYYRE-SADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQE-KALLEEIerHGEKVEECQRFAKQYiNA 1425
Cdd:COG4717 320 ELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEA--GVEDEEELRAALEQA-EE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1426 IKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET---LRRMEEEERLAE--Q 1500
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeaeLEQLEEDGELAEllQ 476
|
410 420 430
....*....|....*....|....*....|....*...
gi 2124423178 1501 QRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQ 1538
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1365-1565 |
9.74e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1365 PLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1443
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1444 ASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLT-------SQ-------YIKFISE----------------TLRRMEE 1493
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQlilsgeeSQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1494 EERLAEQQ----------------RAEERERLAAVEAALEK-QRQLAE--------------AHAQAKAQAEQEAQELQR 1542
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 2124423178 1543 -RMQEEVARREEAAVDAQQQKRSI 1565
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1779-2262 |
1.06e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1779 ERWQLKANEALRLRLQAEEVAQQKSLAQ--AEAEKQKEEAER---------------EARRRGKAEEQAVRQRELAEQEL 1841
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKriRLLEKREAEAEEalreqaelnrlkkkyLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1842 EKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLE----------EELARLQHEAAAATQKRQELEAELAKVRAEM 1911
Cdd:pfam05557 108 CLKNELSE-LRRQIQRAELELQSTNSELEELQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1912 EVLLASKarAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLA- 1987
Cdd:pfam05557 187 EIVKNSK--SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSw 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1988 -AIGEATRLKTEAEIALKEK--EAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASESE---LERQKGLVE 2061
Cdd:pfam05557 265 vKLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2062 DTLRQRRQVEEEILALKV---SFEKAAAGKAELELELGRIRSNAEdtLRSKEQAELEAMR-QRQLAAEEEQRRREAEERV 2137
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAED--MTQKMQAHNEEMEaQLSVAEEELGGYKQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2138 QKSLAA--EEEAARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQDAAQKR---LQAEEKAHAFAVQ 2206
Cdd:pfam05557 421 ERELQAlrQQESLADPSYSKEEVDSLRRKLETLElerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAEAYQ 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2207 QKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAE 2262
Cdd:pfam05557 501 QRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3832-3870 |
1.06e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2124423178 3832 YLYGTGCVAGVYVPGSRQTLTIYQALKKGLLSAEVARLL 3870
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2410-2588 |
1.09e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2410 QRVLQEEAEKMkhvaeEAARLsvAAQEAARLRELAEE--DLAQQRALAEKMLKE---KMQAVQEATRLKAEAELLQQQKE 2484
Cdd:PRK10929 109 QEILQVSSQLL-----EKSRQ--AQQEQDRAREISDSlsQLPQQQTEARRQLNEierRLQTLGTPNTPLAQAQLTALQAE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2485 LA-------------------QEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQA 2544
Cdd:PRK10929 182 SAalkalvdelelaqlsannrQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIV 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2124423178 2545 RA----EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQS 2588
Cdd:PRK10929 262 AQfkinRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQS 309
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1825-2077 |
1.16e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQ--ELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELE 1901
Cdd:pfam13868 67 RKEERKRYRQELEEQieEREQKRQEEyEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1902 AE--------LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEE--AARLRALAEEAKRQRQLAEEDA 1971
Cdd:pfam13868 147 KEeereederILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQEEQERKERQKEREE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1972 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN--ERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQL 2045
Cdd:pfam13868 227 AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKRLEHRRElekqIEEREEQR 306
|
250 260 270
....*....|....*....|....*....|..
gi 2124423178 2046 RKASESELERQKGLVEDTLRQRRQVEEEILAL 2077
Cdd:pfam13868 307 AAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2255-2612 |
1.22e-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: 44.89 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2255 RRQVEEAERLKQSAEEQAQAQAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAeQTLRQKAQVEQE 2334
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEE---------------------------KYKELSASSEELSEEKD-ALLAQRAAHEAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2335 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAL--ILRDKDNTQRV 2412
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2413 LQEEAEKMKHVAEEAARlSVAAQEAAR--LRELAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ--- 2487
Cdd:pfam07888 211 LQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltl 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2488 ---EQARRLQEDKEQMAqqleQETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrkqaeeigEKL 2564
Cdd:pfam07888 287 qlaDASLALREGRARWA----QERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER---------EKL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2124423178 2565 hRTELATQEKVTLVQTLEIQRQQSDhdaerLRQAIAELEREKEKLKQE 2612
Cdd:pfam07888 345 -EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1619-1753 |
1.23e-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: 44.36 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1619 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERR 1698
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1699 LRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVAVAQL 1753
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1557-1744 |
1.24e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1557 DAQQQKRSiqeELQHLRQSSEAEIQAKARQVE--AAERSRLRIE-----EEIRVVRLQLETTERQRGGAEGELQALRARA 1629
Cdd:pfam00038 36 ELRQKKGA---EPSRLYSLYEKEIEDLRRQLDtlTVERARLQLEldnlrLAAEDFRQKYEDELNLRTSAENDLVGLRKDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1630 EEAEAQKRQAQEEAERL------RRQVQDETQRKRQAEAELAVRVkAEAEAAReKQRALQALEEFRLQAEE-AERRLRQA 1702
Cdd:pfam00038 113 DEATLARVDLEAKIESLkeelafLKKNHEEEVRELQAQVSDTQVN-VEMDAAR-KLDLTSALAEIRAQYEEiAAKNREEA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2124423178 1703 EAerarQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQ 1744
Cdd:pfam00038 191 EE----WYQSKLEELQQAAARNGDALRSA-KEEITELRRTIQ 227
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1622-1721 |
1.26e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1622 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElAVRVKAEAEAAREKQRALQALEefrlqaEEAERR 1698
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 2124423178 1699 LRQAEAERARQVQVALETAQRSA 1721
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1835-2056 |
1.27e-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: 44.36 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1835 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEV 1913
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1914 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAERVlaeklaai 1989
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKL-------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1990 geATRLKTEAEIALKEKEAENeRLRRLAEDEAFQRRRLEEQAAQHKADI--EERLAQLRKASESELERQ 2056
Cdd:pfam09787 152 --RNQLTSKSQSSSSQSELEN-RLHQLTETLIQKQTMLEALSTEKNSLVlqLERMEQQIKELQGEGSNG 217
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1510-1717 |
1.27e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1510 AAVEAALEKQRQLAEAHAQAKAQAEQEAQELQ--RRMQEEVARREEAAVDAQQQKRSIQE-----------ELQHLRQSS 1576
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1577 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLETTERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1643
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1644 ERLRRQVQDETQRKRQAEAELAV-RVKAEAEAAREKQRALQAL--------EEFRLQAEeaerrlrQAEAERARQVQVAL 1714
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALaathgynpRDFRKRAE-------QALAANAKTATLAL 1378
|
...
gi 2124423178 1715 ETA 1717
Cdd:PHA03247 1379 EAA 1381
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1828-1971 |
1.29e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1907
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1908 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDA 1971
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1565-1936 |
1.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1565 IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1644
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1645 RLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQAlEEFRLQAEEAERRLRQAEAERARQVQvalETAQRSAEVE 1724
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELE-SLQEEAEELQEELEELQK-ERQDLEQQRKQLEAQIAELQSEIAER---EEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1725 LQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1804
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1805 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1884
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 1885 RLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL 1936
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1864-2075 |
1.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1864 RLRAETEQGEQQRQLLEEELARLQHEAAAAtqkrqelEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEAEAsrf 1943
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARA--- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1944 rELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA- 2021
Cdd:COG3206 234 -ELAEAEARLAALRAQLGSGPDaLPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAq 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2022 ---FQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEdtLRQRRQVEEEIL 2075
Cdd:COG3206 313 rilASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR--LEREVEVARELY 367
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2304-2568 |
1.37e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2376
Cdd:COG1340 14 EEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2377 LFSLRVQMEELG-------KLKARIEA-------------ENRALILRDKDntqrvLQEEAEKMKHVAEEAARLSVAAQE 2436
Cdd:COG1340 94 LDELRKELAELNkaggsidKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2437 AARLRELAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLeqetqgfqr 2513
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL--------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 2514 tleaerqRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2568
Cdd:COG1340 240 -------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1267-1719 |
1.38e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1267 ATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQ 1346
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1347 RELEQLGRQLRyyresADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAI 1426
Cdd:COG5278 163 LALAALLLAAA-----ALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1427 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEER 1506
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1507 ERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQ 1586
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1587 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAV 1666
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1667 RVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQR 1719
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1825-1992 |
1.39e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEAAAATQKRQELEAE 1903
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1904 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEASRFRELAEEaarlralaeEAKRQRQLAEEDAARQRAEAERV 1981
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNEL---------EIAKAKELADIEATKFERIVEAL 797
|
170
....*....|.
gi 2124423178 1982 LAEKLAAIGEA 1992
Cdd:PTZ00491 798 GRETLIAIARA 808
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1516-1694 |
1.39e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1516 LEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEvaRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKarQVEAAERSRL 1595
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKE--EQLDARAEKL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1596 RIEEEirvvrlQLETTERqrggaegelqALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELAVRVKAEAEaa 1675
Cdd:PRK12705 101 DNLEN------QLEEREK----------ALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180
....*....|....*....|
gi 2124423178 1676 REK-QRALQALEEFRLQAEE 1694
Cdd:PRK12705 157 EEKaQRVKKIEEEADLEAER 176
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2464-2559 |
1.42e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2464 QAVQEA-TRLKAEAELLQQQK---ELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA------ERQRQL-EMSAEAERL 2532
Cdd:PRK11637 166 QARQETiAELKQTREELAAQKaelEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlesslqKDQQQLsELRANESRL 245
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 2533 KLRVAEMSR-AQARAEE---DAQRFRKQAEE 2559
Cdd:PRK11637 246 RDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1960-2181 |
1.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1960 AKRQRQLAEEDAARQRAEAERvlaeklaaigEATRLKTEAEIALKEkeaENERLRRLAEDEAFQRRR-LEEQaaqhkadi 2038
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKK----------EAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNeLQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2039 EERLAQlrkaSESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAaagKAELElelgrirsnaedTLRSKEQAELEAMr 2118
Cdd:PRK12704 88 EKRLLQ----KEENLDRKLELLEKREEELEKKEKELEQKQQELEKK---EEELE------------ELIEEQLQELERI- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2119 qrqlaaeeeqrrreaeervqKSLAAEEeaARQRkaALEEVERlKAKVEEARRLR---ERAEQESAR 2181
Cdd:PRK12704 148 --------------------SGLTAEE--AKEI--LLEKVEE-EARHEAAVLIKeieEEAKEEADK 188
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1531-1900 |
1.45e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1531 AQAEQEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQl 1608
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1609 ETTERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKqralqalEEF 1688
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWST-------EVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1689 RLQAEEAERRLRQAEAERA-RQVQVALETAQRSAEVELQSKRASfaEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEA 1767
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYES--KVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1768 ERAREEAERELERWQLKANEALrlrlqaeevaqqkslaqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQl 1847
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKL-------------------------------------EELRRRRQEKESEEFEKLRQ- 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1848 aegtAQQRLAAEQELI--------RLRAETEQG----EQQRQLLEEELARLQHEA-----AAATQKRQEL 1900
Cdd:pfam02029 271 ----KQQEAELELEELkkkreerrKLLEEEEQRrkqeEAERKLREEEEKRRMKEEierrrAEAAEKRQKL 336
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3204-3237 |
1.51e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|....
gi 2124423178 3204 LLEAQAGTGHIIDPATSARLTVDEAVRSGLVGPE 3237
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1749-2204 |
1.69e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 44.62 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1749 AVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1828
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1829 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVR 1908
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1909 AEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1988
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1989 IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRR 2068
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2069 QVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2148
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2149 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFA 2204
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2305-2505 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2305 RQKQAADAEMEKHKKFAEQTLRQK-AQVEQELTTLRLQLEETDHQKSILDEELQRlKAEVTEAARQRS-QVEEELFSLRV 2382
Cdd:COG2268 201 ARIAEAEAERETEIAIAQANREAEeAELEQEREIETARIAEAEAELAKKKAEERR-EAETARAEAEAAyEIAEANAEREV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2383 QME-ELGKLKARIEAEnralilrdkdnTQRVLQEEAEKMKHVAEEAArlsvAAQEAARLRELAEEDLAQQRALAEKmlke 2461
Cdd:COG2268 280 QRQlEIAEREREIELQ-----------EKEAEREEAELEADVRKPAE----AEKQAAEAEAEAEAEAIRAKGLAEA---- 340
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423178 2462 kmqavqEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE 2505
Cdd:COG2268 341 ------EGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1489-1570 |
1.72e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.91 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1489 RRMEEEERLAEQQRAEERERLAAVEA-ALEKQRQLAEAHAQAK---AQAEQEAQELQRR-----MQEEVARREEAAVDAQ 1559
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEalaeaQAEAQASKEKARREIE 111
|
90
....*....|.
gi 2124423178 1560 QQKRSIQEELQ 1570
Cdd:PRK07353 112 QQKQAALAQLE 122
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1328-1605 |
1.73e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1328 VAQLLERWQAVLAQTDLRQRELEQLGRQlryyresadplgawLQDAKRRQEQIQAMVLADSRAVREQLRQ--EKALLEEI 1405
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQ--------------LAQAPAKLRQAQAELEALKDDNDEETREtlSTLSLRQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1406 ERhgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFIS 1485
Cdd:PRK11281 127 ES---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLR-RMEEEERLAEQQRAEERERLAA---VEAALEKQRQLAEAHAQakaQAEQEAQELQ------RRMQ-EEVARREEA 1554
Cdd:PRK11281 191 PSQRvLLQAEQALLNAQNDLQRKSLEGntqLQDLLQKQRDYLTARIQ---RLEHQLQLLQeainskRLTLsEKTVQEAQS 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1555 AVDAQQQKRS--IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1605
Cdd:PRK11281 268 QDEAARIQANplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1884-2011 |
1.75e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 43.63 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1884 ARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKqrlEAEASRfrelaEEAARLRALAEEA-KR 1962
Cdd:PRK06991 146 AWSQAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAA---AAPAAD-----DAEAKKRAIIAAAlER 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1963 QRQLAEEDAARQRA--EAERVLAEKLAAI--GEATRLKTEAEIALKEKEAENE 2011
Cdd:PRK06991 218 ARKKKEELAAQGAGpkNTEGVSAAVQAQIdaAEARRKRLAEQRDAPDDANADG 270
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1515-1686 |
1.78e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1515 ALEKQRQLA--------EAHAQAKAQA-EQEAQ-ELQR-RMQEEVARREEAAVDAQQQKRSiqEELQHLRQS-SEAEIQA 1582
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARgRLERqKMHDKAKAEEQRTKLLELQAES--AAVESSGQSrAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1583 KARQVEAaersrlrieeeirvvrlqletterqrggaEGELQALRARAEeaeaqkrqaqeeAERLRRQVQDETQRKRQaEA 1662
Cdd:PTZ00491 726 EARLIEA-----------------------------EAEVEQAELRAK------------ALRIEAEAELEKLRKRQ-EL 763
|
170 180
....*....|....*....|....
gi 2124423178 1663 ELAVRvKAEAEAAREKQRALQALE 1686
Cdd:PTZ00491 764 ELEYE-QAQNELEIAKAKELADIE 786
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2913-2949 |
1.91e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2124423178 2913 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2949
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2404-2557 |
1.94e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2404 RDKDNTQRVLQE---EAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQ 2480
Cdd:PRK12705 30 RLAKEAERILQEaqkEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREE-ERLVQKEEQLDARAEKLDNLENQLE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2481 QQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQA 2557
Cdd:PRK12705 109 EREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1486-1599 |
1.95e-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: 41.95 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQRA-EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQEL-QRRMQEEVARREEAAVDAQQQKR 1563
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423178 1564 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1599
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
213-288 |
2.13e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.28 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 213 LYEDLRDGHNLISLLEvlsgDSLP-------------REKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 279
Cdd:cd21294 38 LFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113
|
....*....
gi 2124423178 280 TLGLIWTII 288
Cdd:cd21294 114 ILGLIWQII 122
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2836-2873 |
2.15e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.15e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2124423178 2836 RRYLQGRSSIAGLLLKPANEKLSIYTALRRQLLSPGTA 2873
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
1489-1645 |
2.17e-03 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 43.73 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1489 RRMEEEERLAEQQRAE---ERERLAAVEAALEKQRQLAEAHAQA---KAQA-EQEAQELQRRMQEEVARREE-------- 1553
Cdd:pfam05914 165 KQAEEEEKHAELLYDQkrlERDRRALELAKLEEECRRAVNAATKnfnQALAaEQAERRRLEKRQEQEDNLAEiynhltsd 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1554 -------AAVDAQQQKRSIQEELQHLRQSSEAEIQaKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR 1626
Cdd:pfam05914 245 lltenpeVAQSSLGPHRVIPDRWKGMSPEQLKEIR-KEQEQQREEKERRREEEKQRDAEWDRQRLELARAALLLEREQQR 323
|
170 180
....*....|....*....|...
gi 2124423178 1627 ARAEEAEAQ----KRQAQEEAER 1645
Cdd:pfam05914 324 LRRELRRQLdeenLQLAQEQKAR 346
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1573-2045 |
2.19e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1573 RQSSEAEIQAKARQVEAAERSRLRIEEEIRVvRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1652
Cdd:COG3064 7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKE-EAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1653 ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASF 1732
Cdd:COG3064 86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1733 AEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQ 1812
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1813 KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAA 1892
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1893 ATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAA 1972
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRL 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1973 RQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 2045
Cdd:COG3064 406 DLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1499-1602 |
2.21e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 43.24 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1499 EQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAqelqrRMQEEVARREEAAVDAQQQKRS-IQEELQHLRQSSE 1577
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAA-----AAAEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423178 1578 ----------------AEIQAkarQVEAAERSRLRIEEEIR 1602
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1841-2208 |
2.22e-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: 44.12 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1841 LEKQRQLAE-GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAElaKVRAEMEVLLASKA 1919
Cdd:pfam07888 9 LEEESHGEEgGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1920 RAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRAlAEEAKRQRQLAEEDAArqRAEAERVLaeklaaigeatrlktea 1999
Cdd:pfam07888 87 EELRQSREKHEELEEKYKELSASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2000 eialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKV 2079
Cdd:pfam07888 147 -----ERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2080 SFEKAAAGKAELELELGRIRSNAE-------------------DTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKS 2140
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRA 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2141 LAAEEEAARQRKAALE---------EVERLKAKVEEARRLRERAEQESARQ--LQLAQDAAQKRLQAEEKAhAFAVQQK 2208
Cdd:pfam07888 301 RWAQERETLQQSAEADkdrieklsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1825-2263 |
2.24e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgeQQRQLLEEELARLQHEAAAATQKRQELEAEL 1904
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQ--RAAELAAEAAKKLAEAEKAAAEAEKKAAAEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1905 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1984
Cdd:COG3064 98 AKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1985 KLAA-IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT 2063
Cdd:COG3064 178 AAAAlVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2064 LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 2143
Cdd:COG3064 258 GVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2144 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSML 2223
Cdd:COG3064 338 EAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2124423178 2224 ERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAER 2263
Cdd:COG3064 418 VELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTG 457
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1249-1537 |
2.26e-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: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1249 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEvgERLQQRhgERDVEVERWRE-- 1326
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQE--EIAMEISRMREle 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1327 -----------RVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYREsadplgawlQDAKRRQEQIQAMVLADSRAVREQL 1395
Cdd:pfam17380 382 rlqmerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA---------EQEEARQREVRRLEEERAREMERVR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1396 RQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEyvdlRTRYSELTT 1475
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE----KEMEERQKA 528
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1476 LTSQYIKFISETLRR----MEEEERLAEQQR--AEERERLAAVEAALEKQRQLAEAHaqaKAQAEQEA 1537
Cdd:pfam17380 529 IYEEERRREAEEERRkqqeMEERRRIQEQMRkaTEERSRLEAMEREREMMRQIVESE---KARAEYEA 593
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1842-2115 |
2.35e-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: 43.69 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1842 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQL-----LEEELARLqheaaaaTQKRQELEAELAKVRAEMEV 1913
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQYdsnrrLGERIQDI-------TFWKSELEKELEELDEEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1914 LLASKARAEEESRSTSEK---SKQRLEAEASRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAAR 1973
Cdd:pfam03148 76 LLEEKRRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1974 QRAEAErvLAEKLAAIG---EATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLR 2046
Cdd:pfam03148 154 HKLEKD--LSDKKEALEideKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSIL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2047 KASESELERQKGLVEDTLRQRrqVEEeilalkvsFEKAaagKAELELELGRIRSNAEDTlrSKEQAELE 2115
Cdd:pfam03148 232 EQTANDLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEL--EKNIEALE 285
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1354-1566 |
2.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1354 RQLRYYRESADPLGAWLQDAKRRQEQiqamVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINA---IKDYE 1430
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK----ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1431 LQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQRA 1503
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1504 EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEE-------VARREEAAVDAQQQKRSIQ 1566
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2425-2622 |
2.37e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2425 EEAARLSVAAQEAARLRelAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2504
Cdd:PRK05035 465 EKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2505 EQETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV-AEMSRAQAR-AEEDAQRFRKQAEEIGEKLHRTELAT 2571
Cdd:PRK05035 540 AAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAVaAAIARAKAKkAAQQAASAEPEEQVAEVDPKKAAVAA 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2124423178 2572 QEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEE 2622
Cdd:PRK05035 620 AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2876-2909 |
2.37e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.37e-03
10 20 30
....*....|....*....|....*....|....
gi 2124423178 2876 LLEAQAASGFLLDPVQNRRLTVNEAVKEGVVGPE 2909
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2467-2545 |
2.44e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.93 E-value: 2.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 2467 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLEQETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2545
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
186-288 |
2.44e-03 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 41.50 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 186 QKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALD 255
Cdd:cd21292 25 EKVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALN 102
|
90 100 110
....*....|....*....|....*....|...
gi 2124423178 256 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 288
Cdd:cd21292 103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2321-2499 |
2.48e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2321 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR--SQVEEELFSLRVQMEELgklKARIEAEN 2398
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAEL---SARYTPNH 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2399 RALilrdkdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2478
Cdd:COG3206 291 PDV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
170 180
....*....|....*....|.
gi 2124423178 2479 LQQQKELAQEQARRLQEDKEQ 2499
Cdd:COG3206 363 ARELYESLLQRLEEARLAEAL 383
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1491-1570 |
2.55e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1491 MEE-EERLAEQQRAEERERLAAVEAALEKQRQLAEAH-------AQAKAQAEQEAQELQRRMQEEVAR-REEAAVDAQQQ 1561
Cdd:cd06503 28 LDErEEKIAESLEEAEKAKEEAEELLAEYEEKLAEARaeaqeiiEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQE 107
|
....*....
gi 2124423178 1562 KRSIQEELQ 1570
Cdd:cd06503 108 KEKALAELR 116
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1873-2077 |
2.64e-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: 42.60 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1873 EQQRQLLEeeLARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAsrfRELAEEAAR 1952
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLELEI---EEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1953 LRALAEEAKRQRQLA-----EEDAARQRAEAERVLAEklaaigeatrlkteaeiALKEKEAENERLRRLAEDEAFQRRRL 2027
Cdd:COG1579 78 YEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILE-----------------LMERIEELEEELAELEAELAELEAEL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2028 EEQaaqhKADIEERLAQLRKASESELERQKGLVEdtlrqrrQVEEEILAL 2077
Cdd:COG1579 141 EEK----KAELDEELAELEAELEELEAEREELAA-------KIPPELLAL 179
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1566-1752 |
2.65e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 42.34 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1566 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1645
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1646 LRRQVQDetqRKRQAEAELAVRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSaeve 1724
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSREVEEAKRAFEEkLESFEQLQAQFEQEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180
....*....|....*....|....*...
gi 2124423178 1725 LQSKRASFAEKTAQLERTLQEEHVAVAQ 1752
Cdd:pfam15665 152 QRAQSASSLAEQEKLEELHKAELESLRK 179
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1836-2121 |
2.68e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1836 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL 1915
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1916 ASKARAEeesrsTSEKSKQRLEAE--ASRFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAIGEAt 1993
Cdd:PRK11637 110 ASIAKLE-----QQQAAQERLLAAqlDAAFRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1994 RLKTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVedtlrqrrqveee 2073
Cdd:PRK11637 168 RQETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2074 ilALKVSFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-----MRQRQ 2121
Cdd:PRK11637 223 --GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarVRDKQ 274
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1499-1615 |
2.76e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.04 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1499 EQQRAEERERLAAVEAALEKQRQLAEAhaQAKAQAEQEAQELQRRMQEEVARREEAavdaqqQKRSIQEELQHLRQSSEA 1578
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEKAIEAE--RAKAEAAEAEQELLREKQKEEEQMMEA------QERSYQEHVKQLIEKMEA 254
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423178 1579 EIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQR 1615
Cdd:pfam02841 255 EREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1516-1662 |
2.80e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.38 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1516 LEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEA----- 1589
Cdd:pfam13904 47 LKLERQPLEAYENwLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAesask 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1590 --AERSRLRIEEEIRVVRLQLETTERQRggaegelqalraraeeaeaQKRQAQEEAERLRRQVQDETQRKRQAEA 1662
Cdd:pfam13904 127 slAKPERKVSQEEAKEVLQEWERKKLEQ-------------------QQRKREEEQREQLKKEEEEQERKQLAEK 182
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2467-2614 |
2.82e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2467 QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERlklrvaemSRAQARA 2546
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA--------AAAKAKA 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423178 2547 EEDAQRFR---KQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSdhdAERLRQAIAELErEKEKLKQEAK 2614
Cdd:PRK09510 150 EAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK---AAAEAKKKAEAE-AKKKAAAEAK 216
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1825-1980 |
2.82e-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: 43.05 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQelEAEL 1904
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRR--NEEL 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1905 AKvRAEMEVLLASKARAEEESRSTSEKskqrlEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER 1980
Cdd:pfam12037 129 LR-KQEESVAKQEAMRIQAQRRQTEEH-----EAELRRETERAKAEAEAEARAKEERENEDLNLEQ-LREKANEER 197
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2319-2486 |
2.84e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2319 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSLRVQMEELgklkARIEAEN 2398
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL----RSYLSPN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2399 RALIlrdkdntqRVLQEEAEKMKH-VAEEAARLSVAAQEAARLRELAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2476
Cdd:COG3524 248 SPQV--------RQLRRRIAALEKqIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 2124423178 2477 EllQQQKELA 2486
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2305-2612 |
3.02e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.26 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2305 RQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2384
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2385 EELGKLKARIEAENRAlilrdkDNTQRvlqeeaekmkhvaeeaaRLSVAAQEAARLRELAEEDLAQQRALAEKMLKeKMQ 2464
Cdd:pfam15905 132 LELTRVNELLKAKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2465 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQA 2544
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 2545 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQE 2612
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2305-2715 |
3.08e-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: 44.01 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2305 RQKQAADAEMEKHKKFAEQTLRqkaqvEQELTTLRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2382
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLD-----EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2383 QMEE-------LGKLKARIEAENRALILRDKDNTQRVLQEEAEKMK----------HVAEEAARLS-VAAQEAARLRELA 2444
Cdd:pfam01576 167 NLAEeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAeLRAQLAKKEEELQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2445 E-----EDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE--QETQGFQRTLEA 2517
Cdd:pfam01576 247 AalarlEEETAQKNNALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKTELEdtLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2518 ERQRQLEM-----SAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA----TQEKVTLVQTLEIQRQQS 2588
Cdd:pfam01576 324 KREQEVTElkkalEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAleseNAELQAELRTLQQAKQDS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2589 DHDAERLRQAIAEL-------EREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQ-----QSFLSEKDTLLQRE--- 2653
Cdd:pfam01576 404 EHKRKKLEGQLQELqarlsesERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdvsslESQLQDTQELLQEEtrq 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2654 --------RFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQL------VASMEEARQR-QREAEEGV----- 2713
Cdd:pfam01576 484 klnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLeedagtLEALEEGKKRlQRELEALTqqlee 563
|
490
....*....|....
gi 2124423178 2714 ------------RR 2715
Cdd:pfam01576 564 kaaaydklektkNR 577
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1833-1926 |
3.17e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.67 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1833 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME 1912
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 2124423178 1913 VLLASKARAEEESR 1926
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2304-2525 |
3.19e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ-VEEELFSLRV 2382
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2383 QMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEK 2462
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQ 278
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2463 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEM 2525
Cdd:pfam13868 279 EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1824-1984 |
3.21e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1824 GKAEEQAVRQRELAEQELEKQRQLA---EGTAQQRL-AAEQELIR-LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQ 1898
Cdd:pfam04012 42 RQALAQTIARQKQLERRLEQQTEQAkklEEKAQAALtKGNEELAReALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1899 ELEAELAKVRAEMEVLLA--SKARAEEESRSTSEKSK-QRLEAEASRFRE-LAEEAARLRALAEEAKRQRQLAE-EDAAR 1973
Cdd:pfam04012 122 ALETKIQQLKAKKNLLKArlKAAKAQEAVQTSLGSLStSSATDSFERIEEkIEEREARADAAAELASAVDLDAKlEQAGI 201
|
170
....*....|.
gi 2124423178 1974 QRAEAERVLAE 1984
Cdd:pfam04012 202 QMEVSEDVLAR 212
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2408-2711 |
3.21e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2408 NTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRElaeEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQQK--- 2483
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRL---EKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKSIDikk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2484 --ELAQEQARRLQEDKEQMAQQLEQETqGFQRTLEAERQRQLEMSAEAERLKLRVAEM--SRAQARAEEDAQRFRKQAEE 2559
Cdd:COG5185 310 atESLEEQLAAAEAEQELEESKRETET-GIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2560 IGEKLH--RTELATQEKVtLVQTLEIQRQQSDHDAERLRQAIAELEREkekLKQEAKLLQLKSEEMQTVQQEQLLQETQA 2637
Cdd:COG5185 389 TKESLDeiPQNQRGYAQE-ILATLEDTLKAADRQIEELQRQIEQATSS---NEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2638 LQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEE 2711
Cdd:COG5185 465 LEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHI 538
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2306-2579 |
3.30e-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: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2306 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFS-L 2380
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2381 RVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARlsvAAQEAARLRELAEEDLAQQRALAEKMLK 2460
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRAK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2461 EKMQAVQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLE--AERQRQLEMSAEAERLK-- 2533
Cdd:pfam13868 210 LYQEEQERKERQKEREEAekkARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRkqAEDEEIEQEEAEKRRMKrl 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2124423178 2534 -----LRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2579
Cdd:pfam13868 290 ehrreLEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2473-2614 |
3.38e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2473 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQgfQRTLEAERQRQLEMSAEAErlklrvAEMSRAQARAEEDAQR 2552
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK--QRAAEQARQKELEQRAAAE------KAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423178 2553 fRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAK 2614
Cdd:TIGR02794 118 -QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1573-1708 |
3.69e-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: 42.80 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1573 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR--- 1647
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvla 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423178 1648 -------RQVQDETQRKRQAEAELAVRVKAEAEAAREK-QRALQALEEFRLQAEEAERRLRQAEAERAR 1708
Cdd:pfam00529 134 piggisrESLVTAGALVAQAQANLLATVAQLDQIYVQItQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1478-2030 |
3.89e-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: 43.88 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1478 SQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKqrqLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVD 1557
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS---YEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1558 AQQQ-KRSIQEELQHLRQS----------SEAEIQAKARQVEAAERSrlrIEEEIRVVRLQLETTERQRGGAEGELQALR 1626
Cdd:TIGR00606 660 GATAvYSQFITQLTDENQSccpvcqrvfqTEAELQEFISDLQSKLRL---APDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1627 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVrVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAEr 1706
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT-IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK- 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1707 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvavaqlreeaerraqqqaeaerareeaERELERWQLKAN 1786
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ---------------------------QEQIQHLKSKTN 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1787 EALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1866
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1867 AETEQGEQQRQLLEEELarlqhEAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRST-----SEKSKQRLEAEAS 1941
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKI-----QDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINEDMRLMrqdidTQKIQERWLQDNL 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1942 RFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGeatrlKTEAEIALKEKEAENERLRRLAEDEA 2021
Cdd:TIGR00606 1022 TLRKRENE---LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIK-----RNHVLALGRQKGYEKEIKHFKKELRE 1093
|
....*....
gi 2124423178 2022 FQRRRLEEQ 2030
Cdd:TIGR00606 1094 PQFRDAEEK 1102
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1486-1592 |
3.94e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1486 ETLRRMEEEERLAEQQRAEERErlAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARRE---EAAVDAQQQK 1562
Cdd:PRK09510 122 EAAKQAALKQKQAEEAAAKAAA--AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaEAAAKAAAEA 199
|
90 100 110
....*....|....*....|....*....|
gi 2124423178 1563 RSIQEELQHLRQSSEAEIQAKARQVEAAER 1592
Cdd:PRK09510 200 KKKAEAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1499-1741 |
3.98e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1499 EQQRAEERERLaaVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA 1578
Cdd:pfam05667 238 EEYRKRKRTKL--LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1579 EIQAKARQVEAAERsRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLrrqvQDETQRKR 1658
Cdd:pfam05667 316 TSSPPTKVETEEEL-QQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL----EKQYKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1659 QAEAELA------VRVKAEAEAAREKQRALQAL-EEFRLQAEEAERRLRQAEAERARQVQVALETAQ------RSAEVEL 1725
Cdd:pfam05667 391 KTLDLLPdaeeniAKLQALVDASAQRLVELAGQwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKelrekiKEVAEEA 470
|
250
....*....|....*.
gi 2124423178 1726 QSKRASFAEKTAQLER 1741
Cdd:pfam05667 471 KQKEELYKQLVAEYER 486
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3167-3204 |
4.00e-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: 4.00e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2124423178 3167 LRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVAVAL 3204
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1828-1993 |
4.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1907
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1987
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 2124423178 1988 AIGEAT 1993
Cdd:COG3883 275 GAAAAS 280
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1826-2074 |
4.13e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.10 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1826 AEEQAVRQRELAEQELEKQRQLAEGTAQ---------QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1896
Cdd:pfam15558 90 IEKESRWREQAEDQENQRQEKLERARQEaeqrkqcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1897 RQELEAELAKVRAeMEVLLASKARAEEESRSTS-EKSKQRLEAE-----ASRFRELAEEAA-------RLRALAEEAKRQ 1963
Cdd:pfam15558 170 QENNLSELLNHQA-RKVLVDCQAKAEELLRRLSlEQSLQRSQENyeqlvEERHRELREKAQkeeeqfqRAKWRAEEKEEE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1964 RQ--------LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKeaenerlrrlAEDEAFQRRRLEEQAAQHK 2035
Cdd:pfam15558 249 RQehkealaeLADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLK----------VEKEEKCHREGIKEAIKKK 318
|
250 260 270
....*....|....*....|....*....|....*....
gi 2124423178 2036 adiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 2074
Cdd:pfam15558 319 ---EQRSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1484-1585 |
4.16e-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: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1484 ISETLRR----MEEEE-RL---AEQQRAEER----ERLAAVEAAlEKQRQLAEAHAQAKAqAEQEAQELQRRMQEE--VA 1549
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLliaEQHQKVVEKeaetERKRAVIEA-EKDAEVAKIQMQQKI-MEKEAEKKISEIEDEmhLA 237
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2124423178 1550 rREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAR 1585
Cdd:cd03406 238 -REKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1489-1896 |
4.44e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1489 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK-AQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1567
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1568 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1647
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1648 RQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQS 1727
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1728 KRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQA 1807
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1808 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1887
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 2124423178 1888 HEAAAATQK 1896
Cdd:COG3064 424 LALAGAAGA 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2325-2749 |
4.49e-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: 43.57 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2325 LRQKAQVEQELTTLRLQLEETDHQKSILDEELQR----LKAEVTEAARQRSQVEEELFSLRVQMEelgKLKARIEAENRA 2400
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlvlANSELTEARTERDQFSQESGNLDDQLQ---KLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2401 LILrDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELaeedLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQ 2480
Cdd:pfam15921 393 LSL-EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEAL----LKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2481 QQKELAQEQARRLQED---KEQMAQQLEQETQGFQRTLEaERQRQLEMS-AEAERLKLRV-AEMSRAQARAEEDAQRFRK 2555
Cdd:pfam15921 468 AQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQ-EKERAIEATnAEITKLRSRVdLKLQELQHLKNEGDHLRNV 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2556 QAEEIGEKLhrtELATQEKVtlvqtLEIQRQQSDHDAERLRQ---AIAELEREKEKLKQEAKLLQLKSEEMQTvqqeqll 2632
Cdd:pfam15921 547 QTECEALKL---QMAEKDKV-----IEILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRRLELQEFKI------- 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2633 qetqaLQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREaeeg 2712
Cdd:pfam15921 612 -----LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---- 682
|
410 420 430
....*....|....*....|....*....|....*..
gi 2124423178 2713 VRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLE 2749
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1657-1891 |
4.55e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1657 KRQAEAELAVRVKAEaeaaREKQRALQAleEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEkt 1736
Cdd:pfam15709 327 KREQEKASRDRLRAE----RAEMRRLEV--ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1737 aqlERTLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeea 1816
Cdd:pfam15709 399 ---ERQRQEEEERKQRLQLQAAQ-------------------ERARQQQEEFRRKLQELQRKKQQEEAE----------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423178 1817 erearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAA 1891
Cdd:pfam15709 446 --------RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1373-1701 |
4.60e-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: 43.30 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1373 AKRRQEQIQAMvLADSRAVREQLRQE-KALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVaspakkpk 1451
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDEL-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1452 vqsgsESVIQEYVDLRTRYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQ-RQLAEAHAQAK 1530
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1531 AQ--------AEQEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKA----------RQVEAAE 1591
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKKyveknlpeieDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1592 RSRLRIEEEIRVV----RLQLETTERQRgGAEGELQALRARAEEAE---AQKRQAQEEaerLRRQVQDETQRKRQAEAEL 1664
Cdd:pfam06160 305 EQNKELKEELERVqqsyTLNENELERVR-GLEKQLEELEKRYDEIVerlEEKEVAYSE---LQEELEEILEQLEEIEEEQ 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 2124423178 1665 AVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQ 1701
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2418-2512 |
4.69e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2418 EKMKHVAEEAARLSVAAQEAARLRELAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2491
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 2124423178 2492 RLQEDKEQMAQQLEQETQGFQ 2512
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1622-1711 |
4.78e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1622 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELavrvKAEAEaarekQRALQALEEFRLQAEEAERRLRQ 1701
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 2124423178 1702 AEAERARQVQ 1711
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2438-2613 |
4.84e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2438 ARLRELAEEDLAQQRALAEkmLKEKmqAVQEATRLkaeAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA 2517
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTD--LKER--ESQEDAKR---AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2518 ERQRQLEMSAEAERLKLRVA-----EMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDhDA 2592
Cdd:pfam05262 257 AKNLPKPADTSSPKEDKQVAenqkrEIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP-VA 334
|
170 180
....*....|....*....|.
gi 2124423178 2593 ERLRQAIAELEREKEKLKQEA 2613
Cdd:pfam05262 335 EDLQKTKPQVEAQPTSLNEDA 355
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1828-2088 |
4.87e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1828 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQheaaaatQKRQELEAELAKV 1907
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK-------EERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1908 RAEMEVLLASKARAEEESRSTSEKSKqRLEAEASRF----------RELAEEAARLRALAEEAKRQRQLAEE-DAARQRA 1976
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKLRK-EIERLEWRQqtevlspeeeKELVEKIKELEKELEKAKKALEKNEKlKELRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1977 EAERVLAEKL-----AAIGEATRLKTEAeIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASEs 2051
Cdd:COG1340 170 KELRKEAEEIhkkikELAEEAQELHEEM-IELYKEA---DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRK- 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 2124423178 2052 ELERQKGLVEDTLRQRRQVEEEILAlKVSFEKAAAGK 2088
Cdd:COG1340 245 ELKKLRKKQRALKREKEKEELEEKA-EEIFEKLKKGE 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2304-2468 |
5.00e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2304 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQ 2383
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2384 mEELGKLKARIEAENRALILRDKDnTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKM 2463
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 2124423178 2464 QAVQE 2468
Cdd:COG1579 167 ELAAK 171
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1384-1693 |
5.18e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1384 VLADSRAVREQLRQEkalLEEIE-----RHGEKVEECQ-------------RFAKQYINAIKDYELQLVTYKAQLEPVAS 1445
Cdd:PRK10929 17 AYAATAPDEKQITQE---LEQAKaaktpAQAEIVEALQsalnwleerkgslERAKQYQQVIDNFPKLSAELRQQLNNERD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1446 PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAAVEAALEKQRQLA 1523
Cdd:PRK10929 94 EPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1524 EAHAQAKAQAeqeaqelqrrMQEEVARReEAAVDaqqqkrsiQEELQHLRQSSEAEIqakAR-QVEAAERSRLRIEEEIR 1602
Cdd:PRK10929 168 TPLAQAQLTA----------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1603 VVRLQLeTTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL---AVRVKAEA----EAA 1675
Cdd:PRK10929 226 ALRNQL-NSQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAA 292
|
330
....*....|....*...
gi 2124423178 1676 REKQRALQALEEFRLQAE 1693
Cdd:PRK10929 293 SQTLQVRQALNTLREQSQ 310
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1848-1991 |
5.26e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.48 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1848 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS 1927
Cdd:COG4191 1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 1928 TSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGE 1991
Cdd:COG4191 81 LLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGE 144
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1825-2121 |
5.35e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1825 KAEEQAVRQRELAEQElekQRQLAEGTAQqrlaaeqelIRLRAETEQGEQQRQLLEE--ELARLQHEAAAATQKRQ-ELE 1901
Cdd:COG5185 279 RLNENANNLIKQFENT---KEKIAEYTKS---------IDIKKATESLEEQLAAAEAeqELEESKRETETGIQNLTaEIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1902 AELAKVRAEMEVLLASKARAEEESRstSEKSKQRLEAEASRFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERV 1981
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVE--LSKSSEELDSFKDTIESTKES---LDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1982 LAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA-----QHKADIEERLAQL-RKASE--SEL 2053
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrsvrSKKEDLNEELTQIeSRVSTlkATL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2054 ERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNA--EDTLRSKEQAELEAMRQRQ 2121
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELiqASNAKTDGQAANLRTAVID 571
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1495-1741 |
5.48e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1495 ERLAEQQRAEERERLAAVEaALEKQRQlaeahaqakaQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRq 1574
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENK----------DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1575 SSEAEIQA-------------KARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQK----- 1636
Cdd:pfam10174 521 SLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1637 ----------RQAQEEAERLR--RQVQDETQRKRQAEAELAVRVK-AEAEAAREKQRA--LQALEEFRLQAEEAERRLRQ 1701
Cdd:pfam10174 601 kiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSS 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 1702 AE--------------AERARQVQVALETAQRS------------AEVEL-QSKRASFAEKTAQLER 1741
Cdd:pfam10174 681 TQqslaekdghltnlrAERRKQLEEILEMKQEAllaaisekdaniALLELsSSKKKKTQEEVMALKR 747
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1503-1745 |
5.49e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.90 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1503 AEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQeevarreeaavDAQQQKRSIQEELQHLRQSSEAEIQA 1582
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1583 KARqveaaersrlrieeeirvvRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1662
Cdd:pfam12795 74 ILA-------------------SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1663 EL---AVRVKAEAEAAREKQRALQALEEFRLQAEEAE-------RRLRQAEAERARQVQVALETAQRSAEVELQSKRASF 1732
Cdd:pfam12795 135 RLngpAPPGEPLSEAQRWALQAELAALKAQIDMLEQEllsnnnrQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQE 214
|
250
....*....|....
gi 2124423178 1733 AEKT-AQLERTLQE 1745
Cdd:pfam12795 215 AEQAvAQTEQLAEE 228
|
|
| HPtr |
COG2198 |
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; |
1826-2605 |
5.74e-03 |
|
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 43.11 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1826 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1905
Cdd:COG2198 11 LLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLELLLLLLLLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1906 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1985
Cdd:COG2198 91 LLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1986 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLR 2065
Cdd:COG2198 171 LLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2066 QRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEE 2145
Cdd:COG2198 251 LLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2146 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLER 2225
Cdd:COG2198 331 LLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2226 LRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALR 2305
Cdd:COG2198 411 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2306 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQME 2385
Cdd:COG2198 491 LLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGL 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2386 ELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQA 2465
Cdd:COG2198 571 LLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2466 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2545
Cdd:COG2198 651 LLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLL 730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 2546 AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQR----------------QQSDHDAERLRQAIAELERE 2605
Cdd:COG2198 731 LLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEALRRlggdpellrellelflEELPELLAELRQALAAGDLE 806
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1938-2448 |
5.87e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1938 AEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLa 2017
Cdd:COG3899 752 AEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEA- 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2018 edeafQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGR 2097
Cdd:COG3899 831 -----RALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2098 IRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2177
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2178 ESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQ 2257
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2258 VEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfaeqtLRQKAQVEQELTT 2337
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL------------AALALAAAARAAA 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2338 LRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEA 2417
Cdd:COG3899 1134 ALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALA 1213
|
490 500 510
....*....|....*....|....*....|.
gi 2124423178 2418 EKMKHVAEEAARLSVAAQEAARLRELAEEDL 2448
Cdd:COG3899 1214 LLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1873-2048 |
6.21e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.28 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1873 EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAA- 1951
Cdd:cd00176 18 EKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1952 RLRALAEEAKRQRQLAEEDAARQRAEAervlAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAED----EAFQRRRL 2027
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADDLEQWLEE----KEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRlkslNELAEELL 173
|
170 180
....*....|....*....|.
gi 2124423178 2028 EEQAAQHKADIEERLAQLRKA 2048
Cdd:cd00176 174 EEGHPDADEEIEEKLEELNER 194
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
192-287 |
6.41e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 39.59 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 192 KWVNKHLikhWRAEAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN- 266
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYf 91
|
90 100
....*....|....*....|.
gi 2124423178 267 IRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21218 92 LTPEDIVSGNPRLNLAFVATL 112
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2385-2502 |
6.43e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2385 EELGKLKARIEAENRALILRDKDNTQrvLQEEaekmkhVAEEAARLSVAAQEAARLRELAEEdLAQQRALAEKMLKEKMQ 2464
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQDS------VANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2465 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2502
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1463-1753 |
6.47e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1463 YVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEErERLAAV-------EAALEKQRQLAEAHAQAKAQAEQ 1535
Cdd:PRK10811 484 YSVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQ-PALATFampdvppAPTPAEPAAPVVAAAPKAAAATP 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1536 EAQ-----------------ELQRRMQEEVARREEAAVDAQQQKRsiqeelqhlrqsseaeiqaKARQVEAAERSRLRIE 1598
Cdd:PRK10811 563 PAQpgllsrffgalkalfsgGEETKPQEQPAPKAEAKPERQQDRR-------------------KPRQNNRRDRNERRDT 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1599 EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAvrvKAEAEAarek 1678
Cdd:PRK10811 624 RDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA---- 696
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423178 1679 qralQALEEFRLQAEEAERRLRQAEAERA-RQV--QVALETAQrSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1753
Cdd:PRK10811 697 ----LNVEEQSVQETEQEERVQQVQPRRKqRQLnqKVRIEQSV-AEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPL 769
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1500-1694 |
6.67e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1500 QQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE 1579
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1580 IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA-ERLRRQVQDETQRKR 1658
Cdd:PRK07735 156 EEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAkQKASQGNGDSGDEDA 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 2124423178 1659 QAEAELAVRVKAEAeAAREKQRALQALEEFRLQAEE 1694
Cdd:PRK07735 236 KAKAIAAAKAKAAA-AARAKTKGAEGKKEEEPKQEE 270
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2416-2551 |
6.75e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2416 EAEKMK-HVAEEAAR---LSVAAQEAARlrELAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2491
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 2492 RLQEdkeqmaqqLEQETQgfQRTLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2551
Cdd:PTZ00491 761 QELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1931-2079 |
6.98e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1931 KSKQRLEAEASRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAigEATRLKTE 1998
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1999 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALK 2078
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
.
gi 2124423178 2079 V 2079
Cdd:PRK12705 181 I 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2454-2767 |
7.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2454 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQ---ETQGFQRTLEAERQRQLEMSAEAE 2530
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQareELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2531 RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAtqekvtlVQTLEIQRQQSDHDAERLRQAIAELEREKEKLK 2610
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE-------RQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2611 QEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQLfQDEVAKAQKLREEQQRQQKQMEE 2690
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL-PRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2691 EKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQA 2767
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1535-1674 |
7.28e-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: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1535 QEAQELQRRMqEEVARREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQ 1614
Cdd:COG0542 411 EELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423178 1615 RGGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDETQRKRQAEAELAVRVKAEAEA 1674
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1257-1350 |
7.37e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 38.85 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1257 EQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVAQLLERWQ 1336
Cdd:smart00150 18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
|
90
....*....|....
gi 2124423178 1337 AVLAQTDLRQRELE 1350
Cdd:smart00150 88 ELKELAEERRQKLE 101
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2352-2566 |
7.47e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2352 LDEELQRLKAevteaarQRSQVEEELFSLRVQ--MEELGKLKARIEAenraliLRDkdntqrVLQEEAEKMKHVAEEAAR 2429
Cdd:PRK04778 254 IEKEIQDLKE-------QIDENLALLEELDLDeaEEKNEEIQERIDQ------LYD------ILEREVKARKYVEKNSDT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2430 LSvaaqeaarlrelaeEDLAQQRAlAEKMLKEKMQAVQEATRLKAEAelLQQQKELaQEQARRLQEDKEQMAQQLEQETQ 2509
Cdd:PRK04778 315 LP--------------DFLEHAKE-QNKELKEEIDRVKQSYTLNESE--LESVRQL-EKQLESLEKQYDEITERIAEQEI 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2510 GF---QRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHR 2566
Cdd:PRK04778 377 AYselQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEK 436
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1826-1926 |
7.48e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1826 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1905
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 2124423178 1906 KvRAEMEVLLaskarAEEESR 1926
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1494-1592 |
7.49e-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: 40.16 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1494 EERLAEQQRAEERERLAAVEAALEKQRQLAEAHA-------QAKAQAEQEAQELQRRMQEEVARREEAAvdaqqqKRSIQ 1566
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAeaaeiiaEARKEAEAIAEEAKAEAEAEAERIIAQA------EAEIE 106
|
90 100
....*....|....*....|....*.
gi 2124423178 1567 EELQHLRQSSEAEIQAKArqVEAAER 1592
Cdd:COG0711 107 QERAKALAELRAEVADLA--VAIAEK 130
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1164-1708 |
7.56e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1164 RECAQRIAEQQKAQAEVEglgkgVARLSAEAEKVL-----ALPEPSPAAPTLRSELELTLGKL-----EQVRSLSA---I 1230
Cdd:NF041483 559 REETERAIAARQAEAAEE-----LTRLHTEAEERLtaaeeALADARAEAERIRREAAEETERLrteaaERIRTLQAqaeQ 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1231 YLEKLKTISLVIRSTHGAE---------EVLKAHEEQLKEAQAVPATLPELEATKAALkklRAQAEAQQPMFDALRDELR 1301
Cdd:NF041483 634 EAERLRTEAAADASAARAEgenvavrlrSEAAAEAERLKSEAQESADRVRAEAAAAAE---RVGTEAAEALAAAQEEAAR 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1302 GAQEVGERLQQRHGERDVEVERWRERVAQLL-------ERWQA----VLAQTDLRQREL----EQLGRQLRY----YRES 1362
Cdd:NF041483 711 RRREAEETLGSARAEADQERERAREQSEELLasarkrvEEAQAeaqrLVEEADRRATELvsaaEQTAQQVRDsvagLQEQ 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1363 ADPLGAWLQDAK-------RRQEQIQA-MVLADSRAVREQLRQEKALLEeiERHGEKVEECQRFAKQYIN-AIKDYE--- 1430
Cdd:NF041483 791 AEEEIAGLRSAAehaaertRTEAQEEAdRVRSDAYAERERASEDANRLR--REAQEETEAAKALAERTVSeAIAEAErlr 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1431 LQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYI-KFISETLRRMEEEERLAEQQRAEERERL 1509
Cdd:NF041483 869 SDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQADRLIgEATSEAERLTAEARAEAERLRDEARAEA 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1510 AAV--EAALEKQRQLAEAHAQAK------AQAEQEAQELQRRMQEEVAR-REEAAVDAQQQKRSIQEELQhlRQSSEAEI 1580
Cdd:NF041483 949 ERVraDAAAQAEQLIAEATGEAErlraeaAETVGSAQQHAERIRTEAERvKAEAAAEAERLRTEAREEAD--RTLDEARK 1026
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1581 QAKARQVEAAERSRLRIEEeirvvrlqlETTERQRGGAEGELQALRArAEEAEAQKRQ----AQEEAERLRRQVQDE--- 1653
Cdd:NF041483 1027 DANKRRSEAAEQADTLITE---------AAAEADQLTAKAQEEALRT-TTEAEAQADTmvgaARKEAERIVAEATVEgns 1096
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1654 -TQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLqaEEAERRLRQAEAERAR 1708
Cdd:NF041483 1097 lVEKARTDADELLVGARRDATAIRERAEELRDRITGEI--EELHERARRESAEQMK 1150
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2472-2773 |
7.66e-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: 42.85 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2472 LKAEAELLQQQKELAQEQARRLQEdKEQMAQQLEQETQGFQRTLEAERqrqlEMSAEAERLKLRVAEmsraqaraeedaq 2551
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAA------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2552 rfRKQaeEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTvqqeql 2631
Cdd:pfam01576 69 --RKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEE------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2632 lqetqalQQSFLSEKDTLLQRER-FIEQEKAKLEQLFQDEVAKAQKLreeqqrqqkQMEEEKQQLVASMEEAR----QRQ 2706
Cdd:pfam01576 139 -------DILLLEDQNSKLSKERkLLEERISEFTSNLAEEEEKAKSL---------SKLKNKHEAMISDLEERlkkeEKG 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423178 2707 REAEEGVRRKQEELQLLEQQRQQQEKLLAEEnqrLRERLQRLEEEHRAALAHSEEIAASQATAVKAL 2773
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQIAELQAQIAE---LRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1507-1678 |
7.70e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.71 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1507 ERLAAVEAALEK-QRQLAEAHAQAKAQAEQEAQELQRRMQ---EEVARREEAAVDAQQQKrsIQEELQHLRQsseaeiQA 1582
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQkdlEEVRAKLEPYLEELQAK--LGQNVEELRQ------RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1583 KARQVEAAERSRLRIEEEIRVVRlqlETTERQRGGAEGELQALRARAEE-AEAQKRQAQEEAERLRRQVQDETQ----RK 1657
Cdd:pfam01442 76 EPYTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPyAEELRQKLAERLEELKESLAPYAEevqaQL 152
|
170 180
....*....|....*....|.
gi 2124423178 1658 RQAEAELAVRVKAEAEAAREK 1678
Cdd:pfam01442 153 SQRLQELREKLEPQAEDLREK 173
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2434-2618 |
7.85e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2434 AQEAARLRELAEED--LAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETqgf 2511
Cdd:COG1579 3 PEDLRALLDLQELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2512 qrtleaERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHD 2591
Cdd:COG1579 80 ------EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL---AELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|....*....
gi 2124423178 2592 AERLRQAIAELEREKEKLKQ--EAKLLQL 2618
Cdd:COG1579 151 LAELEAELEELEAEREELAAkiPPELLAL 179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2331-2492 |
8.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2331 VEQELTTLrLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAE---NRALILRDKD 2407
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEieeVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2408 NTQRVL-QEEAEKMKH-VAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMlkEKMQAVQEATRLKAEAELLQQQKEL 2485
Cdd:COG1579 81 QLGNVRnNKEYEALQKeIESLKRRISDLEDEILELMERIEELEEELAELEAEL--AELEAELEEKKAELDEELAELEAEL 158
|
....*..
gi 2124423178 2486 AQEQARR 2492
Cdd:COG1579 159 EELEAER 165
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
185-291 |
8.26e-03 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 39.32 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 185 VQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHR 260
Cdd:cd21306 16 VVKKSLITFVNKHLNK-----LNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDA 90
|
90 100 110
....*....|....*....|....*....|.
gi 2124423178 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21306 91 GLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1675-1729 |
8.43e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423178 1675 AREKQRALQaleefRLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1729
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1556-1702 |
8.56e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1556 VDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ 1635
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 1636 KRQAQEEAERLRRQVQdetqrkrQAEAElavrvkaeaEAAREKQRALQALEEFRLqaEEAERR------LRQA 1702
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2428-2569 |
8.85e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2428 ARLSVAAQEAARlrELAEEDLAQQRALAEKmLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE-DKEQMAQQLEQ 2506
Cdd:COG1566 74 ARLDPTDLQAAL--AQAEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlYKKGAVSQQEL 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423178 2507 ETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQArAEEDAQRFRKQAEEIGEKLHRTEL 2569
Cdd:COG1566 151 DEA--RAALDAAQAQLEAAQAQLAQAQAGLREEEELAA-AQAQVAQAEAALAQAELNLARTTI 210
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1345-1664 |
9.08e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1345 RQRELEQLGRQlryyRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEI----ERHGEKVEECQRFAK 1420
Cdd:pfam02029 12 RRRAREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTakreERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1421 QYINAIKDYELQLVTYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTR-YSElttltSQYIKFISETLRRMEEEERL 1497
Cdd:pfam02029 88 EFDPTIADEKESVAERKEnnEEEENSSWEKEEKRDSRLGRYKEEETEIREKeYQE-----NKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1498 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQeevARREEAAVDAQQQKRSIQEELQHLRQSSE 1577
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ---NGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1578 AEIQAKARQ-VEAAERSRLRIEEEirvvrlQLETTERQRGGAEGELQALRARAEE-----AEAQKRQAQEEAERL----- 1646
Cdd:pfam02029 240 AEVFLEAEQkLEELRRRRQEKESE------EFEKLRQKQQEAELELEELKKKREErrkllEEEEQRRKQEEAERKlreee 313
|
330
....*....|....*....
gi 2124423178 1647 -RRQVQDETQRKRQAEAEL 1664
Cdd:pfam02029 314 eKRRMKEEIERRRAEAAEK 332
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1873-1988 |
9.31e-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: 39.77 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1873 EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLaskARAEEESRSTSEKSKQRLEAEASRFRELAEEAAR 1952
Cdd:COG0711 30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEII---AEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIE 106
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423178 1953 lralAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1988
Cdd:COG0711 107 ----QERAKALAELRAEVADLAVAIAEKILGKELDA 138
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4428-4458 |
9.33e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 9.33e-03
10 20 30
....*....|....*....|....*....|.
gi 2124423178 4428 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4458
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
669-763 |
9.50e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 38.85 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 669 LRYLQDLLAWVEENQRRVDGAEWGVDLPSVEAQLGSHRGLHHSIEEFRAKIERARTDEGQL---SPATRGAYRDCLGRLD 745
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 2124423178 746 LQYAKLLNSSKGRLRSLE 763
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1657-2030 |
9.61e-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: 42.31 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1657 KRQAEAELAVRVKAEAEAAREKqralqaleefrLQAEEAERRLRQAEAERArqvqvaLETAQRSAEVELQSKRASFAEKT 1736
Cdd:NF033838 108 KEKSEAELTSKTKKELDAAFEQ-----------FKKDTLEPGKKVAEATKK------VEEAEKKAKDQKEEDRRNYPTNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1737 AQ-LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEALRL------RLQAEEvaqqkslaqaea 1809
Cdd:NF033838 171 YKtLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVES---KKAEATRLekiktdREKAEE------------ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1810 ekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLRAETEQGEQ---------QRQL 1878
Cdd:NF033838 236 ---------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPdkKENDAKSSDSSVGEEtlpspslkpEKKV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1879 LEEELARLQHEAAAATQKRQ-----------ELEAELA----KVR-AEMEVLLASKARAEEEsrstsEKSKQRLEAEASR 1942
Cdd:NF033838 307 AEAEKKVEEAKKKAKDQKEEdrrnyptntykTLELEIAesdvKVKeAELELVKEEAKEPRNE-----EKIKQAKAKVESK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1943 frelAEEAARLralaEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAF 2022
Cdd:NF033838 382 ----KAEATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAE 453
|
410
....*....|
gi 2124423178 2023 Q--RRRLEEQ 2030
Cdd:NF033838 454 EdyARRSEEE 463
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2353-2573 |
9.65e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2353 DEELQRLKAEVTEAARQRSQveEELfsLRVQMEELGKLKARIEAENRALILRDKDNTqrvlqEEAEKMKHVAEEAARLSV 2432
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEAR--KRL--VAKHGAEISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 2433 AAQEAARLRELAEEDLAqqralaekmlKEKMQAVQEAtrlKAEAELLQQQKELAQEQArrlqEDKEQMAQQLEQETQGFQ 2512
Cdd:PRK07735 75 AKQKREGTEEVTEEEKA----------KAKAKAAAAA---KAKAAALAKQKREGTEEV----TEEEKAAAKAKAAAAAKA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423178 2513 RTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2573
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE 198
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1506-1742 |
9.90e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1506 RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE--EVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAK 1583
Cdd:pfam19220 9 RVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRllELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1584 ARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELqalraraeEAEAQKRQA-QEEAERLRRQVQDETQRKRQAEA 1662
Cdd:pfam19220 89 VARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL--------AAETEQNRAlEEENKALREEAQAAEKALQRAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423178 1663 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLR----QAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1738
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAeletQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHR 240
|
....
gi 2124423178 1739 LERT 1742
Cdd:pfam19220 241 AERA 244
|
|
| |
