|
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 |
1.10e-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: 244.23 E-value: 1.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 183 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQV 262
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKI 75
|
90 100 110
....*....|....*....|....*....|
gi 2044209144 263 KLVNIRNDDIADGNPKLTLGLIWTIILHFQ 292
Cdd:cd21188 76 KLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
180-303 |
1.03e-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: 236.46 E-value: 1.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2044209144 260 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 303
Cdd:cd21235 76 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
305-410 |
5.39e-71 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 233.76 E-value: 5.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 2044209144 385 PEDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
178-301 |
8.09e-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: 231.41 E-value: 8.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 178 ATDERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYL 257
Cdd:cd21236 10 YKDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYL 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2044209144 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 |
1.11e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 2044209144 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 |
2.54e-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: 2.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2044209144 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 |
1.22e-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: 195.59 E-value: 1.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 2044209144 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 |
3.51e-52 |
|
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: 179.85 E-value: 3.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 304 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERdLGVTRLL 383
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 2044209144 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 2044209144 185 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 264
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77
|
90 100
....*....|....*....|....*....
gi 2044209144 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 |
7.37e-47 |
|
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: 164.23 E-value: 7.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 7 MPREQLRAVYEVLFREGVMVAKKDRRPrSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKDFNL-PKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 2044209144 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 |
2.65e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 2044209144 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 |
8.74e-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: 162.15 E-value: 8.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLK 85
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21246 86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
184-406 |
1.39e-44 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 174.36 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 184 RVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQ 261
Cdd:COG5069 8 KVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 262 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLF 340
Cdd:COG5069 84 VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 341 NAIIHRHRPMLIDMSKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 406
Cdd:COG5069 161 SALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
181-293 |
2.07e-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: 157.92 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 181 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 258
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2044209144 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21241 78 SKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
306-406 |
3.05e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 157.17 E-value: 3.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2044209144 386 EDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
181-293 |
3.32e-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: 157.35 E-value: 3.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 181 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 258
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2044209144 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
180-289 |
6.48e-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: 6.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLr 258
Cdd:cd21193 11 EERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL- 84
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21193 85 KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
293-408 |
1.48e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 149.82 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSV 372
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2044209144 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
305-410 |
1.76e-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: 149.39 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 2044209144 385 PEDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
181-293 |
1.93e-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: 143.82 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 181 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNK 77
|
90 100 110
....*....|....*....|....*....|...
gi 2044209144 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 |
4.03e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 142.84 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 302 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTR 381
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 2044209144 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 |
4.15e-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: 140.93 E-value: 4.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 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 |
4.39e-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: 140.19 E-value: 4.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 302 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTR 381
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 2044209144 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 |
2.15e-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: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21317 26 DEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLK 100
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21317 101 EQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| 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 2044209144 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 2044209144 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 |
1.06e-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: 135.59 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 183 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQ 261
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKG 77
|
90 100
....*....|....*....|....*...
gi 2044209144 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 2044209144 185 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 262
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGV 78
|
90 100
....*....|....*....|....*....
gi 2044209144 263 KLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21215 79 KLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1481-2117 |
2.76e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.01 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 IRETLRRMEE-EERLaeqqraeerERLAEVEAalEKQRQLAEAHAQAKaQAEReAEELQRRMQEevaRREEAAVdaqQQK 1559
Cdd:COG1196 174 KEEAERKLEAtEENL---------ERLEDILG--ELERQLEPLERQAE-KAER-YRELKEELKE---LEAELLL---LKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1560 RSIQEELQHLrqssEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEAterqrggAEGELQALRARAEEAEAQKRQAQEE 1639
Cdd:COG1196 235 RELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1640 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALEtaQRSAE 1719
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1720 VELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQK 1799
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1800 SLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIR--LRAETEQGEQQRQLLE 1877
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgaVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1878 EELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEET 1957
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1958 KRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 2037
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2038 RLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELgrirsnAEDTLRSKEQAELEATRQR 2117
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL------PEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1458-2045 |
3.00e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.01 E-value: 3.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1458 QEYVDLRTRYSEL-TTLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-------LAEAHAQAKAQ 1529
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1530 AEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER------------------SR 1591
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeaeaelaeaeealleaEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1592 VRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1671
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1672 AREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLR 1751
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1752 EEAERRAQQQAEAERAREEAEQELERWR-----LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQ 1826
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1827 AVRQRELAEQELEKQRQLAEGTAQQRLVAEQEliRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRA 1906
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1907 EMEVLLASKARAEEESRSTSEKSKQRleaeasrfRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAI 1986
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1987 SEATRLKTEAEIALKEKEAENERlrrlAEDE-AFQRRRLEEQAAQHkADIEERLAQLRKA 2045
Cdd:COG1196 763 EELERELERLEREIEALGPVNLL----AIEEyEELEERYDFLSEQR-EDLEEARETLEEA 817
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
180-293 |
3.90e-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: 134.28 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQK 76
|
90 100 110
....*....|....*....|....*....|....
gi 2044209144 260 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21231 77 NNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
290-406 |
1.40e-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: 133.26 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 290 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQA 369
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2044209144 370 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
309-410 |
1.67e-35 |
|
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: 132.17 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 309 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2044209144 388 VDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-114 |
4.94e-35 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 131.69 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 5 MLMPREQLRAVYEVLFREGVMVAKKDRrPRSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQ 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKDP-KGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90 100 110
....*....|....*....|....*....|
gi 2044209144 85 YLHLPPEIVPASLQRVRRPVAMVMPARRTP 114
Cdd:PTZ00034 80 YLHLPPDVFPATHKKKSVNFERKTEEEGSR 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1825-2393 |
6.19e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 144.31 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAegtAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKV 1904
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1905 RAEMEVLLASKARAEEESRSTseksKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEE---DAARQRAEAERVLAE 1981
Cdd:COG1196 287 QAEEYELLAELARLEQDIARL----EERRRELEERLEELEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1982 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKgLVEDTL 2061
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2062 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAE 2141
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2142 EEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2216
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2217 QSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2296
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2297 EQAALKQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFS 2376
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 2044209144 2377 VRVQMEELSKLKARIEA 2393
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1593-2193 |
1.36e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.15 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1593 RIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1672
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1673 REKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLre 1752
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1753 eaerraqqqAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE 1832
Cdd:COG1196 347 ---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1833 LAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLL 1912
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1913 ASKARAEEESRSTSEKSKQRLEAEAS------RFRELAEEAARLRALAEetkRQRQLAEEDAARQRAEAERVLAEKLAAI 1986
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAgavavlIGVEAAYEAALEAALAA---ALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1987 SEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQkglVEDTLRQRRQ 2066
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT---LAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2067 VEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAAR 2146
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2044209144 2147 QRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2193
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
305-403 |
2.72e-33 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 126.00 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 2044209144 385 PEDVDVPQPDEKSIITYVS 403
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1622-2204 |
5.70e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 141.23 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1622 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQRKRqaeaelalrVKAEAEAA------------REKQRALQALEDVR 1686
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAeryrelkeelkeLEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1687 LQAEEAERRLRQAEADRARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAER 1766
Cdd:COG1196 239 AELEELEAELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1767 AREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAE 1846
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1847 GTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTS 1926
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1927 EKSKQRLEAEASRFRELAEEAARLRALAEEtkrQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE 2006
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEA---EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2007 NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKA 2086
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2087 ELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEAR 2166
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
570 580 590
....*....|....*....|....*....|....*...
gi 2044209144 2167 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2204
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
306-406 |
8.64e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 124.44 E-value: 8.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2044209144 386 EDVDVPQPDEKSIITYVSSLY 406
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
184-294 |
9.21e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 122.17 E-value: 9.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 184 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ 261
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDE 88
|
90 100 110
....*....|....*....|....*....|....
gi 2044209144 262 -VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21311 89 gIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
185-293 |
9.80e-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: 9.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 185 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 264
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVEL 77
|
90 100
....*....|....*....|....*....
gi 2044209144 265 VNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21232 78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
185-293 |
1.04e-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: 121.63 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 185 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 262
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGI 78
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 263 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21227 79 KLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
305-403 |
1.77e-31 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 120.71 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 305 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 2044209144 385 PEDVDVPQPDEKSIITYVS 403
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
293-408 |
2.69e-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: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 293 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSV 372
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2044209144 373 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 408
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
309-411 |
4.15e-31 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 120.03 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 309 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 386
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 2044209144 387 DVDVPQPDEKSIITYVSSLYDAMPR 411
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
309-410 |
6.84e-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: 118.91 E-value: 6.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 309 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2044209144 388 VDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
311-406 |
8.80e-31 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 118.60 E-value: 8.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 311 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 389
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 2044209144 390 VPQPDEKSIITYVSSLY 406
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1458-2188 |
1.04e-30 |
|
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: 134.41 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1458 QEYVDLRTRYSELT-TLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqAKAQAEREAEE 1536
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1537 LQRRMQEEVARREeaavDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAE 1616
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1617 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRL 1696
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1697 RQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQEL- 1775
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1776 ---------------ERWRLKANEALRLRLQA---EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQ- 1836
Cdd:TIGR02168 518 lsgilgvlselisvdEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNi 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1837 --------ELEKQRQLAEGTAQQRL----VAE--QELIRLRAETEQGEQQRQLLEEELAR---LQREAAAATHKRQELEA 1899
Cdd:TIGR02168 598 egflgvakDLVKFDPKLRKALSYLLggvlVVDdlDNALELAKKLRPGYRIVTLDGDLVRPggvITGGSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 ELAKVRAEMEvLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVL 1979
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1980 AEKLAAISEATRLKTEAEIALKEKEAE----NERLRRLAEDEAFQRRRLEEQAAQHKaDIEERLAQLR---KASENELER 2052
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEieelEAQIEQLKEELKALREALDELRAELT-LLNEEAANLRerlESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2053 QKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELgrirsNAEDTLRSKEQAELEATRQRqlaaeeeqrrreaee 2132
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-----EALLNERASLEEALALLRSE--------------- 895
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2133 rvQKSLAAEEEAARQRKSALE-EVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2188
Cdd:TIGR02168 896 --LEELSEELRELESKRSELRrELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| 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 2044209144 180 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 289
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
181-295 |
3.27e-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: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 181 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLR 258
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 2044209144 259 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 295
Cdd:cd21191 78 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1849-2606 |
4.63e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.98 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1849 AQQRL-VAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAAtHKRQELEAELAKVRAEMEVLLASKARAEEEsrstse 1927
Cdd:COG1196 177 AERKLeATEENLERLEDILGE-------LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELE------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1928 kskqRLEAEAsrfRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAEN 2007
Cdd:COG1196 243 ----ELEAEL---EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2008 ERLRRLAEdeafQRRRLEEQAAQHKADIEERLAQLRKAsENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAE 2087
Cdd:COG1196 316 ERLEELEE----ELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2088 LELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARR 2167
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2168 LRERAEQESARQLQLAQEAAQKRLQAEEkahafavqqkeqelqqtlqqeqsmlerlraeaeaarraaeeaeearerAERE 2247
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLE------------------------------------------------AEAD 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2248 AAQSRRQVEEAERLKQLAEEQAQAQAqaqaaaekLRKEAEQEAARRAQAEQAALKQKQVADAEmekhkKFAEQTLRQKAQ 2327
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAV--------LIGVEAAYEAALEAALAAALQNIVVEDDE-----VAAAAIEYLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2328 VEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRnqvEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQ 2407
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR---EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2408 RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2487
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2488 RQLQEDKEQMAQQLAQETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgeklhr 2563
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL------ 800
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2044209144 2564 telaTQEKVTLVHTLEiqrqqsdhdaeRLRAAIAELEREKEKL 2606
Cdd:COG1196 801 ----SEQREDLEEARE-----------TLEEAIEEIDRETRER 828
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1038-1115 |
5.05e-30 |
|
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: 115.39 E-value: 5.05e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1038 LAWQCLSRDVQLIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 1115
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
309-408 |
1.53e-29 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 115.08 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 309 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 387
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 2044209144 388 VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
291-408 |
2.32e-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: 115.57 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 291 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAF 370
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2044209144 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 |
8.94e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 112.96 E-value: 8.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1370-2198 |
4.36e-28 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 125.71 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1370 AKQRQERIQAVPLanSQAVREQLQQEKELLEEIERYGEKV--DECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKP 1447
Cdd:NF041483 247 AESDQARRQAAEL--SRAAEQRMQEAEEALREARAEAEKVvaEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1448 KVQSGSESViQEYVDLRTRYSELTTLTSQYIKFI--RETLRRMEEEERLAEQ--QRAEERERLAEVEAALEKQRQLAEAH 1523
Cdd:NF041483 325 AEALKAEAE-QALADARAEAEKLVAEAAEKARTVaaEDTAAQLAKAARTAEEvlTKASEDAKATTRAAAEEAERIRREAE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1524 AQA---KAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE---IQAKAR-----QVEAAERSrv 1592
Cdd:NF041483 404 AEAdrlRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEgerIRGEARreavqQIEEAART-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1593 riEEEIrVVRLQLEATErQRGGAEGELQALRARA-EEAEAQKRQAQE-------EAERLRRQVQDESQRKRQAEAELALR 1664
Cdd:NF041483 482 --AEEL-LTKAKADADE-LRSTATAESERVRTEAiERATTLRRQAEEtlertraEAERLRAEAEEQAEEVRAAAERAARE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1665 VKAEAEAAREKQRALQALEDVRLQAeEAERRLRQAEADRARQVQVAlETAQRSAEVELQSKRASFAEKTaqleRTLQEEH 1744
Cdd:NF041483 558 LREETERAIAARQAEAAEELTRLHT-EAEERLTAAEEALADARAEA-ERIRREAAEETERLRTEAAERI----RTLQAQA 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1745 VAVAQLREEAERRAQQQAEAERAREEAEQELErwrlKANEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAE 1824
Cdd:NF041483 632 EQEAERLRTEAAADASAARAEGENVAVRLRSE----AAAEAERLKSEAQESADR--VRAEAAAAAERVGTEAAEALAAAQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELI---RLRAETEQGEQQRqLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:NF041483 706 EEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSV 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAEASRFRELA-EEAARLRALA-EETKRQRQLAEEDAARQRAEA 1975
Cdd:NF041483 785 AGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEA 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1976 ERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRrlEEQAAQHKADIEERLAQLRKASENELERQKG 2055
Cdd:NF041483 865 ERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAER 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2056 LVEDTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTLRSKEQAeleATRQRQLAAEEEQRrreaeervq 2135
Cdd:NF041483 940 LRDEARAEAERVRADAAAQAEQLIAEATGEAE------RLRAEAAETVGSAQQH---AERIRTEAERVKAE--------- 1001
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 2136 kslaAEEEAARQRKSALEEVERL--KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2198
Cdd:NF041483 1002 ----AAAEAERLRTEAREEADRTldEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
293-408 |
6.33e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 111.33 E-value: 6.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSV 372
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2044209144 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1489-2332 |
8.41e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 125.25 E-value: 8.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1489 EEEERLAEQQRAEERERLAEVEAALEkqrqlaeahAQAKAQAEREAEELQRrmQEEVARREEAAVDAQQQKRSIQEELQH 1568
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEE---------AKKKAEDARKAEEARK--AEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1569 LRQSSEAEIQAKARQVEAAERS-RVRIEEEIRvvrlqlEATERQRggaegeLQALRARAEEAEAQKRQAQEEAERLRRQV 1647
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAeEVRKAEELR------KAEDARK------AEAARKAEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1648 QDESQRKRQAEAELALRVKAEAEAaREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVAlETAQRSAEVelqsKRA 1727
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEI-RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA-DEAKKAEEK----KKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1728 SFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeaerareeaeqelerwRLKANEALRLRLQAEEVAQQKSlaqaeae 1807
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEA-----------------------------------KKKAEEAKKKADAAKKKAEEAK------- 1342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1808 kqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQ---ELIRLRAETEQGEQQRQLLEEELARLQ 1884
Cdd:PTZ00121 1343 --------------KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkadAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1885 REAAAATHKRQeleAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEaEASRFRELAEEAARLRALAEETKRQRQLA 1964
Cdd:PTZ00121 1409 ELKKAAAAKKK---ADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1965 EEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlrrlaedEAFQRRRLEEQaaqHKADIEERLAQLRK 2044
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK-------KAEEAKKADEA---KKAEEKKKADELKK 1553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2045 ASENELERQKGLVEDtlrQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAeee 2124
Cdd:PTZ00121 1554 AEELKKAEEKKKAEE---AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--- 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2125 qrrreaeervqkslaAEEEaarqRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2204
Cdd:PTZ00121 1628 ---------------AEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2205 KEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqlaeeqaqaqaqaqaAAEKLRK 2284
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-----------------KAEEAKK 1751
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 2044209144 2285 EAEqeaarraqaeqaalKQKQVADAEMEKHKKFAEQTLRQKAQVEQEL 2332
Cdd:PTZ00121 1752 DEE--------------EKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1865-2609 |
1.01e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.87 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1865 ETEQGEQQRQLLEEElARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFREL- 1943
Cdd:PTZ00121 1089 ADEATEEAFGKAEEA-KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAe 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1944 ----AEEAARLRAL--AEETKRQRQLAEEDAARQ-----RAEAERVLAE--------KLAAISEATRLKTEAEIALK-EK 2003
Cdd:PTZ00121 1168 earkAEDAKKAEAArkAEEVRKAEELRKAEDARKaeaarKAEEERKAEEarkaedakKAEAVKKAEEAKKDAEEAKKaEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2004 EAENERLRRLAEDEAFQRRRleeQAAQHKADIEERLAQLRKASEneleRQKGLVEDTLRQRRQVEEeilalkasfekaAA 2083
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFAR---RQAAIKAEEARKADELKKAEE----KKKADEAKKAEEKKKADE------------AK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2084 GKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVE 2163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2164 EARR---LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSmlerlraeaeaarraaeEAEEA 2240
Cdd:PTZ00121 1389 EKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-----------------DEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2241 RERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAqaaaeKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQ 2320
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-----EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2321 TlrQKAQVEQELTTLRLQLEETDHQKSILDEELQrlKAEVTEAARQRNQVEEELFSVRVQMEELSKL-KARIEAENRALI 2399
Cdd:PTZ00121 1527 A--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeEARIEEVMKLYE 1602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2400 LRDKDNTQRFLQEEAEKMKqvAEEAARlsvaAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEllqQQ 2479
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE---ED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2480 KELAQEqARQLQEDKEQMAQQLAQETQgfqrtlEAERQRQLEMSAEAERLKlrVAEMSRAQARAEEDAQRFRKQAEEIGE 2559
Cdd:PTZ00121 1674 KKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK--AEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2560 KLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAE-LEREKEKLQEE 2609
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRME 1795
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
293-408 |
1.45e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 110.20 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSV 372
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2044209144 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
311-406 |
2.90e-26 |
|
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: 105.70 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 311 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 389
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 2044209144 390 VPQPDEKSIITYVSSLY 406
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
293-408 |
3.44e-26 |
|
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: 106.31 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 293 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSV 372
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2044209144 373 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1866-2673 |
1.15e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 118.32 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1866 TEQGEQQRQLLEEELARLQREAAAAThkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFREL-- 1943
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1944 AEEAARlralAEETKRQrqlAEEdaARQRAEAERvlAEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 2021
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2022 RRLEEQaaqHKADIEERLAQLRKASENELERQKGLVEDTlrqrRQVEEeilALKASFEKaaagKAELELELGRIRSNAED 2101
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDARKAEAARKAEEE----RKAEE---ARKAEDAK----KAEAVKKAEEAKKDAEE 1241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2102 TLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEE-EAARQRKSALE--------EVERLKAKVEEARRLREra 2172
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAEEKKKADEakkaeekkKADEAKKKAEEAKKADE-- 1319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2173 EQESARQLQLAQEAAQKRlqAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSR 2252
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKK--AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2253 RQVEE----AERLKQLAEEQAQAQAQAQAAAEKlRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQT-----LR 2323
Cdd:PTZ00121 1398 KKAEEdkkkADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkadeAK 1476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2324 QKAQVEQELTTLRLQLEETDHQKsildEELQRlKAEVTEAARQRNQVEEelfsvRVQMEELSKLKARIEAEN--RALILR 2401
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKA----DEAKK-AAEAKKKADEAKKAEE-----AKKADEAKKAEEAKKADEakKAEEKK 1546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2402 DKDNTQRFLQ----EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQ 2477
Cdd:PTZ00121 1547 KADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2478 QQKELAQ--EQARQLQEDKEQMAQQLAQETQGfqrtlEAERQRQLEMSAEAERLKlrvAEMSRaqaRAEEDAqrfRKQAE 2555
Cdd:PTZ00121 1627 KAEEEKKkvEQLKKKEAEEKKKAEELKKAEEE-----NKIKAAEEAKKAEEDKKK---AEEAK---KAEEDE---KKAAE 1692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2556 EIGEKlhrtelatQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRAL 2635
Cdd:PTZ00121 1693 ALKKE--------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
810 820 830
....*....|....*....|....*....|....*...
gi 2044209144 2636 QESFLSEKDRlLQRERFIEQEKAKLEQLFRDEVAKAQK 2673
Cdd:PTZ00121 1765 EEEKKAEEIR-KEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
184-291 |
1.50e-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: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERE 77
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21228 78 SIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
305-411 |
2.29e-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: 103.52 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 305 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVY--RQTNLENLDQAFSVAERDLGVTR 381
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 382 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 411
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
180-293 |
4.31e-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: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 258
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 2044209144 259 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1495-2557 |
6.28e-25 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 115.31 E-value: 6.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1495 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAEREAEELQRRMQ--EEVARRE---EAAVD-----AQQQKRSIQ 1563
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQQldQELAERRqtvESHVNenvawAEQLRARTE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1564 EELQHLRQSSEAEiqakARQVEAAERSRVRieeeirvvRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERL 1643
Cdd:NF041483 163 SQARRLLDESRAE----AEQALAAARAEAE--------RLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1644 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQaeEAERRLRQAEADRARQVQVALETAqrsaevelq 1723
Cdd:NF041483 224 LNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA--------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1724 SKRASFAEKT-AQLERTLQEEhvaVAQLREEAERRAQQQAEAERAREE-AEQELERWRLKANEALRLRLQAEEVAQQKSL 1801
Cdd:NF041483 293 AKQLASAESAnEQRTRTAKEE---IARLVGEATKEAEALKAEAEQALAdARAEAEKLVAEAAEKARTVAAEDTAAQLAKA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1802 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLVAEQELIRLRAETEQGEQQRQLLEEEL 1880
Cdd:NF041483 370 ARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1881 ARLQREAAAATHK-----RQELEAELAKVRAEMEVLLA-SKARAEE-ESRSTSEKSKQRLEA--EASRFRELAE------ 1945
Cdd:NF041483 450 EQLRAEAVAEGERirgeaRREAVQQIEEAARTAEELLTkAKADADElRSTATAESERVRTEAieRATTLRRQAEetlert 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1946 --EAARLRALAEETKRQRQLAEEDAARQ-RAEAERVLAEKLA-AISEATRLKTEAE-------IALKEKEAENERLRRLA 2014
Cdd:NF041483 530 raEAERLRAEAEEQAEEVRAAAERAARElREETERAIAARQAeAAEELTRLHTEAEerltaaeEALADARAEAERIRREA 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2015 EDEAfqrRRLEEQAAqhkadieERLAQLRKASENELERqkglvedtLRQRRQVEeeilalkasfekAAAGKAELELELGR 2094
Cdd:NF041483 610 AEET---ERLRTEAA-------ERIRTLQAQAEQEAER--------LRTEAAAD------------ASAARAEGENVAVR 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2095 IRSNA-EDTLRSKEQAELEATRQRqlAAEEEQRRREAEERVQKSLAAEEEAARQRKSAleeVERLKAKVEEARRLRERAE 2173
Cdd:NF041483 660 LRSEAaAEAERLKSEAQESADRVR--AEAAAAAERVGTEAAEALAAAQEEAARRRREA---EETLGSARAEADQERERAR 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2174 QESARQLQlaqeAAQKRL-QAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSR 2252
Cdd:NF041483 735 EQSEELLA----SARKRVeEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTR 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2253 RQV-EEAERLKqlaEEQAQAQAQAQAAAEKLRkeaeqeaarraqaeqaalkqkQVADAEMEKHKKFAEQTLRQkAQVEQE 2331
Cdd:NF041483 811 TEAqEEADRVR---SDAYAERERASEDANRLR---------------------REAQEETEAAKALAERTVSE-AIAEAE 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2332 lttlRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVR----VQMEELSKLKARIEAENRALILRDKDNTQ 2407
Cdd:NF041483 866 ----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLR 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2408 RFLQEEAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavqEATRLKAEAELLQQQKELAQE 2485
Cdd:NF041483 942 DEARAEAERVRADAAAQAEqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEA-----ERVKAEAAAEAERLRTEAREE 1016
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2486 QARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQrfRKQAEEI 2557
Cdd:NF041483 1017 ADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAA--RKEAERI 1086
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
307-406 |
8.09e-25 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 101.87 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 307 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 386
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 2044209144 387 D-VDVPQPDEKSIITYVSSLY 406
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
184-294 |
1.12e-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: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDRE 89
|
90 100 110
....*....|....*....|....*....|....
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21310 90 HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1821-2517 |
1.17e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 114.85 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1821 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLVAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAE 1900
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEE--ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1901 LAK----VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRElAEEAARLRAL--AEETKRQRQLAEEDAARQRAE 1974
Cdd:PTZ00121 1174 DAKkaeaARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARK-AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1975 AERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED--EAFQRRRLEEqaAQHKADIEERLAQLRKASENELER 2052
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2053 QKGLvedtlrqRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAE-----LEATRQRQLAAEEEQRR 2127
Cdd:PTZ00121 1331 ADAA-------KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADEAKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2128 REAEERVQKSLAAEEEAARQRKSALE--EVERLKAKVEEARR---LRERAEQ-----ESARQLQLAQEAAQKRLQAEEKA 2197
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKadeAKKKAEEakkaeEAKKKAEEAKKADEAKKKAEEAK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2198 HAFAVQQKEQELQQTLQQEQSmlerlRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQA 2277
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKK-----AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2278 AAEKLRKEAEQEAARRAQAEQAALKQ--KQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQR 2355
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE-KKKVEQ 1637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2356 LKAEVTEAARQRNQV--EEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQE 2433
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2434 AARLRQLAEEDLAQQRALAEKMLKEKMQAvQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQEtQGFQRTLE 2513
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE-EDEKRRME 1795
|
....
gi 2044209144 2514 AERQ 2517
Cdd:PTZ00121 1796 VDKK 1799
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1483-2197 |
2.44e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 113.38 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1483 ETLRRMEEEE--RLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-EAEELQRRMQEEVARREEAAVDAQQQK 1559
Cdd:NF041483 155 EQLRARTESQarRLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARaEAEAILRRARKDAERLLNAASTQAQEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1560 RSIQEEL---------QHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEG--ELQALRARAE- 1627
Cdd:NF041483 235 TDHAEQLrsstaaesdQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESanEQRTRTAKEEi 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1628 -----EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAE------AEAAREKQRAL-----QALEDVRLQAEE 1691
Cdd:NF041483 315 arlvgEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEdtaaqlAKAARTAEEVLtkaseDAKATTRAAAEE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1692 AERRLRQAEADRARQVQVALETAQ-------------RSAEVELQSKRASF--------AEKTAQLERTLQE-EHVAVAQ 1749
Cdd:NF041483 395 AERIRREAEAEADRLRGEAADQAEqlkgaakddtkeyRAKTVELQEEARRLrgeaeqlrAEAVAEGERIRGEaRREAVQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1750 LREEAERRAQ----QQAEAERAREEAEQELERWRLKANE-ALRLRLQAEEVAQQkslaqaeaekqkeEAEREARRRGKAE 1824
Cdd:NF041483 475 IEEAARTAEElltkAKADADELRSTATAESERVRTEAIErATTLRRQAEETLER-------------TRAEAERLRAEAE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAE-GTAQQRLVAEQELIRLRAETEQ----GEQQRQLLEEELARLQREAAAATHKRQELEA 1899
Cdd:NF041483 542 EQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErltaAEEALADARAEAERIRREAAEETERLRTEAA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 E-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAsrfrelAEEAARLRALAEET-KRQRQLAEEDAARQRA 1973
Cdd:NF041483 622 ErirtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEA------AAEAERLKSEAQESaDRVRAEAAAAAERVGT 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1974 EAERVLAeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDE-----AFQRRRLEEQAAQHKADIEE---RLAQLRKA 2045
Cdd:NF041483 696 EAAEALA---AAQEEAARRRREAEETLGSARAEADQERERAREQseellASARKRVEEAQAEAQRLVEEadrRATELVSA 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2046 SENELERQKGLVEDTlrqRRQVEEEILALKASFEKAAA-GKAELELELGRIRSnaeDTLRSKEQAELEATRQRQlaaeee 2124
Cdd:NF041483 773 AEQTAQQVRDSVAGL---QEQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS---DAYAERERASEDANRLRR------ 840
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 2125 qrrreaeERVQKSLAAEEEAARQRKSALEEVERLKAKVEE-ARRLRERAeqeSARQLQLAQEAAQKRLQAEEKA 2197
Cdd:NF041483 841 -------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEA---SDTLASAEQDAARTRADAREDA 904
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
309-409 |
2.76e-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: 100.23 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 309 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 388
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 2044209144 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 2044209144 188 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKL 264
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKV 76
|
90 100
....*....|....*....|....*.
gi 2044209144 265 VNIRNDDIADGnPKLTLGLIWTIILH 290
Cdd:smart00033 77 VLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
306-406 |
5.95e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 99.04 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 2044209144 386 EDVDVPQ-PDEKSIITYVSSLY 406
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1160-1705 |
6.44e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1160 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1239
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1240 RSTQGAEEVLRAHEEQLKEAQAvpATLPELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDVEVE 1319
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1320 RWRERVAPLLERWQAALAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELL 1399
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1400 EEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesvIQEYVDLRTRYSELTTLTSQYIK 1479
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA------VLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1480 FIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQ------AKAQAEREAEELQRRMQEEVARREEAAV 1553
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAigaavdLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1554 DAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQrggaEGELQALRARAEEAEAQK 1633
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL----AEEELELEEALLAEEEEE 706
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1634 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRAR 1705
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| 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 2044209144 185 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-V 262
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgV 78
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 263 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:pfam00307 79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-112 |
3.08e-23 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 97.30 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 5 MLMPREQLRAVYEVLFREGVMVAKKDRRpRSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWRHFYWYLTNEGIAHLRQ 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|....*...
gi 2044209144 85 YLHLPPEIVPASLQRVRRPVAmvMPARR 112
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ--RPQRR 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1495-2199 |
6.69e-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: 108.61 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1495 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAER------EAEELQRRMQeevARREEAAVDAQQQKRSIQEELQ 1567
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILnELERQLKSLERQAE-KAERykelkaELRELELALL---VLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1568 HLRQSSEAEIQAKarqveaaersrvriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR-- 1645
Cdd:TIGR02168 253 EELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERql 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1646 -----QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLR--QAEADRARQVQVALETAQRSA 1718
Cdd:TIGR02168 319 eeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEelEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1719 EVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQ 1798
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1799 KSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL-------------EKQRQLA-----EGTAQQRLVAEQELI 1860
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlselisvDEGYEAAieaalGGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1861 RLRAET-EQGEQQR-------QLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLA----------SKARAEEES 1922
Cdd:TIGR02168 559 KKAIAFlKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1923 RSTSEK-----------------SKQRLEAEASRF---RELAEEAARLRALAEETKRQRQlAEEDAARQRAEAERVLAEK 1982
Cdd:TIGR02168 639 KKLRPGyrivtldgdlvrpggviTGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1983 LAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASENELERQKGLVEDTLR 2062
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2063 QRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQlaaeeeqrrreAEERVQKSLAAEE 2142
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE-----------DIESLAAEIEELE 865
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2143 EAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLqlaQEAAQKRLQAEEKAHA 2199
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEEL---RELESKRSELRRELEE 919
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
306-410 |
7.37e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.01 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 2044209144 386 EDVDVPQPDEKSIITYVSSLYDAMP 410
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1829-2620 |
9.06e-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: 108.22 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1829 RQRELAEQELEKQRQLAEgtaqqrlvAEQELIRLRAETeqgeqqrqlLEEELARLQREAAAATHKRQELEAELAKVRAEM 1908
Cdd:TIGR02168 207 RQAEKAERYKELKAELRE--------LELALLVLRLEE---------LREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1909 EVLLASKARAEEEsrstsekskqrLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISE 1988
Cdd:TIGR02168 270 EELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1989 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQH---KADIEERLAQLRKASeNELERQKGLVEDTLRQRR 2065
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLN-NEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2066 QVEEEILALKASFEKAAagKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRrreaeervQKSLAAEEEAA 2145
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2146 RQRKSALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQK 2205
Cdd:TIGR02168 488 QARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2206 EQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRR--------QVEEAERLKQLAEEQAQAQAQAQ- 2276
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllgGVLVVDDLDNALELAKKLRPGYRi 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2277 -AAAEKLRKEAEQEAARRAQAEQAALKQKQvadaEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQR 2355
Cdd:TIGR02168 648 vTLDGDLVRPGGVITGGSAKTNSSILERRR----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2356 LKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAEnRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAA 2435
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2436 RLRQLAEEDLAQQRALAEkmlkekmQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQG---FQRTL 2512
Cdd:TIGR02168 803 EALDELRAELTLLNEEAA-------NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieeLESEL 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2513 EAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVHTLEIQRQQSDHDAER 2591
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTLEE 955
|
810 820
....*....|....*....|....*....
gi 2044209144 2592 LRAAIAELEREKEKLQEEATLLQQKSEEM 2620
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1620-2598 |
1.29e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 107.99 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1620 QALRARAEEAEAQKRQAQEEAERLRRQvqdeSQRKRQAEAELALRVKAE--AEAAREKQRALQALEDVRLQAE-EAERRL 1696
Cdd:NF041483 76 QLLRNAQIQADQLRADAERELRDARAQ----TQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1697 RQAEADRARQVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeAERAREEAEQ 1773
Cdd:NF041483 152 AWAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE--------------------AESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1774 ELERWRLKANEALR-LRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQr 1852
Cdd:NF041483 212 ILRRARKDAERLLNaASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAE- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1853 lVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAA-ATHKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEK 1928
Cdd:NF041483 288 -AKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1929 SKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVlAEKLAAIS----------------EATRL 1992
Cdd:NF041483 367 AKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ-AEQLKGAAkddtkeyraktvelqeEARRL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1993 KTEAEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIE------------------ERLAQLRKASENE 2049
Cdd:NF041483 446 RGEAEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADelrstataeservrteaiERATTLRRQAEET 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2050 LERQKGLVEdtlRQRRQVEEEILALKASFEKAA------------AGKAELELELGRIRSNAEDTLRSKEQAELEatrqr 2117
Cdd:NF041483 526 LERTRAEAE---RLRAEAEEQAEEVRAAAERAArelreeteraiaARQAEAAEELTRLHTEAEERLTAAEEALAD----- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2118 qlaaeeeqrrreaeervqkslaAEEEAARQRKSALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEK 2196
Cdd:NF041483 598 ----------------------ARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAE 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2197 AHAFAVQQKEQELqqtlqqeqsmlerlraeaeaarraaeeaeeareraereaaqsrrqvEEAERLKqlaeeqaqaqAQAQ 2276
Cdd:NF041483 653 GENVAVRLRSEAA----------------------------------------------AEAERLK----------SEAQ 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2277 AAAEKLRKEAEQEAARRAQAEQAALKQKQvadAEMEKHKKFAEQTL------------RQKAQVEQELTTLRLQLEETDH 2344
Cdd:NF041483 677 ESADRVRAEAAAAAERVGTEAAEALAAAQ---EEAARRRREAEETLgsaraeadqereRAREQSEELLASARKRVEEAQA 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2345 QKSILDEELQRLKAEVTEAARQR-NQVEEELFSVRVQM-EELSKLkaRIEAENRAlilrdkDNTQRFLQEEAEKMKqvAE 2422
Cdd:NF041483 754 EAQRLVEEADRRATELVSAAEQTaQQVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SD 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2423 EAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQEATRLKAEAEllqqqkELAQeQARQLQEDKEQMAQQLA 2502
Cdd:NF041483 824 AYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDAS------EYAQ-RVRTEASDTLASAEQDA 893
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2503 QETQGFQRTlEAERQRQlEMSAEAERLKLRV-AEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTlvhtleiq 2581
Cdd:NF041483 894 ARTRADARE-DANRIRS-DAAAQADRLIGEAtSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLI-------- 963
|
1050
....*....|....*..
gi 2044209144 2582 rQQSDHDAERLRAAIAE 2598
Cdd:NF041483 964 -AEATGEAERLRAEAAE 979
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
937-1003 |
3.63e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 92.71 E-value: 3.63e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 937 QLKPRdqAQPMRGRVPLQAVCDYKQVEVTVHKGDQCQLLGPAQPAHWKVLSSSGSEAAVPSVCFLVP 1003
Cdd:pfam17902 1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2000-2755 |
1.13e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.84 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2000 LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENE-LERQKGLVEDTLRQRRQVEEEilalkASF 2078
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEaTEEAFGKAEEAKKTETGKAEE-----ARK 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2079 EKAAAGKAELELELGRIRsNAEDTLRSKEQAELEATRQRQLAAEEEQRRReaeerVQKSLAAEE----EAARQ----RKS 2150
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIARKAEDARK-----AEEARKAEDakkaEAARKaeevRKA 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2151 A----LEEVERLKA--KVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLR 2224
Cdd:PTZ00121 1191 EelrkAEDARKAEAarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2225 AEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAeqaalKQK 2304
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK-----KAA 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2305 QVADAEMEKHKKFAEQTLRQKAQVEQElttlrlqlEETDHQKSildEELQRLKAEVTEAARQRNQVEEElfsvRVQMEEL 2384
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKK--------KEEAKKKA---DAAKKKAEEKKKADEAKKKAEED----KKKADEL 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2385 SKlkaRIEAENRALILRDKDNTQRflqeEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2464
Cdd:PTZ00121 1411 KK---AAAAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2465 EATRLKAEAEllqQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKlRVAEMSRAQA--R 2542
Cdd:PTZ00121 1484 KADEAKKKAE---EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-KADELKKAEElkK 1559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2543 AEE--DAQRFRKQAEEIGEKLHRTELATQ-EKVTLVHTLEIQRQQSDHDAERLRAAiaelEREKEKLQEeatllQQKSEE 2619
Cdd:PTZ00121 1560 AEEkkKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEE-----LKKAEE 1630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2620 mqvvqqeqLLQETRALQESFLSEKDRLLQRERFIEQEKAKLEQLFR---DEVAKAQKLReeqqRQQQQMEQEREQLVASM 2696
Cdd:PTZ00121 1631 --------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeEDKKKAEEAK----KAEEDEKKAAEALKKEA 1698
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 2697 EEARQ----RQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHRAALAH 2755
Cdd:PTZ00121 1699 EEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
306-404 |
2.22e-21 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 91.91 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVY-RQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 2044209144 385 PEDVDVPQPDEKSIITYVSS 404
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1245-2015 |
4.75e-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: 102.44 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1245 AEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDVEVERWRER 1324
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1325 VAPLLERWQAALAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEIER 1404
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1405 YGEKvdecqqlakqyINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfIRET 1484
Cdd:TIGR02168 405 LEAR-----------LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1485 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER------------EAEE---------LQRRMQE 1543
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEgyeaaieaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1544 EVARREEAAVDAQQ---QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLE-------------- 1606
Cdd:TIGR02168 550 VVVENLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvd 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1607 ----ATERQR----GG----AEGEL---QALRARAEEAEAQKRQAQE-EAERLRRQVQDESQRKRQAEAELalrvkaeAE 1670
Cdd:TIGR02168 630 dldnALELAKklrpGYrivtLDGDLvrpGGVITGGSAKTNSSILERRrEIEELEEKIEELEEKIAELEKAL-------AE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1671 AAREKQRALQALEDVRLQAEEAERRLRQAEAD----RARQVQVALETAQRSAEV-ELQSKRASFAEKTAQLERTLQEEHV 1745
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDlarlEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEA 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1746 AVAQLreeaerraqqqaEAERAREEAEQELERWRLKANEAlRLRLQAEEVAQQKSlaqaeaekqkeeaerearrrgkAEE 1825
Cdd:TIGR02168 783 EIEEL------------EAQIEQLKEELKALREALDELRA-ELTLLNEEAANLRE----------------------RLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1826 QAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVR 1905
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1906 AEMEVLLASKARAEEEsRSTSEKSKQRLEAEASRFRE-LAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAE--- 1981
Cdd:TIGR02168 908 SKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgp 986
|
810 820 830
....*....|....*....|....*....|....*
gi 2044209144 1982 -KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 2015
Cdd:TIGR02168 987 vNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1245-2069 |
8.58e-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: 101.67 E-value: 8.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1245 AEEVLRAHE--EQLKEAQAVPATLpELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDveverwr 1322
Cdd:TIGR02168 209 AEKAERYKElkAELRELELALLVL-RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1323 ERVAPLLERWQAALAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQavplansqavrEQLQQEKELLEEI 1402
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-----------EELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1403 ErygEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDlrtrySELTTLTSQYIKFIR 1482
Cdd:TIGR02168 350 K---EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1483 ETLrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEevARREEAAvdAQQQKRSI 1562
Cdd:TIGR02168 422 EIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQ--LQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1563 QEELQHLRQSSEAEIQAKArqveaaerSRVRIEEEIRVVRLQLEATERQRGGAE----GELQALRARAEEAEAQKRQAQE 1638
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLK--------NQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1639 EAERLRR----------QVQDESQRKRQAEAELALRVKAEAEAAREK-QRALQALEDVRLQAEEAERRLRQAEADRARQV 1707
Cdd:TIGR02168 567 QNELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1708 QVALE--------------TAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQ 1773
Cdd:TIGR02168 647 IVTLDgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1774 ELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTAQQRL 1853
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1854 VAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRL 1933
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED----IESLAAEI 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1934 EAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTE-AEIALKEKEAEN----- 2007
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKlAQLELRLEGLEVridnl 941
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 2008 -ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRK----------ASENELERQKGLVEDTLRQRRQVEE 2069
Cdd:TIGR02168 942 qERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENkikelgpvnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
310-407 |
1.18e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 90.10 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 310 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 388
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2044209144 389 DVPQPDEKSIITYVSSLYD 407
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1476-2112 |
1.22e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 100.88 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1476 QYIKFIRETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAEREAEELQRRMQEEV 1545
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1546 ARREEaavdaqqqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQAL 1622
Cdd:PRK02224 286 ERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1623 RARAEEaeaqkrqAQEEAERLrrqvqdesqrkrqaEAELalrvkAEAEAAREKQRAlqALEDVRLQAEEAERRLRQAEad 1702
Cdd:PRK02224 355 EERAEE-------LREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAP-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1703 rarqvqVALETAQRSAEvELQSKRASFAEKTAQLERTLQEehvavaqlreeaerraqqqaeaerareeaeqelERWRLKA 1782
Cdd:PRK02224 405 ------VDLGNAEDFLE-ELREERDELREREAELEATLRT---------------------------------ARERVEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1783 NEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAEqELEKQRqLAEGTAQQRLVAEQELIRL 1862
Cdd:PRK02224 445 AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA-ELEDLE-EEVEEVEERLERAEDLVEA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1863 RAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLEAEASRFRE 1942
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1943 LAEEAARLRALAEetkrqrQLAEEDAARQRAEAervLAEKLAAISEatrLKTEAEIALKEKeaeNERLRRLAEDeaFQRR 2022
Cdd:PRK02224 584 LKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDERRERLAEK---RERKRELEAE--FDEA 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2023 RLEE------QAAQHKADIEERLAQLRkASENELERQKGLVE------DTLRQRR-QVEEEILALKASFEKAaagkAELE 2089
Cdd:PRK02224 647 RIEEaredkeRAEEYLEQVEEKLDELR-EERDDLQAEIGAVEneleelEELRERReALENRVEALEALYDEA----EELE 721
|
650 660
....*....|....*....|...
gi 2044209144 2090 LELGRIRSNaedtLRSKEQAELE 2112
Cdd:PRK02224 722 SMYGDLRAE----LRQRNVETLE 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1941-2713 |
2.45e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1941 RELAEEAA---RLRALAEETKRQRQLAEEDAARqraeAERVLAEKLAAISeatRLKTEAEIALKEKEAENERLRRLAEDE 2017
Cdd:COG1196 158 RAIIEEAAgisKYKERKEEAERKLEATEENLER----LEDILGELERQLE---PLERQAEKAERYRELKEELKELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2018 AFQRRRLEEQAAQHKADIEERLAQLRKAsENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRS 2097
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2098 NAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESA 2177
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2178 RQLQLAQEAAQKRLQAEEKAHAFAVQQkeqelqqtlqqeqsmlerlraeaEAARRAAEEAEEARERAEREAAQSRRQVEE 2257
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERL-----------------------ERLEEELEELEEALAELEEEEEEEEEALEE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2258 AERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRL 2337
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2338 QLEetdhqksILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARieaenRALILRDKDNTQRFLQEEAEKM 2417
Cdd:COG1196 527 AVL-------IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-----RATFLPLDKIRARAALAAALAR 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2418 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK---AEAELLQQQKELAQEQARQLQEDK 2494
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRevtLEGEGGSAGGSLTGGSRRELLAAL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2495 EQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL 2574
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2575 VHTLEIQRQQSDHDAERLRAAIAELERekeklqeeatllqqkseemqvvqqeqllQETRALQESflsekDRLLQRERFIE 2654
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEALGP----------------------------VNLLAIEEY-----EELEERYDFLS 801
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2655 QEKAKLEqlfrdevakaqklreeqqrqqqqmeqereqlvASMEEARQRQREAEEGVRRK 2713
Cdd:COG1196 802 EQREDLE--------------------------------EARETLEEAIEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2320-2839 |
3.50e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2320 QTLRQKAQVEQELTTLRLQLEETDHQKSILdeELQRLKAEVTEAARQRNQVEEELfsvRVQMEELSKLKARIEaENRALI 2399
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAEL---EELEAELAELEAELE-ELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2400 LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEkmlkekmqavQEATRLKAEAELLQQQ 2479
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE----------ELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2480 KELAQE--QARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEI 2557
Cdd:COG1196 347 EEAEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2558 GEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRALQE 2637
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2638 SFLSEKDRLLQRERFIEQEKAKL----EQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRK 2713
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLigveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2714 QEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQAAASKALPNGRDVLdGPAAEAEPEHAFDGL 2793
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT-LEGEGGSAGGSLTGG 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2044209144 2794 RRKVPAQRLQEVGILSAEELQRLAQGRTTVAELAQREDVRQYLQGR 2839
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
184-294 |
3.78e-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: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRE 90
|
90 100 110
....*....|....*....|....*....|....
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21309 91 SIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
306-406 |
4.12e-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: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDP 385
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 2044209144 386 EDVDV--PQPDEKSIITYVSSLY 406
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
184-294 |
4.44e-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: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 184 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRE 93
|
90 100 110
....*....|....*....|....*....|....
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21308 94 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
306-405 |
5.42e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 87.92 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 2044209144 386 ED-VDVPQPDEKSIITYVSSL 405
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1097-2175 |
6.80e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 98.74 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1097 QAEREYGSCSRHYQQLLQSAEQGAQE-ESRCQRCISELKDIRL-QLEACETRTVHRLRLPlDKEPARECAQRIAEQQKAQ 1174
Cdd:NF041483 251 QARRQAAELSRAAEQRMQEAEEALREaRAEAEKVVAEAKEAAAkQLASAESANEQRTRTA-KEEIARLVGEATKEAEALK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1175 AEVEGLgkgVARLSAEAEKVLAlpEPSPAAPTLRSEleltlgkleqvrslsaiyleklKTISLVIRSTQGAEEVLRAHEE 1254
Cdd:NF041483 330 AEAEQA---LADARAEAEKLVA--EAAEKARTVAAE----------------------DTAAQLAKAARTAEEVLTKASE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1255 QLKeaqavpatlpelEATKAA---LKKLRVQAEAQQpvfDALRDElrgAQEVGERLQrqhGERDVEVERWRERVAPLLEr 1331
Cdd:NF041483 383 DAK------------ATTRAAaeeAERIRREAEAEA---DRLRGE---AADQAEQLK---GAAKDDTKEYRAKTVELQE- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1332 wqaalaqtdvRQRELEQLGRQLRyyresadplgawlQDAKQRQERIQAvplansQAVREQLQQekelLEEIERYGEKVde 1411
Cdd:NF041483 441 ----------EARRLRGEAEQLR-------------AEAVAEGERIRG------EARREAVQQ----IEEAARTAEEL-- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1412 cqqLAKqyinAIKDYELQLVTYKAQLEPVASPAK------KPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIRETL 1485
Cdd:NF041483 486 ---LTK----AKADADELRSTATAESERVRTEAIerattlRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAAREL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAEELQRRMQEEVAR-REEAAvdaqqqkrsiqE 1564
Cdd:NF041483 559 R--EETERAIAARQAEAAEELTRLHTEAEERLTAAE---EALADARAEAERIRREAAEETERlRTEAA-----------E 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1565 ELQHLRQSSEAEIQaKARQVEAAERSRVRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1643
Cdd:NF041483 623 RIRTLQAQAEQEAE-RLRTEAAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEAL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1644 RRQVQDESQRKRQAEAELAlrvKAEAEAAREKQRAlqaledvRLQAEE----AERRLRQAEADRARQVQVALETAQR--- 1716
Cdd:NF041483 702 AAAQEEAARRRREAEETLG---SARAEADQERERA-------REQSEEllasARKRVEEAQAEAQRLVEEADRRATElvs 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1717 SAEVELQSKRASFAEKTAQLERTLQ-----EEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANE------A 1785
Cdd:NF041483 772 AAEQTAQQVRDSVAGLQEQAEEEIAglrsaAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEeteaakA 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1786 LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqQRLVAEQELIRLRAE 1865
Cdd:NF041483 852 LAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQA-DRLIGEATSEAERLT 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1866 TEQGEQQRQLLEEELARLQREAAAATHKRQELEAELA----KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFR 1941
Cdd:NF041483 931 AEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATgeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLR 1010
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1942 ELA-EEAARL--RALAEETKRQRQLAEE---DAARQRAEAERVLAEklaAISEATRLKTEAE------IALKEKEAEner 2009
Cdd:NF041483 1011 TEArEEADRTldEARKDANKRRSEAAEQadtLITEAAAEADQLTAK---AQEEALRTTTEAEaqadtmVGAARKEAE--- 1084
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2010 lrRLAEDEAFQRRRLEEQAaqhKADIEERLAQLRKASENELERQkglveDTLRQRRQVEEEILALKASFEKAAAGKAELE 2089
Cdd:NF041483 1085 --RIVAEATVEGNSLVEKA---RTDADELLVGARRDATAIRERA-----EELRDRITGEIEELHERARRESAEQMKSAGE 1154
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2090 lelgriRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVE-EARRL 2168
Cdd:NF041483 1155 ------RCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEaEAKRT 1228
|
....*..
gi 2044209144 2169 RERAEQE 2175
Cdd:NF041483 1229 VEEGKRE 1235
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
302-407 |
7.68e-20 |
|
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: 87.70 E-value: 7.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 302 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTR 381
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 2044209144 382 LLDPEDV-DVPQPDEKSIITYVSSLYD 407
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1652-2561 |
8.23e-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: 98.59 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1652 QRKRQAEAELalrvkaeaeaaREKQRALQALEDVRlqaEEAERRL----RQAE-ADRARQVQVALETAQRSAEV-ELQSK 1725
Cdd:TIGR02168 172 ERRKETERKL-----------ERTRENLDRLEDIL---NELERQLksleRQAEkAERYKELKAELRELELALLVlRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1726 RASFAEKTAQLERTLQEEHVAVAQLREEAERraqqqaeaerareeaeqeLERWRLKANEalrlrLQAEEVAQQKSLAQAe 1805
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEK------------------LEELRLEVSE-----LEEEIEELQKELYAL- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1806 aekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQlaegtAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQR 1885
Cdd:TIGR02168 294 ------------------------ANEISRLEQQKQIL-----RERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1886 EAAAATHKRQELEAELAKVRAEMevllaskaraeEESRSTSEKSKQRLEAEASRFRELAEEAARLRAlaeetkrQRQLAE 1965
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAEL-----------EELESRLEELEEQLETLRSKVAQLELQIASLNN-------EIERLE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1966 EDAARQRAEAERVLAEKLAAISEATRLKteaeiaLKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 2045
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2046 sENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSnaedtlRSKEQAELEATrqrqlaaeeeq 2125
Cdd:TIGR02168 481 -ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV------DEGYEAAIEAA----------- 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2126 rrreAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAF---AV 2202
Cdd:TIGR02168 543 ----LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkAL 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2203 QQKEQELQQTLQQEQSMLERLRAEAEAA-------RRAAEEAEEARERAEREAAQSRRQveEAERLKQLAEEQAQAQAQA 2275
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdLVRPGGVITGGSAKTNSSILERRR--EIEELEEKIEELEEKIAEL 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2276 QAAAEKLRKEAEQEAARRAQAEQAALKQKQ---VADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEE 2352
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2353 LQRLKAEVTEAARQRNQVEEELFSVRvqmEELSKLKARIEAENRAL--ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVA 2430
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2431 AQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQR 2510
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2511 tLEAERQRQLEMSAEAERLKLRVAEmsRAQARAEEDAQRFRKQAEEIGEKL 2561
Cdd:TIGR02168 934 -LEVRIDNLQERLSEEYSLTLEEAE--ALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1478-2196 |
9.67e-20 |
|
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: 98.22 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1478 IKFIRETLRRMEEE--------ERLAEQQRAEERERLAEVEAALEK----QRQLAEAHAQaKAQAEREAEELQRRMQEEV 1545
Cdd:TIGR02169 193 IDEKRQQLERLRRErekaeryqALLKEKREYEGYELLKEKEALERQkeaiERQLASLEEE-LEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1546 ARREEAA--VDAQQQKRSIQ-----EELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRG----- 1613
Cdd:TIGR02169 272 QLLEELNkkIKDLGEEEQLRvkekiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkr 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1614 ---------GAEGELQALRARAEEAEAQKR--------------QAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAE 1670
Cdd:TIGR02169 352 rdklteeyaELKEELEDLRAELEEVDKEFAetrdelkdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1671 AAREKQRALQA-LEDVRLQAEEAERRLRQAEADR--ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAV 1747
Cdd:TIGR02169 431 GIEAKINELEEeKEDKALEIKKQEWKLEQLAADLskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1748 AQLREEAERRAQQQAEAERAREEAeqelERWRLKANEALRLRLQA-----EEVAQQK---------------SLAQAEAE 1807
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVG----ERYATAIEVAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1808 KQKEEAEREARRRGKA---------EEQAVR---QRELAEQELEKQRQL--------------------------AEGTA 1849
Cdd:TIGR02169 587 RRDLSILSEDGVIGFAvdlvefdpkYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGI 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1850 QQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTS 1926
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1927 EKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKL-AAISEATRLKTEAEIALKEKEA 2005
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEARLREIEQKLNRLTL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2006 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAsENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGK 2085
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2086 AELELELGRIRSNAEDTlrsKEQAELEATRQRQLAAEEEQRRRE-AEERVQKSLAAEEEAARQRKSALEEVErLKAKVEE 2164
Cdd:TIGR02169 906 EELEAQIEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIpEEELSLEDVQAELQRVEEEIRALEPVN-MLAIQEY 981
|
810 820 830
....*....|....*....|....*....|...
gi 2044209144 2165 ARRLRERAEQESARQ-LQLAQEAAQKRLQAEEK 2196
Cdd:TIGR02169 982 EEVLKRLDELKEKRAkLEEERKAILERIEEYEK 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2319-2864 |
1.17e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2319 EQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVtEAARQRNQVEEELFsvrvqmeelsklkariEAENRAL 2398
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGE-------LERQLEPLERQA-EKAERYRELKEELK----------------ELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2399 ILRDKDntqrfLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQ 2478
Cdd:COG1196 231 LLKLRE-----LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---LLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2479 QKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIG 2558
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2559 EKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEmqvvqQEQLLQETRALQES 2638
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA-----LEEAAEEEAELEEE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2639 FLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREqlVASMEEARQRQREAEEGVRRKQEELQ 2718
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG--VKAALLLAGLRGLAGAVAVLIGVEAA 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2719 LLEQQRQQQERLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQAAASKALPnGRDVLDGPAAEAEPEHAFDGLRRKVP 2798
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL-AAALARGAIGAAVDLVASDLREADAR 614
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2799 AQRLQEVGILSAEELQRLAQGRTTVAELAQRE-DVRQYLQGRSGIAGLLLKPANEKLSIYAALRRQL 2864
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1834-2711 |
1.38e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.97 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1834 AEQELEKQRQLAEgtaQQRLVAEQELIRLRAETeqgeqQRQLLE--EELARLQREA-AAATHKRQELEAELAKVRAEMEV 1910
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1911 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRA--LAEETkRQRQLAEEDAARqrAEAERVLaekLAAISE 1988
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1989 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR----LEEQAAQHKADIEERLAQLRKASENELE-------RQKGLV 2057
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRqaaeLSRAAEQRMQEAEEALREARAEAEKVVAeakeaaaKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2058 EDTLRQR-RQVEEEILALKASFEK-AAAGKAELELELG-------RIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRR 2128
Cdd:NF041483 300 ESANEQRtRTAKEEIARLVGEATKeAEALKAEAEQALAdaraeaeKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2129 EAEERVQKSLAAEEEAARQRKSALEEVERLKAKV--------------------------EEARRLRERAEQESARQLql 2182
Cdd:NF041483 380 ASEDAKATTRAAAEEAERIRREAEAEADRLRGEAadqaeqlkgaakddtkeyraktvelqEEARRLRGEAEQLRAEAV-- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2183 aqeAAQKRLQAEekAHAFAVQQKEQELQQTLQQeqsMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAerLK 2262
Cdd:NF041483 458 ---AEGERIRGE--ARREAVQQIEEAARTAEEL---LTKAKADADELRSTATAESERVRTEAIERATTLRRQAEET--LE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2263 QLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQV-ADAEMEKHKKFAEQTLrqkAQVEQELTTLRlqlEE 2341
Cdd:NF041483 528 RTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERL---TAAEEALADAR---AE 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2342 TDHQKSILDEELQRLKAEVTEAARQ-RNQVEEELFSVRVQMEELSKlKARIEAENRALILRD-------------KDNTQ 2407
Cdd:NF041483 602 AERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAADAS-AARAEGENVAVRLRSeaaaeaerlkseaQESAD 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2408 RFLQEEAEKMKQVAEEAAR-LSVAAQEAARLRQLAEEDLAQQRALA-----------EKML----KEKMQAVQEATRLKA 2471
Cdd:NF041483 681 RVRAEAAAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEAdqererareqsEELLasarKRVEEAQAEAQRLVE 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2472 EAELLQQQKELAQEQ-ARQLQEDKEQMAQQLAQETQGFQRTLE--AERQRQlEMSAEAERLKlrvAEMSRAQARAEEDAQ 2548
Cdd:NF041483 761 EADRRATELVSAAEQtAQQVRDSVAGLQEQAEEEIAGLRSAAEhaAERTRT-EAQEEADRVR---SDAYAERERASEDAN 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2549 RFRKQAEEIGEKLHrtELATQEKVTLVHTLEIQRQQSDHDAERLR----AAIAELEREKEKLQEEATllQQKSEEMQVVQ 2624
Cdd:NF041483 837 RLRREAQEETEAAK--ALAERTVSEAIAEAERLRSDASEYAQRVRteasDTLASAEQDAARTRADAR--EDANRIRSDAA 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2625 QEQLLQETRALQESFLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQR 2704
Cdd:NF041483 913 AQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIR 992
|
....*..
gi 2044209144 2705 EAEEGVR 2711
Cdd:NF041483 993 TEAERVK 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2243-2834 |
1.81e-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: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2243 RAEREAAQSRRQVEEAERlkqlaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQTL 2322
Cdd:COG1196 245 EAELEELEAELEELEAEL----------------AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2323 RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELsklkARIEAENRALILRD 2402
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2403 KDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKEL 2482
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2483 AQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEklh 2562
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE--- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2563 rTELATQEKVTLVHTLEIQRQQSDHDAERL--RAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRALQESFL 2640
Cdd:COG1196 542 -AALAAALQNIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2641 SEKDRLLQRERfIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQEELQLL 2720
Cdd:COG1196 621 TLLGRTLVAAR-LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2721 EQQRQQQERLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQAAASKALPNGRDVLDGPAAEAEPEHAFDGLRRKVpaQ 2800
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI--E 777
|
570 580 590
....*....|....*....|....*....|....
gi 2044209144 2801 RLQEVGILSAEELQRLAQGRTTVAElaQREDVRQ 2834
Cdd:COG1196 778 ALGPVNLLAIEEYEELEERYDFLSE--QREDLEE 809
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
309-405 |
2.43e-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: 85.83 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 309 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTN----LENLDQAFSVAERDLGVTRLLD 384
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2044209144 385 PEDVDVPQPDEKSIITYVSSL 405
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1933-2749 |
1.07e-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: 94.74 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1933 LEAEASRFRELAEEAA---RLRALAEETKRQRQLAEEDAAR------------QRAEAERVLAEKLAAISEATRlKTEAE 1997
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1998 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAsenelerqkglvedtlrqRRQVEEEILALKAS 2077
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLE------------------VSELEEEIEELQKE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2078 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQlaaeeeqrrreaeervqKSLAAEEEAARQRK---SALEE 2154
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-----------------KLDELAEELAELEEkleELKEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2155 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsmlerlraeaeaarraa 2234
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI------------------------------------- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2235 eeaeeareraereAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKH 2314
Cdd:TIGR02168 396 -------------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2315 KKFAEQTLRQKaqvEQELTTLRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARI 2391
Cdd:TIGR02168 463 LEELREELEEA---EQALDAAERELAQLQARLDSLerlQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2392 EA---ENRALILRDKDNTQR----FLQE-------------------EAEKMKQVAEEAARLSVAA---QEAARLRQLAE 2442
Cdd:TIGR02168 540 EAalgGRLQAVVVENLNAAKkaiaFLKQnelgrvtflpldsikgteiQGNDREILKNIEGFLGVAKdlvKFDPKLRKALS 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2443 ---------EDLAQQRALAEKMLKEKMQAVQEATRL--------------------KAEAELLQQQKELAQEQARQLQ-- 2491
Cdd:TIGR02168 620 yllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEka 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2492 -EDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2570
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2571 KVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRaLQESFLSEKDRLLQRE 2650
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIESLA 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2651 RFIEQEKAKLEQLfRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQERL 2730
Cdd:TIGR02168 859 AEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
890
....*....|....*....
gi 2044209144 2731 LAEENQRLRERLQRLEEEH 2749
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLEEA 956
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1487-2205 |
2.14e-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: 93.88 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1487 RMEEEERLAEQQRAEERERLAEVEAALEKQRqlaEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEEL 1566
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1567 QHLRQSSEAEIQA-----KARQVEAAERSRVRIEEE---------IRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1632
Cdd:pfam02463 243 QELLRDEQEEIESskqeiEKEEEKLAQVLKENKEEEkekklqeeeLKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1633 KRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALE 1712
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1713 TAQrsaEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQA 1792
Cdd:pfam02463 403 EEK---EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1793 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQG 1869
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1870 EQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-SRFRELAEEAA 1948
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGiLKDTELTKLKE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1949 RLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 2028
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2029 AQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 2108
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2109 AELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQE--- 2185
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEeel 879
|
730 740
....*....|....*....|
gi 2044209144 2186 AAQKRLQAEEKAHAFAVQQK 2205
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEK 899
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1878-2619 |
2.97e-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: 93.58 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1878 EELARLQREAAAATH---KRQELEAELAKVRAEMEVLlaskaraeEESRSTSEKSKQRLEAEAS---RFRELAEE----- 1946
Cdd:TIGR02168 155 EERRAIFEEAAGISKykeRRKETERKLERTRENLDRL--------EDILNELERQLKSLERQAEkaeRYKELKAElrele 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1947 ----AARLRALAEEtKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeafqrr 2022
Cdd:TIGR02168 227 lallVLRLEELREE-LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2023 RLEEQAAQHKadieERLAQLrkasENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDT 2102
Cdd:TIGR02168 299 RLEQQKQILR----ERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2103 LRSKEQAELEATRQRqlaaeeeqrrreaeervqkslAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQL 2182
Cdd:TIGR02168 371 ESRLEELEEQLETLR---------------------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2183 AQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLK 2262
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2263 QLAEEQAQAQAQAQAAAEKLR----------------------------KEAEQEAARRAQAEQAALKQKQVADAEMEKH 2314
Cdd:TIGR02168 510 ALLKNQSGLSGILGVLSELISvdegyeaaieaalggrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLDSIKGTEIQGN 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2315 KKFAEQTLRQKAQVEQELTTLRLQLE------------------------ETDHQKSI---------------------- 2348
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddldnalelakKLRPGYRIvtldgdlvrpggvitggsaktn 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2349 -----LDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEEL----SKLKARIEAENRALILRDKDntqrfLQEEAEKMKQ 2419
Cdd:TIGR02168 670 ssileRRREIEELEEKIEELEEKIAELEKALAELRKELEELeeelEQLRKELEELSRQISALRKD-----LARLEAEVEQ 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2420 VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQE---DKEQ 2496
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaaNLRE 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2497 MAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVH 2576
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 2044209144 2577 TLEIQRQQSDHDAERLRAAIAELEREKEKL-QEEATLLQQKSEE 2619
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEE 948
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
186-291 |
3.04e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 83.01 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 186 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVK 263
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVD 77
|
90 100
....*....|....*....|....*...
gi 2044209144 264 LVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21212 78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
306-405 |
6.31e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 82.21 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERdLGVTRLLDP 385
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 2044209144 386 ED-VDVPQPDEKSIITYVSSL 405
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1390-2164 |
1.10e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 91.39 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1390 EQLQQEKELLEEIERYGEKVD-ECQQLAKQyinaIKDYELQLVTYKAQLepvaspAKKPKvqsgsesviqEYVDLRTRYS 1468
Cdd:pfam01576 194 ERLKKEEKGRQELEKAKRKLEgESTDLQEQ----IAELQAQIAELRAQL------AKKEE----------ELQAALARLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1469 ELTTLTSQYIKFIRET------LRRMEEEERL----AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQ 1538
Cdd:pfam01576 254 EETAQKNNALKKIRELeaqiseLQEDLESERAarnkAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1539 RRMQEEVARREEAAVDAQQQKRSIQEELQ-HLRQSSEAEIQ-AKARQveAAERSRVRIEEEIRVVRLQLEATERQRGGAE 1616
Cdd:pfam01576 334 KALEEETRSHEAQLQEMRQKHTQALEELTeQLEQAKRNKANlEKAKQ--ALESENAELQAELRTLQQAKQDSEHKRKKLE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1617 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRL 1696
Cdd:pfam01576 412 GQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1697 RQAEADRA--RQVQVALETAQRSAEVELQSKRASFAEktaqLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQE 1774
Cdd:pfam01576 492 RQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1775 LERWRlKANEALRLRLQAEEVAQQkslaqaeaekqkeeaerearrrgkaeeqavRQRELAEQELEKQRQLAEGTAQQRLV 1854
Cdd:pfam01576 568 YDKLE-KTKNRLQQELDDLLVDLD------------------------------HQRQLVSNLEKKQKKFDQMLAEEKAI 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1855 AEQELI-RLRAETEQGEQQRQLLEeelarLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAeEESRSTSEKSKQRL 1933
Cdd:pfam01576 617 SARYAEeRDRAEAEAREKETRALS-----LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDV-GKNVHELERSKRAL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1934 EAEASRFRELAEEA---------ARLR------ALAEETKRQRQLAEEDA-------ARQRAEAERVLAEKLAAISEATR 1991
Cdd:pfam01576 691 EQQVEEMKTQLEELedelqatedAKLRlevnmqALKAQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVA 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1992 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE-RLAQ---LRKASENElERQKGLVEDTL------ 2061
Cdd:pfam01576 771 AKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedl 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2062 ----RQRRQVEEEILALKASFEKAAAGKAELELEL----GRIRSNAEDTLRSKEQAELEATRQRQLaaeeeqrrREAEER 2133
Cdd:pfam01576 850 aaseRARRQAQQERDELADEIASGASGKSALQDEKrrleARIAQLEEELEEEQSNTELLNDRLRKS--------TLQVEQ 921
|
810 820 830
....*....|....*....|....*....|....*
gi 2044209144 2134 VQKSLAAEEEAARQRKSALEEVER----LKAKVEE 2164
Cdd:pfam01576 922 LTTELAAERSTSQKSESARQQLERqnkeLKAKLQE 956
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
187-289 |
1.34e-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: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 187 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-K 263
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpE 76
|
90 100
....*....|....*....|....*..
gi 2044209144 264 LVNIRNDDI-ADGNPKLTLGLIWTIIL 289
Cdd:cd00014 77 LDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1483-2052 |
2.26e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 90.36 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1483 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AEELQRRMQEEVARREEAAVDA 1555
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1556 QQQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATE-----------RQRG 1613
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1614 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA---LEDVRLQAE 1690
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFvgeLIEVRPEEE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1691 E----AERRLRQA------EADRARQV-----QVALETAQRSAEVELQSKRA--------SFAEK--------TAQLERT 1739
Cdd:COG4913 475 RwrgaIERVLGGFaltllvPPEHYAAAlrwvnRLHLRGRLVYERVRTGLPDPerprldpdSLAGKldfkphpfRAWLEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1740 LQEE--HVAV---AQLREEA----ERRAQQQAEAERAREEAEQELERWRL-KANEALRLRLQAEEVAQQKSLAQAEAEKQ 1809
Cdd:COG4913 555 LGRRfdYVCVdspEELRRHPraitRAGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1810 KEeaerearrrgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLVAEQELIRLRA---ETEQGEQQRQLLEEELARL 1883
Cdd:COG4913 635 AL----------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1884 QREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTsekskQRLEAEAsRFRELAEEAARlRALAEETKRQRQL 1963
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE-----LRALLEE-RFAAALGDAVE-RELRENLEERIDA 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1964 AEEDAARQRAEAERVLAE-KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRRLEEQAAQHKADIEERLA 2040
Cdd:COG4913 778 LRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLR 856
|
650
....*....|..
gi 2044209144 2041 QLRKASENELER 2052
Cdd:COG4913 857 RAIREIKERIDP 868
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
310-407 |
3.32e-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: 80.31 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 310 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 388
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2044209144 389 DVPQPDEKSIITYVSSLYD 407
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1954-2748 |
9.30e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.49 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1954 AEETKRQRQLAEEDAA------RQRAEAERVLAEKLAAISEATRLKTEAEIA-LKEKEAENERLRRLAEDEAFQRRRLEE 2026
Cdd:pfam02463 147 IAMMKPERRLEIEEEAagsrlkRKKKEALKKLIEETENLAELIIDLEELKLQeLKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2027 QAAQHKADIEERLAQLRKASENELERqkglvEDTLRQRRQVEEEILAL-KASFEKAAAGKAELELELGRIRSNAEDTLRS 2105
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEE-----IESSKQEIEKEEEKLAQvLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2106 KEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2185
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2186 AAQKRL-QAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQL 2264
Cdd:pfam02463 382 ESERLSsAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2265 AEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKK--FAEQTLRQKAQVEQELTTLRLQLEET 2342
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLalIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2343 DHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMkqvae 2422
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD----- 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2423 eaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLA 2502
Cdd:pfam02463 617 ---EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2503 QETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVHTLEIQ 2581
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLkKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2582 RQQSDHDAERLRAAIAELEREKEKLQEEatLLQQKSEEMQVVQqeqllqetrALQESFLSEKDRLLQRERFIEQEKAKLE 2661
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEE--ELRALEEELKEEA---------ELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2662 QLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRER 2741
Cdd:pfam02463 843 KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
....*..
gi 2044209144 2742 LQRLEEE 2748
Cdd:pfam02463 923 IKEEAEI 929
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1345-2081 |
1.15e-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: 88.10 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1345 ELEQLGRQLRYYRESADPLGAWLQDAKQRQERIqavpLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIK 1424
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE----LKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1425 DYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELttltsQYIKFIRETLRRMEEEERLAEQQRAEERE 1504
Cdd:TIGR00618 271 ELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-----QSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1505 RLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEvarrEEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQV 1584
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ----QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1585 EAAERSRVRIEEEirvvrLQLEATERQRGGAEGELQALRARaeEAEAQK-RQAQEEAERLRRQVQDESQRKRQAEAELAL 1663
Cdd:TIGR00618 422 LQGQLAHAKKQQE-----LQQRYAELCAAAITCTAQCEKLE--KIHLQEsAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1664 RVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1743
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ--LETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1744 HVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEvaqqkslaqaeaekqkeeaerearrrgKA 1823
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP---------------------------EQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1824 EEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAK 1903
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1904 VRAEMEVLLAS-KARAEEESRSTSEKSK--QRLEAEA---SRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAER 1977
Cdd:TIGR00618 706 LRELETHIEEYdREFNEIENASSSLGSDlaAREDALNqslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1978 VLAEKLAAISEATRLkteaeiaLKEKEAENERLRRLAEDEafqRRRLEEQAAQHKADIEERLAQLRKaSENELERQKGLV 2057
Cdd:TIGR00618 786 EIQFFNRLREEDTHL-------LKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSA-TLGEITHQLLKY 854
|
730 740
....*....|....*....|....
gi 2044209144 2058 EDTLRQRRQVEEEILALKASFEKA 2081
Cdd:TIGR00618 855 EECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
308-419 |
1.17e-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: 78.88 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 2044209144 388 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 419
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1155-1742 |
1.29e-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: 88.19 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1155 LDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKL-EQVRSLSAIYLEKLK 1233
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeEQLETLRSKVAQLEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1234 TISLvIRSTQgaeEVLRAHEEQLKEAQAVPATlpelEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGE 1313
Cdd:TIGR02168 394 QIAS-LNNEI---ERLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1314 RDVEVERWRERVAPL---LERWQAALAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAKQR---------------QE 1375
Cdd:TIGR02168 466 LREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieaalGG 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1376 RIQAVPLANSQAVREQLQQEKE-------LLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASP----- 1443
Cdd:TIGR02168 546 RLQAVVVENLNAAKKAIAFLKQnelgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggv 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1444 ----------AKKPKVQSGSESVIQEYVDLRTRYS--------ELTTL-TSQYIKFIRETLRRMEEEERLAEQQRAEERE 1504
Cdd:TIGR02168 626 lvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1505 RLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQ---EEVARREEAAVDAQQQKRSIQEELQHLRQsseaeiqaka 1581
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEIEELEERLEEAEE---------- 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1582 rQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAE--- 1658
Cdd:TIGR02168 776 -ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedi 854
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1659 AELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRsaevelqskrasfaektaqLER 1738
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE-------------------LRR 915
|
....
gi 2044209144 1739 TLQE 1742
Cdd:TIGR02168 916 ELEE 919
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
308-411 |
3.05e-16 |
|
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: 77.40 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 2044209144 388 VDV--PQPDEKSIITYVSSLYDAMPR 411
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
311-406 |
5.20e-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: 76.63 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 311 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 389
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 2044209144 390 VPQPDEKSIITYVSSLY 406
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1490-1967 |
7.47e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 84.82 E-value: 7.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1490 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQR-RMQEEVARREEAAVDAQQQKRSIQEELQH 1568
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1569 LRQSsEAEIQAKARQVEAAERSRVRIEEEI-RVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1647
Cdd:COG4717 151 LEER-LEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1648 QDESQRKRQAEAELALRvkaeaeaareKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVeLQSKRA 1727
Cdd:COG4717 230 EQLENELEAAALEERLK----------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL-LAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1728 SFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAE 1807
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1808 KQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLVAEQELIRLRAETEQGEQqrqlLEEELARLQREA 1887
Cdd:COG4717 379 AGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1888 AAATHKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEED 1967
Cdd:COG4717 442 EELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1877-2748 |
8.33e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.41 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1877 EEELARLQREAAAATHKRQELEA--ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-SRFRELAEEAARLRAL 1953
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEAlkKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQlKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1954 AEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 2033
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2034 DIEERlaqlrKASENE---LERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAE 2110
Cdd:pfam02463 312 DEEKL-----KESEKEkkkAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2111 LEATRQRQLaaeeeqrrreaeervQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKR 2190
Cdd:pfam02463 387 SSAAKLKEE---------------ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2191 LQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQ 2270
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2271 AQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVA-------DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEetd 2343
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRaltelplGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL--- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2344 hQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALIL--RDKDNTQRFLQEEAEKMKQVA 2421
Cdd:pfam02463 609 -DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVkaSLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2422 EEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQ 2500
Cdd:pfam02463 688 ELAkEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD--KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2501 LAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAE--EDAQRFRKQAEEIGEKLHRTELATQEKVTLVHTL 2578
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEElkEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2579 EIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRALQEsfLSEKDRLL----QRERFIE 2654
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE--ESQKLNLLeekeNEIEERI 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2655 QEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEE 2734
Cdd:pfam02463 924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
890
....*....|....
gi 2044209144 2735 NQRLRERLQRLEEE 2748
Cdd:pfam02463 1004 KKKLIRAIIEETCQ 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1245-1743 |
1.58e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1245 AEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRvqaeaqqpvfDALRDELRGAQEVGERLQRQHGERDVEVERWRER 1324
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1325 VAPLLERWQAALAQTDVRQRELEQLGRQLRYYRESADPLgawLQDAKQRQERiqavplanSQAVREqlqQEKELLEEIER 1404
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL---REDADDLEER--------AEELRE---EAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1405 YGEKVDECQqlakqyiNAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfIRET 1484
Cdd:PRK02224 375 AREAVEDRR-------EEIEELEEEIEELRERFG--DAPVDLGNAEDFLEELREERDELREREAELEAT-------LRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1485 LRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAK--AQAEREAEELQRR- 1540
Cdd:PRK02224 439 RERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEdlVEAEDRIERLEERr 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1541 --MQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRvvRLQLEATERQRGGAEGE 1618
Cdd:PRK02224 519 edLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESLERIRT 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1619 LQALRARAE---EAEAQKRQAQEEAERLRR-QVQDESQRKRQAEAELAlrvKAEAEAARE-KQRALQALEDV--RLQAEE 1691
Cdd:PRK02224 597 LLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYLEQVeeKLDELR 673
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1692 AERRLRQAEADRARQVQVALEtaqrsaevELQSKRASFAEKTAQLErTLQEE 1743
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELE--------ELRERREALENRVEALE-ALYDE 716
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2949-2987 |
1.75e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.75 E-value: 1.75e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 2949 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 2987
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3608-3646 |
1.75e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.75 E-value: 1.75e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3608 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 3646
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1302-2174 |
1.85e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1302 EVGERLQRQHGERDvEVERWRE--------RVAPLLERWQAALAQTDVRQRELEQLGRQL----RYYRESADPLGAWLQD 1369
Cdd:TIGR02169 195 EKRQQLERLRRERE-KAERYQAllkekreyEGYELLKEKEALERQKEAIERQLASLEEELekltEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1370 AKQRQERIQAVPLANSQAVREQLQqekELLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKV 1449
Cdd:TIGR02169 274 LEELNKKIKDLGEEEQLRVKEKIG---ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1450 QSgsESVIQEYVDLRTRYSELttltsqyikfiretLRRMEEEERLAeqqrAEERERLAEVEAALEKqrqlaeahaqakaq 1529
Cdd:TIGR02169 351 RR--DKLTEEYAELKEELEDL--------------RAELEEVDKEF----AETRDELKDYREKLEK-------------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1530 AEREAEELQR---RMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLE 1606
Cdd:TIGR02169 397 LKREINELKReldRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1607 ATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDESQRKRQAE----AELaLRVKAEAEAARE---KQRAL 1679
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVhgtvAQL-GSVGERYATAIEvaaGNRLN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1680 QALEDVRLQAEEAERRLRQAEADRA--------RQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLR 1751
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRKAGRAtflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1752 EEAerraqqqaeaerareeaeqelerwRLKANeaLRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVR-- 1829
Cdd:TIGR02169 631 AAR------------------------RLMGK--YRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERle 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1830 ----QRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVR 1905
Cdd:TIGR02169 685 glkrELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1906 AEMEVLLASKARAEEEsrstSEKSKQRLeaEASRFRELAEEaarLRALAEETKRQR-QLAEEDAARQRAEAERVLAEKLA 1984
Cdd:TIGR02169 765 ARIEELEEDLHKLEEA----LNDLEARL--SHSRIPEIQAE---LSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKEI 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1985 AISEATRLKTEAEIALKEKEAEN------ERLRRLAEDEAFQrRRLEEQAAQHKADIEERLAQLRKAsENELERQKGLVE 2058
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENlngkkeELEEELEELEAAL-RDLESRLGDLKKERDELEAQLREL-ERKIEELEAQIE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2059 dtlrqrrQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLrSKEQaeLEATRQRQLAAEEEQRRReaeervqkSL 2138
Cdd:TIGR02169 914 -------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL-SLED--VQAELQRVEEEIRALEPV--------NM 975
|
890 900 910
....*....|....*....|....*....|....*.
gi 2044209144 2139 AAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQ 2174
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1266-1691 |
2.05e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 83.28 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1266 LPELEATKAALKKLRVQAEAqqpvFDALRDELRGAQEVGERLQRQHGERDVEVERWR--ERVAPLLERWQAALAQTDVRQ 1343
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1344 RELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQA----VPLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQY 1419
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEElleqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1420 INAIKDYELQLVTYKAQlEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTT--------LTSQYIKFIRETLRRMEEE 1491
Cdd:COG4717 226 EEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlglLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1492 ERLAEQQRAEERERlAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKrsIQEELQHLRQ 1571
Cdd:COG4717 305 EELQALPALEELEE-EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1572 SSEAEIQAKARQVEAaersRVRIEEEIRVVRLQLEA---------TERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1642
Cdd:COG4717 382 EDEEELRAALEQAEE----YQELKEELEELEEQLEEllgeleellEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1643 LRRQVQ-----DESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEE 1691
Cdd:COG4717 458 LEAELEqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4186-4224 |
3.02e-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: 3.02e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 4186 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4224
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
308-407 |
3.05e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 74.62 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 2044209144 388 VDV--PQPDEKSIITYVSSLYD 407
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
762-945 |
3.29e-15 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 77.87 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 762 LHGFVAAATKELMWLSEKEEEEVGFDWGEHNSNMAGKKESYSALMRELEVKEKKIKEIQSTGDRLLREGHPARPTVESFQ 841
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 842 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVRETEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDEKEQLNEY 921
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170 180
....*....|....*....|....
gi 2044209144 922 RAHLSGLAKRARAVVQLKPRDQAQ 945
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADE 182
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1383-2194 |
3.34e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 83.30 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1383 ANSQAVREQLQQEKELLEEI-----ERYGEKVDECQQL---AKQYINAIKDYELQL-----VTYKAQLEPVASPAKKPKV 1449
Cdd:pfam01576 57 AEAEEMRARLAARKQELEEIlheleSRLEEEEERSQQLqneKKKMQQHIQDLEEQLdeeeaARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1450 qsgsESVIQEYVDLRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ 1529
Cdd:pfam01576 137 ----EEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1530 AEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAkARQVEAAERSRVRIEEEIRVVRLQLEATE 1609
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA-LKKIRELEAQISELQEDLESERAARNKAE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1610 RQRGGAEGELQALRARAEE-----AEAQKRQAQEEAE--RLRRQVQDESQRKrqaeaelalrvkaEAEAAREKQRALQAL 1682
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDtldttAAQQELRSKREQEvtELKKALEEETRSH-------------EAQLQEMRQKHTQAL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1683 EDVRLQAEEAERrlRQAEADRARQVqVALETAQRSAEVE-LQSKRASFAEKTAQLERTLQEEHVAVAQlreeaerraqqq 1761
Cdd:pfam01576 359 EELTEQLEQAKR--NKANLEKAKQA-LESENAELQAELRtLQQAKQDSEHKRKKLEGQLQELQARLSE------------ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1762 aeaerareeaeqeLERWRLKANEALRlRLQAEEVAQQKSLaqaeaekqkeeaereARRRGKAEEQAVRQRELAEQELEKQ 1841
Cdd:pfam01576 424 -------------SERQRAELAEKLS-KLQSELESVSSLL---------------NEAEGKNIKLSKDVSSLESQLQDTQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1842 RQLAEGTAQQRLVAEqeliRLRA-ETEQGEQQRQLLEEELAR--LQREAAAATHKRQELEAELAKVRAEMEVLLASKARA 1918
Cdd:pfam01576 475 ELLQEETRQKLNLST----RLRQlEDERNSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1919 EEESRSTSekskQRLEAEASRFRELAEEAARLRA----LAEETKRQRQLAEEDAARQRaEAERVLAEKLAAISEATRLKT 1994
Cdd:pfam01576 551 QRELEALT----QQLEEKAAAYDKLEKTKNRLQQelddLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERD 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1995 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASEN--ELERQKGLVEDTLRQ-RRQVEEei 2071
Cdd:pfam01576 626 RAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNvhELERSKRALEQQVEEmKTQLEE-- 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2072 laLKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEatRQRQLaaeeeqrrreaEERVQKSLAAEEEAARQRKSA 2151
Cdd:pfam01576 704 --LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEE--KRRQL-----------VKQVRELEAELEDERKQRAQA 768
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2152 LE-------EVERLKAKVEEARRLREraeqESARQLQLAQeAAQKRLQAE 2194
Cdd:pfam01576 769 VAakkklelDLKELEAQIDAANKGRE----EAVKQLKKLQ-AQMKDLQRE 813
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1203-1957 |
7.85e-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: 81.94 E-value: 7.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1203 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKtislvirSTQGAEEVLRAHEEQLKE-AQAVPATLPELEATKAALKKLRV 1281
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKK-------SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1282 QAEAQQPVFDALRDELRGAQEVGERLQRQHGERDVEverwrervaplLERWQAALAQTDVRQRELEQLGRQLRYYRESAd 1361
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLAAHIK- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1362 plgAWLQDAKQRQERIQAvpLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVA 1441
Cdd:TIGR00618 301 ---AVTQIEQQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1442 SPAKKPKVQSGSESVIQEyvDLRTRYSELTTLTSQYIKFIRETLRRMEEEERL--AEQQRAEERERLAEVEAALEKQRQ- 1518
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQc 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1519 --LAEAHAQAKAQAEREAEE-------LQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA--EIQAKARQVEAA 1587
Cdd:TIGR00618 454 ekLEKIHLQESAQSLKEREQqlqtkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRMQRG 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1588 ERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1667
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1668 EAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAV 1747
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL---QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1748 AQLreeAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQA 1827
Cdd:TIGR00618 690 EQL---TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1828 VRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQR----QLLEEELARLQREAAAATHKRQELEAELAK 1903
Cdd:TIGR00618 767 NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdeDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1904 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEET 1957
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEI 900
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1518-1888 |
8.97e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 81.71 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1518 QLAEAHAQAKAQAEREAEELQRRMQEEVARreeaavdaqQQKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1590
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1591 RVRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEAELALRVK-AEA 1669
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1670 EAAREKQRALQALEDVRLQAEEA-ERRLRQAEADRARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvava 1748
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1749 qlreeaerraqqqaEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQav 1828
Cdd:pfam17380 470 --------------EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-- 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1829 rQRELAEQELEKQRQLAE--GTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1888
Cdd:pfam17380 534 -RRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
308-409 |
1.09e-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: 73.20 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 2044209144 388 -VDVPQPDEKSIITYVSSLYDAM 409
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1158-1732 |
2.33e-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: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1158 EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1237
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1238 VIRSTQGAEEvlraheEQLKEaqavpatlpELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDVE 1317
Cdd:COG4913 331 QIRGNGGDRL------EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1318 VERWRERVAPLLERWQAALAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDAkqRQERIQAVPLANSQA--------VR 1389
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDL---RRELRELEAEIASLERRKSNIPARLLAL--RDALAEALGLDEAELpfvgelieVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1390 EqlqQEKELLEEIERY--GEKV-----DECQQLAKQYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqeyvd 1462
Cdd:COG4913 471 P---EEERWRGAIERVlgGFALtllvpPEHYAAALRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG-------- 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1463 lrtrysELTTLTSQYIKFIRETLRRM------EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAK 1527
Cdd:COG4913 539 ------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1528 AQAEREAEELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEIqakarQVEAAERSRVRIEEEIRvvrlQLEA 1607
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELE----RLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1608 terqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALE-DVR 1686
Cdd:COG4913 683 -------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELRALlEER 754
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2044209144 1687 LQAEEAERRLRQAEADRARQVQvALETAQRSAEVELQSKRASFAEK 1732
Cdd:COG4913 755 FAAALGDAVERELRENLEERID-ALRARLNRAEEELERAMRAFNRE 799
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
306-406 |
2.33e-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: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAErDLGVTRLLDP 385
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 2044209144 386 ED-VDVPQPDEKSIITYVSSLY 406
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1471-2196 |
2.63e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.40 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1471 TTLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREE 1550
Cdd:TIGR00618 134 DLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1551 AAVDAQQQKRSIQEELQHLR--QSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQrggaEGELQALRARAEE 1628
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ----EAVLEETQERINR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1629 AEAQKRQA--QEEAERLRRQVQDESQRKRQAEAELA-LRVKAEAEAAREKQRALQALEDVRLQAEEAERRlRQAEADRAR 1705
Cdd:TIGR00618 289 ARKAAPLAahIKAVTQIEQQAQRIHTELQSKMRSRAkLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR-DAHEVATSI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1706 QVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKanea 1785
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC---- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1786 lrlRLQAEEVAQQKSLAQAEAEKQKEEAerearrrgKAEEQAVRQRE-LAEQELEKQ----RQLAEGTAQQRLVAEQELI 1860
Cdd:TIGR00618 444 ---AAAITCTAQCEKLEKIHLQESAQSL--------KEREQQLQTKEqIHLQETRKKavvlARLLELQEEPCPLCGSCIH 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1861 RLRAET------------EQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEmEVLLASKARAEEESRSTSEK 1928
Cdd:TIGR00618 513 PNPARQdidnpgpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1929 SKQRLEaeasrfRELAEEAARLRALAEETKRQ-RQLAEEDAARQRAEAERVLAEKLAaiSEATRLKTEAEIALKEKEAEN 2007
Cdd:TIGR00618 592 ITVRLQ------DLTEKLSEAEDMLACEQHALlRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREH 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2008 ERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAE 2087
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSE---KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2088 LELELGRIRSNAEDTLrsKEQAELEATRQRQLAAEEEQRrreaeervQKSLAAEEEAARQRKSALEEVERLKAKVEEARR 2167
Cdd:TIGR00618 741 LNQSLKELMHQARTVL--KARTEAHFNNNEEVTAALQTG--------AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
730 740 750
....*....|....*....|....*....|
gi 2044209144 2168 LRERAEQE-SARQLQLAQEAAQKRLQAEEK 2196
Cdd:TIGR00618 811 EIPSDEDIlNLQCETLVQEEEQFLSRLEEK 840
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
183-287 |
5.47e-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: 71.02 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 183 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRH 259
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEE 77
|
90 100
....*....|....*....|....*....
gi 2044209144 260 R-QVKLVNIRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21225 78 DlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1108-1742 |
5.61e-14 |
|
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: 79.33 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1108 HYQQLLQSAEQGAQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkepaRECAQRIAEQQK----AQAEVEGLGK 1182
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1183 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLRAHEEQLKE--- 1258
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqle 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1259 --AQAVPATLPELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGER-----LQRQHGERDVEVERWRERVAPLLER 1331
Cdd:TIGR02168 383 tlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1332 WQAALAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQAVPLANSQ------AVREQLQQEKELLEEIERY 1405
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgVLSELISVDEGYEAAIEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1406 GEK-----VDECQQLAKQYINAIKDYELQLVTYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTLT 1474
Cdd:TIGR02168 543 LGGrlqavVVENLNAAKKAIAFLKQNELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1475 SQYikFIRETLrrmEEEERLAEQQRAEER-----ERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARRE 1549
Cdd:TIGR02168 623 GGV--LVVDDL---DNALELAKKLRPGYRivtldGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1550 EAAVDAQQQKRSIQEELQHLR---QSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1626
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1627 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARq 1706
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES- 856
|
650 660 670
....*....|....*....|....*....|....*.
gi 2044209144 1707 VQVALETAQRSAEvELQSKRASFAEKTAQLERTLQE 1742
Cdd:TIGR02168 857 LAAEIEELEELIE-ELESELEALLNERASLEEALAL 891
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
186-291 |
6.26e-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: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 186 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRH 259
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMAS 73
|
90 100 110
....*....|....*....|....*....|..
gi 2044209144 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 |
7.00e-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: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 179 TDERDrvqKKTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQ 248
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVE 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2044209144 249 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 290
Cdd:cd21219 66 NCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1062-1696 |
1.27e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1062 KPEEQRQAL---RSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSR-----HYQQLLQSAEQGAQ-EESRCQRCISE 1132
Cdd:PTZ00121 1177 KAEAARKAEevrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKaEEERNNEEIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1133 LKDIRLQ--------LEACETRTVHRLRLPLDKEPARECAQ----RIAEQQKAQAE----VEGLGKGV--ARLSAEAEKV 1194
Cdd:PTZ00121 1257 FEEARMAhfarrqaaIKAEEARKADELKKAEEKKKADEAKKaeekKKADEAKKKAEeakkADEAKKKAeeAKKKADAAKK 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1195 LAlPEPSPAAPTLRSELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEEVLRAHEEQLKEAQAVPATLPELEATKA 1274
Cdd:PTZ00121 1337 KA-EEAKKAAEAAKAEAEAAADEAEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1275 ALKKlrvqAEAQQPVFDALR---DELRGAQEVGERLQRQHGERDVEVERWRERVAPLLERWQAALAQTDVRQRELEQlgr 1351
Cdd:PTZ00121 1409 ELKK----AAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1352 qlryyRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEIERYGE--KVDEcqqlAKQYINAIKDYELQ 1429
Cdd:PTZ00121 1482 -----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELK 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1430 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLR----TRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRAEERER 1505
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1506 laeveaalEKQRQLAEAHAQAKaqaeREAEELQRRMQEEVARREEAAVDAQQQKRSIQEelqhLRQSSEAEiqakarqvE 1585
Cdd:PTZ00121 1633 --------KKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDE--------K 1688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1586 AAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElalrv 1665
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK----- 1763
|
650 660 670
....*....|....*....|....*....|.
gi 2044209144 1666 KAEAEAAREKQRALQALEDVRLQAEEAERRL 1696
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3867-3905 |
1.32e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.32e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3867 LLEAQAATGFLLEPVKGERLTVDEAVRKGLVGPELHDRL 3905
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2137-2831 |
1.39e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2137 SLAAEEEAARQRKSALEEVERLKAKVEEARRlRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQkeqelqqtlqqe 2216
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK------------ 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2217 qsMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2296
Cdd:PTZ00121 1142 --AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2297 EQAALKQKQVADAEmEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFS 2376
Cdd:PTZ00121 1220 AEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2377 VRVQMEELSKLKAriEAENRALILRDKDNTQRflqEEAEKMKQVAEEAARLSVAAQEAARLRQlAEEDLAQQRALAEKML 2456
Cdd:PTZ00121 1299 EEKKKADEAKKKA--EEAKKADEAKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAA-DEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2457 KEKMQAVQEATRLKAEaellqqQKELAQEQARQLQEDKEQmAQQLAQETQGFQRTLEAerQRQLEMSAEAERLKLRVAEM 2536
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAE------EKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEA--KKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2537 SRA---QARAEEdaqrfRKQAEEIGEKLHRTELATQEKvtlvhtleiQRQQSDHDAERLRAAIAELEREKEKLQEEATLl 2613
Cdd:PTZ00121 1444 KKAdeaKKKAEE-----AKKAEEAKKKAEEAKKADEAK---------KKAEEAKKADEAKKKAEEAKKKADEAKKAAEA- 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2614 QQKSEEMQVVQQEQLLQETRALQESFLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKLReeQQRQQQQMEQEREQLV 2693
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK--KAEEDKNMALRKAEEA 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2694 ASMEEAR-----------------QRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHRAALAH- 2755
Cdd:PTZ00121 1587 KKAEEARieevmklyeeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEe 1666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2756 ---SEEIAASQAAASKALPNGRDVLDGPAAEAEPEHAFDGLRRKVPAQ--------RLQEVGILSAEELQRLAQGRTTVA 2824
Cdd:PTZ00121 1667 akkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkkaeelkKAEEENKIKAEEAKKEAEEDKKKA 1746
|
....*..
gi 2044209144 2825 ELAQRED 2831
Cdd:PTZ00121 1747 EEAKKDE 1753
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
306-403 |
1.60e-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: 69.33 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHRPMLI-DMSKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 2044209144 385 PEDVDVPQPDEKSIITYVS 403
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1110-2019 |
1.67e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.80 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1110 QQLLQSAEQGAQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1189
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1190 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEEVLRAHEEQLKEAQ 1260
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1261 AVPATL-PELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDVEVERWRERvapllerwqaalaqT 1339
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--------------L 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1340 DVRQRELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQAvplansqAVREQLQQEKELLEEIERYGEKVDECQQLAKQY 1419
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1420 INAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTlTSQYIKFIRETLRRMEE--EERLAEQ 1497
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYD---------RVEKELSKLQRELAEAEAQARASEE-RVRGGRAVEEVLKASIQgvHGTVAQL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1498 QRAEERERLA-EVEAALEKQRQLAEAHAQAKaqaerEAEELQRRMQEEVA--------RREEAAVDAQQQKRSIQEELQH 1568
Cdd:TIGR02169 531 GSVGERYATAiEVAAGNRLNNVVVEDDAVAK-----EAIELLKRRKAGRAtflplnkmRDERRDLSILSEDGVIGFAVDL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1569 LRqsSEAEIQAKARQV-------EAAERSRvRIEEEIRVVRLQLEATERQ---RGGA-EGELQALRARAEEAEAQKRQAQ 1637
Cdd:TIGR02169 606 VE--FDPKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGILFSRSEPAELQRLRER 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1638 EEA-ERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEdvrlQAEEAERRLRQAEADRARQVQVALEtaqr 1716
Cdd:TIGR02169 683 LEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE----QEEEKLKERLEELEEDLSSLEQEIE---- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1717 saevELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERraqqqaeaerareeaeqelERWRLKANEalrLRLQAEEVA 1796
Cdd:TIGR02169 755 ----NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------SRIPEIQAE---LSKLEEEVS 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1797 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVaEQELIRLRAETEQGEQQRQLL 1876
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDL 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1877 EEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE--AEASRFRELAEE----AARL 1950
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAElqrvEEEI 967
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1951 RALAEETKRQRQLAEEDAARQRAeaervLAEKLAaiseatRLKTEAEiALKEKEAENERLRRLAEDEAF 2019
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILERIEEYEKKKREVFMEAF 1024
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
306-406 |
1.96e-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: 69.67 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAErDLGVTRLLDP 385
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 2044209144 386 ED-VDVPQPDEKSIITYVSSLY 406
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3201-3239 |
2.99e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.58 E-value: 2.99e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3201 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPELHEKL 3239
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1549-2171 |
3.54e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1549 EEAAVDAQQQKRSIQEELQHLRQ--SSEAEIQakaRQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1626
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKfiKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1627 EEAEaqkrQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEaDRARQ 1706
Cdd:PRK03918 238 EEIE----ELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL-DELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1707 VQVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeaeRAREEAEQELERWRLKANEAL 1786
Cdd:PRK03918 312 IEKRLSRLEEEIN-GIEERIKELEEKEERLEELKKKL----------------------KELEKRLEELEERHELYEEAK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1787 RLRLQAEEVAQQKSlaqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQlaegtaqqrlvAEQELIRLRAET 1866
Cdd:PRK03918 369 AKKEELERLKKRLT--------------------GLTPEKLEKELEELEKAKEEIEE-----------EISKITARIGEL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1867 EQGEQQRQLLEEELARLQRE-----AAAATHKRQELeaeLAKVRAEMEVLLASKARAEEESRSTsEKSKQRLE---AEAS 1938
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKL-RKELRELEkvlKKES 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1939 RFRELAEEAARLRALAEETKrqrQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIA---LKEKEAENERLRRLAE 2015
Cdd:PRK03918 494 ELIKLKELAEQLKELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2016 DEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SENELERQKGLVEDTLRQRRQVEEEILALKASFEKAaagKA 2086
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL---RK 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2087 ELElELGRIRSnaEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEAR 2166
Cdd:PRK03918 648 ELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
....*
gi 2044209144 2167 RLRER 2171
Cdd:PRK03918 725 ELREK 729
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
205-288 |
5.85e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 205 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGN 276
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGH 100
|
90
....*....|..
gi 2044209144 277 PKLTLGLIWTII 288
Cdd:cd21223 101 REKTLALLWRII 112
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1837-2599 |
6.38e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.78 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1837 ELEKQRQLAEGTAQQRLVAEQELIRLRAE----TEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVL- 1911
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQe 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1912 -------LASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALaEETKRQRQLAEEDAARQRAEAERVLAEKLA 1984
Cdd:TIGR00618 254 eqlkkqqLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV-TQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1985 AISEATRLKtEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqhkadIEERLAQLRKASENELERQKGLVEDTLRQR 2064
Cdd:TIGR00618 333 HVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-----LTQHIHTLQQQKTTLTQKLQSLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2065 R---QVEEEILALKASFEKAAAGKAELELELGRI---RSNAEDTLRSKEQAELEATRQRQlaaeeeqrrreaeervqkSL 2138
Cdd:TIGR00618 407 ReqaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAelcAAAITCTAQCEKLEKIHLQESAQ------------------SL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2139 AAEEEAARQRKSALEEVERLKAkvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQS 2218
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKA--VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2219 MLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRkeaeqeaarraqaeq 2298
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA--------------- 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2299 aALKQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETdhqksildeelqRLKAEVTEAARQRNQVEEELFSVR 2378
Cdd:TIGR00618 612 -CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT------------LTQERVREHALSIRVLPKELLASR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2379 VQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2458
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2459 KMQAVQEAT-RLKAEAELLQQQKELAQE---QARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVA 2534
Cdd:TIGR00618 759 RTEAHFNNNeEVTAALQTGAELSHLAAEiqfFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2535 EMSRAQAraeedaqRFRKQAEEIGEKLHRTELATQEK---VTLVHTLEIQRQ-QSDHDAERLRAAIAEL 2599
Cdd:TIGR00618 839 EKSATLG-------EITHQLLKYEECSKQLAQLTQEQakiIQLSDKLNGINQiKIQFDGDALIKFLHEI 900
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1822-2038 |
8.22e-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: 73.64 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEASRFRELAEE-AARLRALAEETKRQRQLAEEdAARQRAEAER 1977
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 1978 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2038
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
308-408 |
9.89e-13 |
|
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: 67.38 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 387
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 2044209144 388 VdVPQPDEKSIITYVSSLYDA 408
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1857-2619 |
1.02e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1857 QELIRLRAETEQGEQQRQLLEE-----------ELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRST 1925
Cdd:TIGR02169 198 QQLERLRREREKAERYQALLKEkreyegyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1926 SEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLaaiSEATRLKTEAEIALKEKEA 2005
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL---AEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2006 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE------NELERQKGLVEDTLRQRRqveEEILALKASFE 2079
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEklkreiNELKRELDRLQEELQRLS---EELADLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2080 KAAAGKAELELEL-----------GRIRSNAEDtlRSKEQAELEATRQRQlaaeeeqrrrEAEERVQKSLAAEEEAARQR 2148
Cdd:TIGR02169 431 GIEAKINELEEEKedkaleikkqeWKLEQLAAD--LSKYEQELYDLKEEY----------DRVEKELSKLQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2149 KSALEEVERLKAKVEEARRLRERAEQESARQL-------QLAQE-AAQKRLQA------EEKAHAFAVQQKEQELQQTLQ 2214
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryATAIEvAAGNRLNNvvveddAVAKEAIELLKRRKAGRATFL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2215 QEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQV----------EEAERLK---QLAEEQAQAQAQAQAAAEK 2281
Cdd:TIGR02169 579 PLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVfgdtlvvediEAARRLMgkyRMVTLEGELFEKSGAMTGG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2282 LRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQTLRQKA--QVEQELTTLRLQLEETDHQKSILDEELQRLKAE 2359
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2360 VTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRAL-----ILRDKDNTQRFlQEEAEKMKQVAEEAARLSVAAQEA 2434
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRI-PEIQAELSKLEEEVSRIEARLREI 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2435 ARlrqlAEEDLAQQRALAEKMLKEkmqavqeatrLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAqETQGFQRTLEA 2514
Cdd:TIGR02169 818 EQ----KLNRLTLEKEYLEKEIQE----------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-ELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2515 ERQrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLH----------RTELATQEKVTLVHTLEIQRQQ 2584
Cdd:TIGR02169 883 RLG---DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleeelseieDPKGEDEEIPEEELSLEDVQAE 959
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2585 SDHDAERLRA-------AIAELERE----------KEKLQEEATLLQQKSEE 2619
Cdd:TIGR02169 960 LQRVEEEIRAlepvnmlAIQEYEEVlkrldelkekRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1557-2500 |
1.08e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1557 QQKRSIQEELQHLRQSsEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA----- 1631
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1632 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR------EKQRALQALEDVRLQAEEAE-----RRLRQAE 1700
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1701 ADRARQVQVALETaqrsaEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQaeaerareeaeqelerwrl 1780
Cdd:TIGR02169 311 AEKERELEDAEER-----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1781 kanEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLVAEQEL 1859
Cdd:TIGR02169 367 ---EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1860 IRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAE 1936
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1937 ASRFRELAEeaarlralaeeTKRQRQLAEEDAARQRAEAERVLAEKLAAiseatrlktEAEIALKEKEAENER---LRRL 2013
Cdd:TIGR02169 524 HGTVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKM 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2014 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELeRQKGLVEDTLRQRRQVEEEILALKAS--FEKAAAgkaeleLE 2091
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGA------MT 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2092 LGRIRSNAEDTLRSKEQAELEATRQRqlaaeeeqrrreaeervqkslaaEEEAARQRKSALEEVERLKAKVEEARRLRER 2171
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2172 AEQE----SARQLQLAQEAAQKRLQAEEkahafaVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAERE 2247
Cdd:TIGR02169 714 ASRKigeiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2248 AAQSRRQVEEAERLKQlaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQTLRQKAQ 2327
Cdd:TIGR02169 788 LSHSRIPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2328 VEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQ 2407
Cdd:TIGR02169 852 IEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2408 RfLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2487
Cdd:TIGR02169 925 K-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
970
....*....|...
gi 2044209144 2488 RQLQEDKEQMAQQ 2500
Cdd:TIGR02169 1003 KAILERIEEYEKK 1015
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
308-407 |
1.62e-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: 66.59 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 308 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTN---LENLDQAFSVAER-DLGVTRLL 383
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 2044209144 384 DPEDVdVPQPDEKSIITYVSSLYD 407
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2873-2911 |
1.73e-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: 1.73e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 2873 LLEAQAATGFLLDPVQNRRLTVNEAVKEGVVGPELHHKL 2911
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1531-2052 |
1.88e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1531 EREAEELQRRMQEEVA---RREEAAVDAQQQKRSiqeeLQHLRQSSEaEIQAKARQVEAAERSRVRIEEEIRVVRLQLEA 1607
Cdd:COG4913 220 EPDTFEAADALVEHFDdleRAHEALEDAREQIEL----LEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1608 TERQRggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAELALRVKAEAEAAREKQRALQALEDVR 1686
Cdd:COG4913 295 AELEE--LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1687 LQAEEAERRLrQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTlqeehvavaqlreeaerraqqqaeaer 1766
Cdd:COG4913 373 LPLPASAEEF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--------------------------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1767 areeaEQEL---------------------------------------------ERWRLKANEAL--------------- 1786
Cdd:COG4913 425 -----EAEIaslerrksniparllalrdalaealgldeaelpfvgelievrpeeERWRGAIERVLggfaltllvppehya 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1787 -----------RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAvrQRELA----------EQELEKQRQ-- 1843
Cdd:COG4913 500 aalrwvnrlhlRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWL--EAELGrrfdyvcvdsPEELRRHPRai 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1844 LAEGTAQQRLVAEQELIRLRAETE-----QGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARA 1918
Cdd:COG4913 578 TRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1919 EEESRSTS--------EKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAAR---QRAEAERVLAEKLAAIS 1987
Cdd:COG4913 658 WDEIDVASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLE 737
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 1988 EATRLKTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKASENELER 2052
Cdd:COG4913 738 AAEDLARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3532-3570 |
1.89e-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: 1.89e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3532 LLEAQAATGFLIDPVRNQRLYVHEAVKAGVVGPELHEKL 3570
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1485-1686 |
2.66e-12 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 72.60 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1485 LRRMEEEERLAEQQRAEeRERLAEVEAAlEKQRQLAEAHAQAKAQ------AEREAE-ELQRRMQEEVARREEAAVDAQQ 1557
Cdd:COG2268 191 RRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREietariAEAEAElAKKKAEERREAETARAEAEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1558 QKRSIQEELQHLRQsseAEIQAKARQVEAAERSRVRIEEEirvvrlqLEATERQRGGAEGELQALRARAeEAEAQKRQAQ 1637
Cdd:COG2268 269 EIAEANAEREVQRQ---LEIAEREREIELQEKEAEREEAE-------LEADVRKPAEAEKQAAEAEAEA-EAEAIRAKGL 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2044209144 1638 EEAERLRRQVqdESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVR 1686
Cdd:COG2268 338 AEAEGKRALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4455-4493 |
3.40e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.40e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 4455 LLEAQACTGGIIDPSSGERFPVTDAVSRGLVDKIMVDRI 4493
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3943-3981 |
4.74e-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: 4.74e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3943 LLDAQLATGGIVDPHLGFHLPLEVAYQRGYLNKDTHDQL 3981
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1570-2196 |
5.58e-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: 72.95 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1570 RQSSEAEIQAKARQVEA--AERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1643
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1644 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVeLQ 1723
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1724 SKRASFAEKTAQLERTLQEEHVA-VAQLREEAERRAQQQAEAERAREEAEQELER-WRLKANEALR-LRLQAEEVAQQKS 1800
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESeLREQLEAGKLeFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1801 LAQAEAEKQKEEAEREARRRGKAEEqAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEEL 1880
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1881 ARLQREAAAATH----KRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEE 1956
Cdd:pfam12128 527 LQLFPQAGTLLHflrkEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1957 TKRQRQLAEEDAARQR---AEAERVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQHKA 2033
Cdd:pfam12128 602 LRERLDKAEEALQSARekqAAAEEQLVQANGELEKASREETFARTALKNAR---LDLRRLFDEKQSEKDKKNKALAERKD 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2034 DIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEkaaagkAELELELGRIRSN--AEDTLRSKEQAEL 2111
Cdd:pfam12128 679 SANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSGAKAELKAL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2112 EATRQRQLAAEEEQRRREAEERVQ-KSLAAEEEAARQRKSA------------LEEVERLKAKVEEARRLRERAEQESAR 2178
Cdd:pfam12128 753 ETWYKRDLASLGVDPDVIAKLKREiRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAISELQQQLAR 832
|
650
....*....|....*...
gi 2044209144 2179 QlqlaQEAAQKRLQAEEK 2196
Cdd:pfam12128 833 L----IADTKLRRAKLEM 846
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4110-4148 |
8.27e-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: 8.27e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 4110 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4148
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
666-855 |
8.75e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 67.86 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 666 LRYLQDLLAWVEENQRRVDSAEWGGDLPSVEAQLGSHRGLHQSIDEFRAKIERARADEGQL---SPAPRGTYRDCLGRLD 742
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 743 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLSEKEEEEVGFDWGEHNSNMAGKKESYSALMRELEVKEKKIKEI 819
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2044209144 820 QSTGDRLLREGHP-ARPTVESFQAALQTQWSWMLQLC 855
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1064-1719 |
1.24e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1064 EEQRQALRSLELHYQAFLRDSQDAggfgpeDRLQAEREYgscsrhyQQLLQSAEQGAQEESRCQRCISELKDIRLQLEAC 1143
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERL------AELEYLRAA-------LRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1144 ETRtvhrlrlpldkeparecaQRIAEQQKAQAEVEGLGKGVARLSAeaekvlalpepspaaptLRSELELTLGKLEQVRS 1223
Cdd:COG4913 315 EAR------------------LDALREELDELEAQIRGNGGDRLEQ-----------------LEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1224 LSAIYLEKLKTISLVIRSTqgaeevlrahEEQLKEAQA-VPATLPELEATKAALKKLRVQAEAQqpvFDALRDELRGAQE 1302
Cdd:COG4913 360 RRARLEALLAALGLPLPAS----------AEEFAALRAeAAALLEALEEELEALEEALAEAEAA---LRDLRRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1303 VGERLQRQHGERDVEVERWRER--------------------VAPLLERWQAALaqtdvrQRELEQLGRQL----RYYRE 1358
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDAlaealgldeaelpfvgelieVRPEEERWRGAI------ERVLGGFALTLlvppEHYAA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1359 SAdplgAWLQDAKQRQE-RIQAVPLANSQAVREQLqQEKELLEEIERygeKVDECQQLAKQYINAIKDYELqlvtykaql 1437
Cdd:COG4913 501 AL----RWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLDF---KPHPFRAWLEAELGRRFDYVC--------- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1438 epVASPAkkpkvqsgsesviqeyvDLRtRYSELTTLTSQyIKFIReTLRRMEEEERL---------AEQQRAEERERLAE 1508
Cdd:COG4913 564 --VDSPE-----------------ELR-RHPRAITRAGQ-VKGNG-TRHEKDDRRRIrsryvlgfdNRAKLAALEAELAE 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1509 VEAALEKQRQLAEAHAQAKAQAEREAEELQRRmqEEVARREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKARQVEAAE 1588
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELE 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1589 RSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE------------------AQKRQAQEEAERLRRQVQDE 1650
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaaLGDAVERELRENLEERIDAL 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1651 SQRKRQAEAELALRVK--------------AEAEAAREKQRALQALEDVRL---QAEEAERRLRQAEADRArQVQVALET 1713
Cdd:COG4913 779 RARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEDGLpeyEERFKELLNENSIEFVA-DLLSKLRR 857
|
....*.
gi 2044209144 1714 AQRSAE 1719
Cdd:COG4913 858 AIREIK 863
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
308-403 |
1.28e-11 |
|
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: 63.94 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 308 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHRPMLI-DMSKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 386
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 2044209144 387 DVDVPQPDEKSIITYVS 403
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3277-3315 |
1.43e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.43e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3277 LLDAQLSTGGIVDPSKSHRVPMDVAYARGYLDQETSRAL 3315
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2319-2666 |
1.43e-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: 70.92 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2319 EQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQRLKAEVTEAARQRNQVEEELFSV--RVQMEELSKLKaRIEAENR 2396
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKAR-QAEMDRQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2397 ALILRDKDNTQRFLQEEAEKMKQvaEEAARlsvaaqEAARLRQlaeEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2476
Cdd:pfam17380 333 AAIYAEQERMAMERERELERIRQ--EERKR------ELERIRQ---EEIAMEISRMRELERLQMERQQKNERVRQELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2477 QQQKELAQEQARQLQEDKEQMAQQLAQETQGFQ---RTLEAERQRQLEmsaeaerlKLRVAEMSRAQaraeeDAQRFRKQ 2553
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrevRRLEEERAREME--------RVRLEEQERQQ-----QVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2554 AEEigEKLHRTELATQekvtlvhtleiQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETR 2633
Cdd:pfam17380 469 EEE--RKRKKLELEKE-----------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR 535
|
330 340 350
....*....|....*....|....*....|....*....
gi 2044209144 2634 ALQES------FLSEKDRLLQRERFIEQEKAKLEQLFRD 2666
Cdd:pfam17380 536 REAEEerrkqqEMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2302-2837 |
1.91e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2302 KQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIldEELQRLKaEVTEAARQRNQVEEELFSVRVQM 2381
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA--EEARKAE-DARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2382 EELSKLK--------ARIEAENRALILRDKDNTQRflQEEAEKMkqvaeEAARLSVAAQEAARLRQLAEEDLAQQRALAE 2453
Cdd:PTZ00121 1161 EDARKAEearkaedaKKAEAARKAEEVRKAEELRK--AEDARKA-----EAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2454 KMLKEKMQAvQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQlAQETQGFQRTLEAERQRQLEMSAEAERLKlRV 2533
Cdd:PTZ00121 1234 EAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK-ADELKKAEEKKKADEAKKAEEKKKADEAK-KK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2534 AEMSRAQARAEEDAQRFRKQAEEIG----EKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQE- 2608
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKkkaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEk 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2609 -EATLLQQKSEEmqvVQQEQLLQETRALQESFLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKA---QKLREEQQRQQQQ 2684
Cdd:PTZ00121 1391 kKADEAKKKAEE---DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEAKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2685 MEQEREQLVASMEEAR---QRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRErLQRLEEEHRA-ALAHSEEIA 2760
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKkadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE-AKKAEEAKKAdEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2761 ASQA-AASKALPNGRDVLDGPAAEAEPEHAFDGLRR-----KVPAQRLQEVGIL-------SAEELQRLAQGRTTVAELA 2827
Cdd:PTZ00121 1547 KADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLyeeekkmKAEEAKKAEEAKIKAEELK 1626
|
570
....*....|
gi 2044209144 2828 QREDVRQYLQ 2837
Cdd:PTZ00121 1627 KAEEEKKKVE 1636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1825-2029 |
2.06e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKV 1904
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1905 ---------RAEMEVLLASKARAEEESRSTSEKS-KQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAE 1974
Cdd:COG4942 110 lralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 1975 AERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 2029
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
188-294 |
2.79e-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: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 188 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHR 260
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1298-2026 |
4.14e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.87 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1298 RGAQEVGERLQRQHGE---RDVEVERWRERVAPLLERWQAALAQTDVRQRELEQLGRQLRyyresadplGAWLQDAKqRQ 1374
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEhwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYK---------SDETLIAS-RQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1375 ERIQAVPLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQ-----LVTYKAQLEpvaspaKKPKV 1449
Cdd:pfam12128 279 EERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfldadIETAAADQE------QLPSW 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1450 QSGSESVIQEYVDLRTRYSELTTLTSQYIKFIRETLRRMEE--EERLAEQQRAEERERlAEVEAALEKQ-RQLAEAHAQA 1526
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAgiKDKLAKIREARDRQL-AVAEDDLQALeSELREQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1527 KAQAEREAEELQRRMQEEVARREEAAVDaqqqkrsiQEELQHLRQSSEAEIQAKARQvEAAERSRVRIEEEIRVVRLQLE 1606
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLRLNQATAT--------PELLLQLENFDERIERAREEQ-EAANAEVERLQSELRQARKRRD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1607 ATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDESQR-KRQAEAELALRVKAEAEAAREKQRALQALED 1684
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLRKEAPDWEQSiGKVISPELLHRTDLDPEVWDGSVGGELNLYG 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1685 VRLQ------------AEEAERRLRQAEAD----RARQVQVALETAQRSAEVELQSKRASFAEKTAQ-----LERTLQEE 1743
Cdd:pfam12128 583 VKLDlkridvpewaasEEELRERLDKAEEAlqsaREKQAAAEEQLVQANGELEKASREETFARTALKnarldLRRLFDEK 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1744 HVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLaqaEAEKQKEEAEREARRRGKA 1823
Cdd:pfam12128 663 QSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYW---QVVEGALDAQLALLKAAIA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1824 EEQAVRQRELAEQELEKQRQLAegtaqQRLVAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATH----------- 1892
Cdd:pfam12128 740 ARRSGAKAELKALETWYKRDLA-----SLGVDPDVIAKL-------KREIRTLERKIERIAVRRQEVLRyfdwyqetwlq 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1893 KRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRAlaeetkRQRQLAEEDAARQR 1972
Cdd:pfam12128 808 RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANS 881
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1973 AEAERVLAEKLAAISEaTRLKTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 2026
Cdd:pfam12128 882 EQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1825-2199 |
4.26e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQL--AEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELA 1902
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1903 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEED--------------- 1967
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1968 AARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASE 2047
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2048 NELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQR 2126
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 2127 RREAEERVQKSLAAE-EEAARQRKSALEEVERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2199
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1503-2028 |
4.40e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.89 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1503 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR 1582
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1583 QVEAAERSRVRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEA 1659
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1660 ELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1739
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1740 LQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARR 1819
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1820 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEA 1899
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVL 1979
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2044209144 1980 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 2028
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1500-1685 |
4.54e-11 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 68.75 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1500 AEERERLAEVEAALEKQRQLAEAHAQ-AKAQAEREAEELQRRMQEEVARREEAavdaqQQKRSIQEELQHLRQSSEaeiQ 1578
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIA-----EAEAELAKKKAEERREAE---T 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1579 AKARQVEAAERSRVRIEEEIRVvrlQLEATERQRGGAEGELQALRARAEE-------AEAQKRQAQEEAErlrrqvqdes 1651
Cdd:COG2268 260 ARAEAEAAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELeadvrkpAEAEKQAAEAEAE---------- 326
|
170 180 190
....*....|....*....|....*....|....*
gi 2044209144 1652 qrkrqAEAE-LALRVKAEAEAAREKQRALQALEDV 1685
Cdd:COG2268 327 -----AEAEaIRAKGLAEAEGKRALAEAWNKLGDA 356
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1495-1693 |
4.63e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.29 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1495 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREeaavdAQQQKrsiQEELQHLRQSS 1573
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1574 EAEIQAKARQVEAAERSRvRIEEEIRVvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDESQR 1653
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAKK-KAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2044209144 1654 KRQAEAELAL-RVKAEAEAAREKQRALQALEDVRLQAEEAE 1693
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1463-2119 |
5.43e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 69.40 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1463 LRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQAEREA---EELQR 1539
Cdd:pfam07111 53 LELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1540 RMQEEVARREeaavdAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSrvrieeeirvvrlqLEATERQRGGAEGEL 1619
Cdd:pfam07111 132 KNLEEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1620 QalraraeeaeaqkrQAQEEAERLRRQVqdeSQRKRQAEAELALrvkaeAEAAReKQRALQALEDVRLQAEEAERRLRQA 1699
Cdd:pfam07111 193 A--------------EAQKEAELLRKQL---SKTQEELEAQVTL-----VESLR-KYVGEQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1700 EADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLreeaerraqqqaeaeraREEAEQELERWR 1779
Cdd:pfam07111 250 TMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEF-----------------PKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1780 LKANeALRLRLQAEEVAQQKSLaqaeAEKQKEEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLAEGTAQQRLVAEQ 1857
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSV----KQLRGQVAELQEQVTSQSQEQAILQRALQDKaaEVEVERMSAKGLQMELSRAQE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1858 ELIRLRAETEQGEQQRQL-----------LEEELARLQREAAAATHKRQELEAELAKVRAeMEVLLASK---ARAEEESR 1923
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKvalAQLRQESC 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1924 STSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQlAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 2003
Cdd:pfam07111 467 PPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2004 EAENER--LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLrkasENELERQKGLVEDTLRQRRQVEEEILALKASFEKA 2081
Cdd:pfam07111 546 QLEVARqgQQESTEEAASLRQELTQQQEIYGQALQEKVAEV----ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
650 660 670
....*....|....*....|....*....|....*...
gi 2044209144 2082 AAGKAELELELGRIRSNAEdtlrsKEQAELEATRQRQL 2119
Cdd:pfam07111 622 ATQEKERNQELRRLQDEAR-----KEEGQRLARRVQEL 654
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1352-1742 |
6.41e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1352 QLRYYRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQLV 1431
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1432 TYKAQLEPVAspAKKPKVQSGSESVIQEYVDLRTRYSElttltsQYIKFIRETLRRMEEEerlaeqqRAEERERLAEVEA 1511
Cdd:TIGR02169 755 NVKSELKELE--ARIEELEEDLHKLEEALNDLEARLSH------SRIPEIQAELSKLEEE-------VSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1512 ALEKQRQLaeahaqaKAQAEREAEELQRRMQEEVARREEaavdaqqqKRSIQEELQHLRQSSEAEIQAKARQVEAAERSR 1591
Cdd:TIGR02169 820 KLNRLTLE-------KEYLEKEIQELQEQRIDLKEQIKS--------IEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1592 VRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEAELALR-VKAEAE 1670
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE---IPEEELSLEdVQAELQ 961
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1671 aarEKQRALQALEDVRLQA----EEAERRLRQAEADRARQVQVALETAQRSAEVElQSKRASFAEKTAQLERTLQE 1742
Cdd:TIGR02169 962 ---RVEEEIRALEPVNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYE-KKKREVFMEAFEAINENFNE 1033
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4531-4569 |
7.74e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 7.74e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 4531 FLEAQYLTGGLIEPDVPGRVPLDEALQRGMVDARTAQKL 4569
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2302-2504 |
8.18e-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: 67.48 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2302 KQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEEL---FSVR 2378
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2379 VQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2458
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2044209144 2459 KMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQE 2504
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1792-2174 |
9.83e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1792 AEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG-TAQQRLVAEQEliRLRAETEQGE 1870
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAE--SLREDADDLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1871 QQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEASRFRE-LAEEAAR 1949
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELRErEAELEAT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1950 LRALAEETKRQRQLAEE----DAARQRAEAERV--LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAF---- 2019
Cdd:PRK02224 435 LRTARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2020 --QRRRLEEQAAQHKADIEE---RLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGR 2094
Cdd:PRK02224 515 eeRREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLER 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2095 IRS------NAEDTL-----RSKEQAELEATRQRQLaaeeeqrrreaeervqkslaaeeEAARQRKSALEEvERLKAKVE 2163
Cdd:PRK02224 594 IRTllaaiaDAEDEIerlreKREALAELNDERRERL-----------------------AEKRERKRELEA-EFDEARIE 649
|
410
....*....|.
gi 2044209144 2164 EARRLRERAEQ 2174
Cdd:PRK02224 650 EAREDKERAEE 660
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1824-2455 |
1.37e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.07 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1824 EEQAVRQRELAEQELEKQRQLAEGTAQ--------QRLVAEQELIRLR----------AETEQGEQQRQLLEEELARLQR 1885
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQLRARieelraqeAVLEETQERINRArkaaplaahiKAVTQIEQQAQRIHTELQSKMR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1886 EAAAATHKRQELEAELAKVRaEMEVLLASKARAEEESRSTSEKSKQRLE------AEASRFRELAEEAARLRALAEETKR 1959
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREiscqqhTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1960 QRQLAEEDAARQRAE--AERVLAEKLAAISEATRLKTEAEIALK---EKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 2034
Cdd:TIGR00618 401 ELDILQREQATIDTRtsAFRDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2035 IEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILA----------LKASFEKAAAGKAELELELGRIRSNAEDTLR 2104
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2105 SKEQAELE------ATRQRQLAAEEEQRRREAEERVQKSLaaeEEAARQRKSALEEVERLKAKVEEA-----RRLRERAE 2173
Cdd:TIGR00618 561 LKEQMQEIqqsfsiLTQCDNRSKEDIPNLQNITVRLQDLT---EKLSEAEDMLACEQHALLRKLQPEqdlqdVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2174 QESARQLQLAQEAAQKRL-QAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSR 2252
Cdd:TIGR00618 638 SQELALKLTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2253 RQVEEAERLKQLAEEQAQAQAQAQAAAEKlrkeaeqeaaRRAQAEQAALKQKQVADAEMEKHKKFAEQTLRQKAQVEQEL 2332
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAAREDALNQSLK----------ELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2333 TTLRLQLEETDHQKSILDEEL-QRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIeaenRALILRDKDNTQRFlQ 2411
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI----THQLLKYEECSKQL-A 862
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2044209144 2412 EEAEKMKQVAEEAARLSVAAQ-----EAARLRQLAEEDLAQQRALAEKM 2455
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKLNGINQikiqfDGDALIKFLHEITLYANVRLANQ 911
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1500-1986 |
1.37e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1500 AEERERLaeVEAALEKQRQLAEAHAQAKAQAEReAEELQRRMQEEVARREEAAVDAQQQKrsiqeelQHLRQSSEAEIQA 1579
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1580 KA--RQVEAAERSRVRIEEEIRVVRlqlEATERQrggaegelqalraraEEAEAQKRQAQEEAERLRRQVQDESQRkrqa 1657
Cdd:PRK04863 348 EKieRYQADLEELEERLEEQNEVVE---EADEQQ---------------EENEARAEAAEEEVDELKSQLADYQQA---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1658 eaelalrVKAEAEAAREKQRALQALEDVR-------LQAEEAERRLRQAEADRARQVQVALETAQRsaeVELQSKRASFA 1730
Cdd:PRK04863 406 -------LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1731 EKTAQLERTLQEEhvavaqlreeaerraqqqaeaerareeaEQELERWRlKANEALR----LRLQAEEVAQQKslaqaea 1806
Cdd:PRK04863 476 EQAYQLVRKIAGE----------------------------VSRSEAWD-VARELLRrlreQRHLAEQLQQLR------- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1807 ekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQgeqQRQLLEEELARLQRE 1886
Cdd:PRK04863 520 ----------------MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA---RLESLSESVSEARER 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1887 AAAATHKRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEE 1956
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALArlreqsgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
490 500 510
....*....|....*....|....*....|
gi 2044209144 1957 TKRQRQLAEEDAARQRAEAERVLAEKLAAI 1986
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAERFGGVLLSEI 690
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1476-2193 |
1.61e-10 |
|
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: 67.84 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1476 QYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDA 1555
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1556 QQQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRVRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1625
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1626 --AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEAELAlRVKAEAEAAREKQRALQAledvrlQAEEAERRLRQAEAD 1702
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1703 RARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQeehVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKA 1782
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1783 NEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1853
Cdd:pfam15921 391 KE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1854 VAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTHKRQELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1929
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1930 KQRLEAEASRFRELAEEAARLRALAEETKRQR-QLAEEDAA----RQ----------------------RAEAERVLAEK 1982
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQqienmtqlvgqhgrtagamqveKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1983 LAAISEATRLKTEAEIALKEKEAE---------------NERLRRLaEDEAFQRRRLEEQAAQHKADI-------EERLA 2040
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARvsdlelekvklvnagSERLRAV-KDIKQERDQLLNEVKTSRNELnslsedyEVLKR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2041 QLRKASE------NELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAG-KAELELELGRIrsnaeDTLRSK----EQA 2109
Cdd:pfam15921 682 NFRNKSEemetttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGmQKQITAKRGQI-----DALQSKiqflEEA 756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2110 ELEATRQRQLAAEEEQRRREAEERV---QKSLAAEEEAARQRKSALEE--------VERLKAKVEEARRLRERAEQESAR 2178
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEkvanmevaLDKASLQFAECQDIIQRQEQESVR 836
|
810
....*....|....*
gi 2044209144 2179 qLQLAQEAAQKRLQA 2193
Cdd:pfam15921 837 -LKLQHTLDVKELQG 850
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1268-1750 |
1.91e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1268 ELEATKAALKKLRVQAEAQQPV------FDALRDELRGAQEVGERLQRQHGERdvEVERWRERvaplLERWQAALAQTDV 1341
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAE----LEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1342 RQRELEQLgrqlryyresadplgawLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEierygeKVDECQQLAKQYIN 1421
Cdd:COG4913 310 ELERLEAR-----------------LDALREELDELEAQIRGNGGDRLEQLEREIERLER------ELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1422 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSELT------------------TLTSQYIKF- 1480
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDLRrelreleaeiaslerrksNIPARLLALr 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 --IRETLRRMEEEER-LAE--QQRAEERE-RLAeVEAALEKQRQ--LAEAHAQAKAQAEREAEELQRRMQ-EEVARREEA 1551
Cdd:COG4913 447 daLAEALGLDEAELPfVGEliEVRPEEERwRGA-IERVLGGFALtlLVPPEHYAAALRWVNRLHLRGRLVyERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1552 AVDAQQQKRSIQEEL------------QHLRQS-------SEAEIQAKARQVEAA-----ERSRVRIEEEIRVVRLQL-- 1605
Cdd:COG4913 526 PERPRLDPDSLAGKLdfkphpfrawleAELGRRfdyvcvdSPEELRRHPRAITRAgqvkgNGTRHEKDDRRRIRSRYVlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1606 EATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElaLRVKAEAEAAREKQRALQALEDV 1685
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 1686 RLQAEEAERRLRQAEA--DRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1750
Cdd:COG4913 684 SDDLAALEEQLEELEAelEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1520-1743 |
2.23e-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: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1520 AEAHAQAKAQAEREAEELQRRMQEEVARREEAavdaQQQKRSIQEELqhlrQSSEAEIQAKARQVEAAERSRVRIEEEIR 1599
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQL----AALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1600 VVRLQLEATERQRGGAEGELQALRARAEEAEAQKR-------QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1672
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 1673 REKQRALQALEDVRLQAEEAERRLRQAEADRARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1743
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1620-1975 |
3.38e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.69 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1620 QALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEAELAlrvkaeaeaaREKQRalqaledvRLQAEEAERRlRQA 1699
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKM------EQERLRQEKEEKA----------REVER--------RRKLEEAEKA-RQA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1700 EADRarQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWR 1779
Cdd:pfam17380 328 EMDR--QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1780 LKANEALRlRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEqaVRQRELA-EQELEKQRQLAEGTAQQRLVAEQE 1858
Cdd:pfam17380 406 ILEEERQR-KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER--VRLEEQErQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1859 LiRLRAETEqgEQQRQLLEEELARLQREAAAATHKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSKQRLEAEas 1938
Cdd:pfam17380 483 K-RDRKRAE--EQRRKILEKELEERKQAMIEEERKRKLLEKEMEE-RQKAIYEEERRREAEEERRKQQEMEERRRIQE-- 556
|
330 340 350
....*....|....*....|....*....|....*..
gi 2044209144 1939 RFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEA 1975
Cdd:pfam17380 557 QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| 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 2044209144 187 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 256
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 2044209144 257 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 288
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2318-2545 |
3.90e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2318 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELfsvRVQMEELSKLKARIEAENRA 2397
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2398 LILRdKDNTQRFLQEeAEKMKQVAEEAARLSVA-AQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2476
Cdd:COG4942 99 LEAQ-KEELAELLRA-LYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2477 QQQKElAQEQARQ-LQEDKEQMAQQLAQetqgFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2545
Cdd:COG4942 177 EALLA-ELEEERAaLEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1822-2119 |
4.07e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.30 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQ-RELAEQELEKQRQLAEG-TAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAthKRQELEA 1899
Cdd:pfam17380 295 KMEQERLRQeKEEKAREVERRRKLEEAeKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERI--RQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 ELAKVRaEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRAL--AEETKRQRQLAEEDAARQRaEAER 1977
Cdd:pfam17380 373 EISRMR-ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIraEQEEARQREVRRLEEERAR-EMER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1978 VLAEKLAAISEATRLKteaeialkEKEAENERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLRKASENELERQKGLV 2057
Cdd:pfam17380 451 VRLEEQERQQQVERLR--------QQEEERKRKKLELEKEKRDRKRAEEQ----RRKILEKELEERKQAMIEEERKRKLL 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 2058 EDTLRQRRQ-VEEEILALKASFEKaaagKAELELElGRIRSNAEDTLRSKEQAELEAT-RQRQL 2119
Cdd:pfam17380 519 EKEMEERQKaIYEEERRREAEEER----RKQQEME-ERRRIQEQMRKATEERSRLEAMeREREM 577
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1825-2712 |
4.10e-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: 66.74 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEGTAQQrlvAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKV 1904
Cdd:pfam01576 109 EEQLDEEEAARQKLQLEKVTTEAKIKK---LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKH 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1905 RAeMEVLLASKARAEEESRSTSEKSKQRLEAEASrfrELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLA 1984
Cdd:pfam01576 186 EA-MISDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1985 AISEATRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQAAQHKADIEERL------AQLRKASENEL-ERQKGLV 2057
Cdd:pfam01576 262 ALKKIREL--EAQISELQEDLESERAARNKAEK--QRRDLGEELEALKTELEDTLdttaaqQELRSKREQEVtELKKALE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2058 EDTLRQRRQVEE-------EILALKASFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEATRQRQlaaeeeqrr 2127
Cdd:pfam01576 338 EETRSHEAQLQEmrqkhtqALEELTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK--------- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2128 rEAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESAR----------QLQLAQEAAQkrlqaEEKA 2197
Cdd:pfam01576 409 -KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesQLQDTQELLQ-----EETR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2198 HAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAE----RLKQLAEEQAQAQA 2273
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEegkkRLQRELEALTQQLE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2274 QAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKF--------------AEQTLRQKAQVEQELT---TLR 2336
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFdqmlaeekaisaryAEERDRAEAEAREKETralSLA 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2337 LQLEETDHQKSILDEELQRLKAE--------------VTEAARQRNQVEEELFSVRVQMEELS-------KLKARIEAEN 2395
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEmedlvsskddvgknVHELERSKRALEQQVEEMKTQLEELEdelqateDAKLRLEVNM 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2396 RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLA-------EEDLAQQRALAEKMLKEKMQAVQEATR 2468
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKK 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2469 LKAEAELLQQQKE---LAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2545
Cdd:pfam01576 803 LQAQMKDLQRELEearASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2546 DAQRFRKQAEEIGEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQ 2625
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2626 EQLLQETRALQESFLSEKDRLLQRERfieqEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQR- 2704
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESR----ERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRq 1038
|
970
....*....|
gi 2044209144 2705 --EAEEGVRR 2712
Cdd:pfam01576 1039 leEAEEEASR 1048
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1209-2091 |
5.14e-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: 66.24 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1209 SELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEEVLRAHEEQLKEAQAVPATLPELEATK--AALKKLRVQAEAQ 1286
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1287 QPVFDALRDELRGAQEVGERLQRQHGERDVEVERWRERVAPLLERWQAALaQTDVR--QRELEQLGRQLRyyresadplg 1364
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIA---------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1365 awlqDAKQRQERIQAvPLANSQAVREQLQQEKELLE-EIERYGEKVDecqqlakQYINAIKDYELQLVTYKAQLEPVASP 1443
Cdd:TIGR02169 312 ----EKERELEDAEE-RLAKLEAEIDKLLAEIEELErEIEEERKRRD-------KLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1444 AKKPKvqsgsesviQEYVDLRTRYSELTtltsQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAH 1523
Cdd:TIGR02169 380 FAETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1524 AQAKAQAEREAEELQRRMQeevarreeaavDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERSRVRIEEEIRVVRL 1603
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1604 QLEATERQRGGAEGELQAL------RARAEEAEAQKR----------QAQEEAERLRR------------QVQDESQRKR 1655
Cdd:TIGR02169 512 VEEVLKASIQGVHGTVAQLgsvgerYATAIEVAAGNRlnnvvveddaVAKEAIELLKRrkagratflplnKMRDERRDLS 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1656 QAEAELALRVKAEAEAAREKQRAL--QALED-VRLQAEEAERRLrqaeADRARQVQVALETAQRSA-------------- 1718
Cdd:TIGR02169 592 ILSEDGVIGFAVDLVEFDPKYEPAfkYVFGDtLVVEDIEAARRL----MGKYRMVTLEGELFEKSGamtggsraprggil 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1719 -EVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELErwRLKANEAlRLRLQAEEVAQ 1797
Cdd:TIGR02169 668 fSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEE-KLKERLEELEE 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1798 QKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE--------LAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQG 1869
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlearLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1870 EQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEA------SR 1939
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdlKKERDELEAqlreleRK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1940 FRELAEEAARLRALAEETKRQRQLAEEdaarQRAEAERVLAEklaaISEATRLKTEAEIALKEKEAENERLRRLAEDEAF 2019
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEE----ELSEIEDPKGE----DEEIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2020 QRRRLEEQAAQHKaDIEERLAQLRKASENELERqkglVEDTLRQRRQVEEEIL-----ALKASFEKAAAGKAELELE 2091
Cdd:TIGR02169 977 AIQEYEEVLKRLD-ELKEKRAKLEEERKAILER----IEEYEKKKREVFMEAFeaineNFNEIFAELSGGTGELILE 1048
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1825-2195 |
5.22e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQR--------QLLEEELARLQREAAAATHKRQE 1896
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1897 L--------------EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLR----------- 1951
Cdd:COG4913 364 LeallaalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparll 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1952 ----ALAEETKRQR----------QLAEEDAARQRAeAERVL----------AEKLAAISEA-------TRLKTEaEIAL 2000
Cdd:COG4913 444 alrdALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLggfaltllvpPEHYAAALRWvnrlhlrGRLVYE-RVRT 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2001 KEKEAENERL--RRLAE-----DEAFQ---RRRLEEQAAQHKADIEERLAQLRKA-------SENELERQKG-------- 2055
Cdd:COG4913 522 GLPDPERPRLdpDSLAGkldfkPHPFRawlEAELGRRFDYVCVDSPEELRRHPRAitragqvKGNGTRHEKDdrrrirsr 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2056 --LVEDTLRQRRQVEEEILALKASFEKAAAGKAELelelgrirsnaedtlrskeQAELEATRQRQLAAEEEQRRREAEER 2133
Cdd:COG4913 602 yvLGFDNRAKLAALEAELAELEEELAEAEERLEAL-------------------EAELDALQERREALQRLAEYSWDEID 662
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 2134 VQkSLAAEEEAARQRKSALE----EVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2195
Cdd:COG4913 663 VA-SAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
181-285 |
6.54e-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: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 181 ERDRvQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQI 252
Cdd:cd21300 4 EGER-EARVFTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 2044209144 253 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 285
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1482-1705 |
7.70e-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: 64.40 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRS 1561
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1562 IQE---ELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1638
Cdd:COG4942 106 LAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1639 EAERLRRQVqdesQRKRQAEAELALRVKAEAEAAREKQRALQALEDV--RLQAEEAERRLRQAEADRAR 1705
Cdd:COG4942 186 ERAALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAA 250
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1514-1735 |
9.18e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1514 EKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEaavdaQQQKRSIQEELQhlRQSSEAEIQAKARQVEAAERsrvr 1593
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-----LEKERLAAQEQK--KQAEEAAKQAALKQKQAEEA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1594 ieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEAELALRVKAEAEAA 1672
Cdd:PRK09510 138 ----------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 1673 REKQRALQAledvrlqAEEAErrlRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1735
Cdd:PRK09510 203 AEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1245-2025 |
9.91e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 65.36 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1245 AEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRVQ-AEAQQpvfdALrDEL-------RGAQEVGERLQRQHGERDV 1316
Cdd:COG3096 366 QEEVVEEAAEQLAEAEA------RLEAAEEEVDSLKSQlADYQQ----AL-DVQqtraiqyQQAVQALEKARALCGLPDL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1317 EVERwrerVAPLLERWQAALAQTDVRQRELE-----------QLGRQLRYYRESADPL---GAWlQDAKQ--RQERIQAV 1380
Cdd:COG3096 435 TPEN----AEDYLAAFRAKEQQATEEVLELEqklsvadaarrQFEKAYELVCKIAGEVersQAW-QTAREllRRYRSQQA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1381 PLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVAspAKKPKVQSGSESVIQEY 1460
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE--EQAAEAVEQRSELRQQL 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1461 VDLRTRYSELTTLTSQYIKfIRETLRRMEEE---------------ERLAEQQRA--EERERLAEVEAALEKQ-RQLAEA 1522
Cdd:COG3096 588 EQLRARIKELAARAPAWLA-AQDALERLREQsgealadsqevtaamQQLLEREREatVERDELAARKQALESQiERLSQP 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1523 ----HAQAKAQAEREAEELQRRMQEEVARREEAAVDAQ----------QQKRSIQEELQHLrQSSEAEIQAKARQVEAAE 1588
Cdd:COG3096 667 ggaeDPRLLALAERLGGVLLSEIYDDVTLEDAPYFSALygparhaivvPDLSAVKEQLAGL-EDCPEDLYLIEGDPDSFD 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1589 RSRVRIEEEIRVVRLQLEatERQ-------------RGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ--- 1652
Cdd:COG3096 746 DSVFDAEELEDAVVVKLS--DRQwrysrfpevplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvg 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1653 --------------------RKRQAEAELA------LRVKAEAEAAREKQRALQAL---------EDVRLQAEEAERRLR 1697
Cdd:COG3096 824 ghlavafapdpeaelaalrqRRSELERELAqhraqeQQLRQQLDQLKEQLQLLNKLlpqanlladETLADRLEELREELD 903
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1698 QAEADRA--RQVQVALETAQRSAEVeLQSKRASFAEKTAQLERTLQEEHVAVAQLreeaerraqqqaeaerareeaeqel 1775
Cdd:COG3096 904 AAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQLQADYLQAKEQQRRLKQQI------------------------- 957
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1776 erwrlkanEALrlrlqaEEVAQQKslaqaeaEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLV 1854
Cdd:COG3096 958 --------FAL------SEVVQRR-------PHFSYEDAVGLLGENSDLNEKLRARlEQAEEARREAREQLRQAQAQYSQ 1016
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1855 AEQELIRLRAETEQGEQQRQLLEEELA----RLQREAAAATH-KRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS 1929
Cdd:COG3096 1017 YNQVLASLKSSRDAKQQTLQELEQELEelgvQADAEAEERARiRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1930 KQrLEAEASRFRELAEEA----ARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKlaaiseatrlkteAEIALKEKEA 2005
Cdd:COG3096 1097 RK-AERDYKQEREQVVQAkagwCAVLRLARDNDVERRLHRRELAYLSADELRSMSDK-------------ALGALRLAVA 1162
|
890 900
....*....|....*....|...
gi 2044209144 2006 ENERLR---RLAEDEAFQRRRLE 2025
Cdd:COG3096 1163 DNEHLRdalRLSEDPRRPERKVQ 1185
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1479-1721 |
1.08e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 63.40 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1479 KFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQ 1558
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1559 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEeirvVRLQLEATERQRGGAEGELQALRARAEEaEAQKRQAQE 1638
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREEAEKKARQ-RQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1639 EAERLRRQVQDESQRKRQAEAELALRVKAEAE------AAREKQRALQALEDVRLQAEEAER-RLRQAEADRARQVQVAL 1711
Cdd:pfam13868 243 EQIELKERRLAEEAEREEEEFERMLRKQAEDEeieqeeAEKRRMKRLEHRRELEKQIEEREEqRAAEREEELEEGERLRE 322
|
250
....*....|
gi 2044209144 1712 ETAQRSAEVE 1721
Cdd:pfam13868 323 EEAERRERIE 332
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
310-405 |
1.35e-09 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 59.24 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 310 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNL-----------------------EN 365
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 366 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 405
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1864-2425 |
1.36e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1864 AETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEASRFR 1941
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1942 E-LAEEAARLRALAEETKRQRQLAEEDAARQRAEAERV-LAEKLAAIS-EATRLKTEA---EIALKEKEAENERLRRLAE 2015
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeYLDELREIEkRLSRLEEEIngiEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2016 DEAFQRRRLEEQAAQHKA--DIEERLAQLR----KASENELERQKGLVEDTLRQRRQVEEEILALKASfekaaagKAELE 2089
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELErlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2090 LELGRIRSNAEDTLRSKEQ-----AELEATRQRQLAAEEEQRRREaeerVQKSLAAEEEAARQRKSALEEVERLKAKVEE 2164
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKR----IEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2165 ARRLRERAEQESArqlqlaqeaaqkrlqAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERA 2244
Cdd:PRK03918 495 LIKLKELAEQLKE---------------LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2245 EREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQTLRQ 2324
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2325 KA--QVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRA 2397
Cdd:PRK03918 640 KRleELRKELEELEKKYSEEEYEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
|
570 580
....*....|....*....|....*...
gi 2044209144 2398 LilrdkDNTQRfLQEEAEKMKQVAEEAA 2425
Cdd:PRK03918 720 L-----ERVEE-LREKVKKYKALLKERA 741
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1498-2015 |
1.77e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.59 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1498 QRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQAeREAEELQRRmQEEVARREEAAVDaqqqkrsiqeelqHLrqsseAE 1576
Cdd:COG3096 279 ERRELSERALELRRELfGARRQLAEEQYRLVEMA-RELEELSAR-ESDLEQDYQAASD-------------HL-----NL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1577 IQAKARQVEAAERSRVRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrkrq 1656
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD------- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1657 aeaelalrvkaeaeaareKQRALQALEDVRLQAEEAERRLRqaeadRARQVQVALETAQRSAEVELQSKRASFAEKTAQ- 1735
Cdd:COG3096 401 ------------------YQQALDVQQTRAIQYQQAVQALE-----KARALCGLPDLTPENAEDYLAAFRAKEQQATEEv 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1736 --LERTLQEEHVAVAQLReeaerraqqqaeaerareeaeqelerwrlKANEALRL------RLQAEEVAQQkslaqaeae 1807
Cdd:COG3096 458 leLEQKLSVADAARRQFE-----------------------------KAYELVCKiageveRSQAWQTARE--------- 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1808 kqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEgtaqqrlvaeqelirlraeTEQGEQQRQLLEEELARLQREA 1887
Cdd:COG3096 500 ---------------LLRRYRSQQALAQRLQQLRAQLAE-------------------LEQRLRQQQNAERLLEEFCQRI 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1888 AAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ------RLEAEASRFRELAEEAARLRALAEETKRQR 1961
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQlrarikELAARAPAWLAAQDALERLREQSGEALADS 625
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1962 QlaEEDAARQR-AEAERVL-AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAE 2015
Cdd:COG3096 626 Q--EVTAAMQQlLEREREAtVERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2302-2532 |
1.85e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2302 KQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQM 2381
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2382 EELSKLKARIEAENRALILRDKDNTQRFLQEeAEKMKQVAEE-AARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKM 2460
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRR-LQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2461 QAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLR 2532
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1164-1746 |
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 2044209144 1164 AQRIAEQ-QKAQAEVEGLGKGVARLSAEA---EKVLALPEPSPAA---PTLRSELELTLGKLEQVRSLSAIYLEKLKTIS 1236
Cdd:PRK04863 468 AQAAHSQfEQAYQLVRKIAGEVSRSEAWDvarELLRRLREQRHLAeqlQQLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1237 LVIRSTQGAEEVLRAHEEQLKEAQAVPAtlpELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDV 1316
Cdd:PRK04863 548 KNLDDEDELEQLQEELEARLESLSESVS---EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1317 EVERWRERVAPLLERWQAALAQTDVRQRELEQLGRQLryyRESADPLGAWLQDAKQRQERIQAVPLA------------- 1383
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARKQALDEEI---ERLSQPGGSEDPRLNALAERFGGVLLSeiyddvsledapy 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1384 ---------------NSQAVREQLQQEKELLEEI-------ERYGEKVDECQQLAKQYINAIKDYELQLVTYKAqlEPVA 1441
Cdd:PRK04863 702 fsalygparhaivvpDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLF 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1442 SPAKKPK----VQSGSESVIQEYVDLRTRYSELTTLTSQYIKFI----------------RETLRRMEEEERLAEQQRAE 1501
Cdd:PRK04863 780 GRAAREKrieqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIgshlavafeadpeaelRQLNRRRVELERALADHESQ 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1502 ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQA 1579
Cdd:PRK04863 860 EQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQ 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1580 KARQVEAAE------RSRVRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDES 1651
Cdd:PRK04863 940 LKQDYQQAQqtqrdaKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQL 1015
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1652 QRKRQAEAELALRVKAEAEAAREKQRALQALeDVRLQAEEAER-RLRQAEAD----RARQVQVALETAQRSAEVELQS-- 1724
Cdd:PRK04863 1016 AQYNQVLASLKSSYDAKRQMLQELKQELQDL-GVPADSGAEERaRARRDELHarlsANRSRRNQLEKQLTFCEAEMDNlt 1094
|
650 660
....*....|....*....|..
gi 2044209144 1725 KRASFAEKTAQLERTLQEEHVA 1746
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAKA 1116
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1448-2091 |
1.91e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1448 KVQSGSESVIQEYVDLRTRyselTTLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAK 1527
Cdd:pfam05483 131 KVSLKLEEEIQENKDLIKE----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK---MILAFEELR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1528 AQAEREAEELQRRMQEEvarreeaavdaqqqkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEA 1607
Cdd:pfam05483 204 VQAENARLEMHFKLKED------------------HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1608 TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAL----- 1682
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnkaka 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1683 ----------------------EDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1740
Cdd:pfam05483 346 ahsfvvtefeattcsleellrtEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1741 QEEHVA-----VAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAE-----EVAQQKSLAQAEAEKQK 1810
Cdd:pfam05483 426 QFEKIAeelkgKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEklkniELTAHCDKLLLENKELT 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1811 EEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlvaeQELIRLRAE-TEQGEQQRQLL---EEELARLQRE 1886
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR----DELESVREEfIQKGDEVKCKLdksEENARSIEYE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1887 AAAATHKRQELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEETKRQRQLAEE 1966
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIE----NKNKNIEELHQENKALKKKGSAEN---KQLNAYEIKVNKLELELASAKQKFEE 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1967 --DAARQRAEAERVLAEKLaaISEATRLKTEAEIALK-EKEAENERLRRLAEDEAFqrrrLEEQAAQHKADIEERLAQ-- 2041
Cdd:pfam05483 655 iiDNYQKEIEDKKISEEKL--LEEVEKAKAIADEAVKlQKEIDKRCQHKIAEMVAL----MEKHKHQYDKIIEERDSElg 728
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2042 LRKASENELERQKGLVEDTLRQRRQveeEILALKASFEKAAAGKAELELE 2091
Cdd:pfam05483 729 LYKNKEQEQSSAKAALEIELSNIKA---ELLSLKKQLEIEKEEKEKLKME 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1313-1966 |
1.98e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1313 ERDVEVERWRERVAPlLERWQAALAqtdVRQRELEQLGR-------------QLRYYRESADPLGAWLQDAKQRQERIQA 1379
Cdd:PRK03918 108 EGDSSVREWVERLIP-YHVFLNAIY---IRQGEIDAILEsdesrekvvrqilGLDDYENAYKNLGEVIKEIKRRIERLEK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1380 VpLANSQAVREQL-QQEKELLEEIERYGEKVDECQQLAKQYINAIKDYElqlvTYKAQLEPVASPAKKPKVQSGSESVIQ 1458
Cdd:PRK03918 184 F-IKRTENIEELIkEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1459 EYV-DLRTRYSELttltSQYIKFIRETLRRMEEEERLAEQQRA------EERERLAEVEAALEKQRQLAEAHAQAKAQAE 1531
Cdd:PRK03918 259 EKIrELEERIEEL----KKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1532 ---REAEELQRRMQEEVARREEAAVDAQ--QQKRSIQEELQHLRQS-SEAEIQAKARQVEAAERSRVRIEEEIRVVRlql 1605
Cdd:PRK03918 335 ekeERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKIT--- 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1606 eateRQRGGAEGELQALRARAEEAEAQK-------RQAQEE-----AERLRRQVQDESQRKRQAEAEL--ALRVKAEAEA 1671
Cdd:PRK03918 412 ----ARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrkelLEEYTAELKRIEKELKEIEEKErkLRKELRELEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1672 AREKQRALQALEDVRLQAEEAERRLRqaeadrarqvQVALETAQRSAEvELQSKRASFAEKTAQLeRTLQEEHVAVAQLR 1751
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLK----------KYNLEELEKKAE-EYEKLKEKLIKLKGEI-KSLKKELEKLEELK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1752 EEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1831
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1832 ELAEQELEKQRQLAEgtAQQRLVAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATHKRQELEAELAKVRAEMEVL 1911
Cdd:PRK03918 636 AETEKRLEELRKELE--ELEKKYSEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 1912 laSKARAEEESrstSEKSKQRLEAEASRFRELAEEAARlRALAEETKRQRQLAEE 1966
Cdd:PRK03918 707 --EKAKKELEK---LEKALERVEELREKVKKYKALLKE-RALSKVGEIASEIFEE 755
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2320-2619 |
2.92e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2320 QTLRQKA-QVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRvqmEELSKLKARiEAENRAL 2398
Cdd:PRK02224 359 EELREEAaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR---EERDELRER-EAELEAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2399 I--LRDKDNTQRFLQEEAE--KMKQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKmLKEKMQAVQEATRLKAEAE 2474
Cdd:PRK02224 435 LrtARERVEEAEALLEAGKcpECGQPVEGSPHVETIEEDRERVEELEAE-LEDLEEEVEE-VEERLERAEDLVEAEDRIE 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2475 LLQQQKELAQE---QARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFR 2551
Cdd:PRK02224 513 RLEERREDLEEliaERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2552 K-------------QAEEIGEKL-HRTELATQEKVTLVHTLEIQRQ-QSDHDAERLRAAIAELEREKEKLQEEATLLQQK 2616
Cdd:PRK02224 593 RirtllaaiadaedEIERLREKReALAELNDERRERLAEKRERKRElEAEFDEARIEEAREDKERAEEYLEQVEEKLDEL 672
|
...
gi 2044209144 2617 SEE 2619
Cdd:PRK02224 673 REE 675
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1247-2096 |
3.46e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.82 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1247 EVLRAHEEQLKEAQAVPATLPELEATKAALKKLRVQAEA----QQPVFDALRdelrgAQEVGERLQRQHGERDVEVERWR 1322
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasdhLNLVQTALR-----QQEKIERYQADLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1323 ERVAPLLERWQAALAQTDVRQRELEQLGRQLRYYRESADPL----GAWlQDAKQRQERIQ------AVPLANSQAVREQL 1392
Cdd:PRK04863 369 EVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQqtraIQY-QQAVQALERAKqlcglpDLTADNAEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1393 Q-QEKELLEEIERYGEKVDECQQLAKQYINAikdyeLQLVTykaqlePVASPAKKPKVQSGSESVIQEYVDLRTRYSELT 1471
Cdd:PRK04863 448 QaKEQEATEELLSLEQKLSVAQAAHSQFEQA-----YQLVR------KIAGEVSRSEAWDVARELLRRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1472 TLTSQYikfirETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQA-------EREAEEL 1537
Cdd:PRK04863 517 QLRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalRQQLEQL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1538 QRRMQEEVARREE--AAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATErQRGGA 1615
Cdd:PRK04863 592 QARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGS 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1616 EGE-LQALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDES-------------QRKRQA-- 1657
Cdd:PRK04863 671 EDPrLNALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDSFDDSvf 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1658 ---EAELALRVK-AEAE--------------AAREKQralqaLEDVRLQAEEAERRLRQAEADRaRQVQVALETAQR--- 1716
Cdd:PRK04863 751 sveELEKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAFSRfig 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1717 ---------SAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERwRLkanEALR 1787
Cdd:PRK04863 825 shlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLAD-RV---EEIR 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1788 LRLQAEEVAQQkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQ--------------LAEGTAQQR 1852
Cdd:PRK04863 901 EQLDEAEEAKR-FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDyQQAQQTQRDAKQqafaltevvqrrahFSYEDAAEM 979
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1853 LVAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQREAAAATHKRQELEAELAK--VRAEMEVLLASK 1915
Cdd:PRK04863 980 LAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAEERAR 1059
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1916 ARAEEESRSTSEKSKQRLEAEASRFR---ELAEEAARLRALAEETKRQRQLAEE---------DAARQRAEAERVLAEKL 1983
Cdd:PRK04863 1060 ARRDELHARLSANRSRRNQLEKQLTFceaEMDNLTKKLRKLERDYHEMREQVVNakagwcavlRLVKDNGVERRLHRREL 1139
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1984 AAISeATRLKTEAEI---ALKEKEAENERLR---RLAEDEAFQRR--RLEEQAAQH-----KADIeERLAQLRKASEnEL 2050
Cdd:PRK04863 1140 AYLS-ADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRPERkvQFYIAVYQHlreriRQDI-IRTDDPVEAIE-QM 1216
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 2044209144 2051 ERQKGLVEDTLRQRrqveEEILALkASFEKAAAGKAELELELGRIR 2096
Cdd:PRK04863 1217 EIELSRLTEELTSR----EQKLAI-SSESVANIIRKTIQREQNRIR 1257
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1363-1750 |
3.83e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1363 LGAWLQDAKQRQERIQAV-PLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINA---IKDYELQLVTYKAQLE 1438
Cdd:COG4717 47 LLERLEKEADELFKPQGRkPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeaeLEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1439 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfiRETLRRMEEEERLAEQQRAEERERL-AEVEAALEKQR 1517
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELREL--------EEELEELEAELAELQEELEELLEQLsLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1518 QLAEAHAQAKAQAEREAEELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAE--------------------- 1576
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltia 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1577 ---------------IQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEA 1640
Cdd:COG4717 277 gvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLeLLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1641 ERLRRQVQDESQRKRQaeAELALRVKAEAEAA-REKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAE 1719
Cdd:COG4717 357 EELEEELQLEELEQEI--AALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL 434
|
410 420 430
....*....|....*....|....*....|.
gi 2044209144 1720 VELQSKRASFAEKTAQLERTLQEEHVAVAQL 1750
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQL 465
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1860-2705 |
4.12e-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: 63.45 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1860 IRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEA-- 1935
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLMNlf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1936 EASRFRELAEEA----ARLRALAEETKRQRQLAEEDAARQraeaERVLAEKLAAISEATRLKTEAEIALKEKEAENERLR 2011
Cdd:TIGR00618 174 PLDQYTQLALMEfakkKSLHGKAELLTLRSQLLTLCTPCM----PDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2012 RLAEdeafQRRRLEEQAAQHKADIEERLAQLRKASENELERQkglvedtlrQRRQVEEeilalkasfeKAAAGKAELELE 2091
Cdd:TIGR00618 250 EAQE----EQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2092 LGRIRSNAEdtLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRER 2171
Cdd:TIGR00618 307 QQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2172 AEQESArQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQS 2251
Cdd:TIGR00618 385 QQQKTT-LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2252 RRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQTLRQKAQVEQE 2331
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2332 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELsklkarieaenralilrdkdntQRFLQ 2411
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------------------QDLTE 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2412 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDlaQQralaekmlKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQ 2491
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL--QQ--------CSQELALKLTALHALQLTLTQERVREHALSIRVLP 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2492 EDKEQMAQQLAQETQGFQRTLEAERQrQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEigeklhrtelatQEK 2571
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA------------ARE 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2572 VTLVHTL-EIQRQQsdhdaerlRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQEtRALQESFLSEKDRLLQre 2650
Cdd:TIGR00618 739 DALNQSLkELMHQA--------RTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN-RLREEDTHLLKTLEAE-- 807
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 2651 rfIEQEKAKLEQLFRDEVAKAQklreeqqrqqqqmeQEREQLVASMEEARQRQRE 2705
Cdd:TIGR00618 808 --IGQEIPSDEDILNLQCETLV--------------QEEEQFLSRLEEKSATLGE 846
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
301-403 |
4.59e-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: 57.10 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 301 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHRPMLI-DMSKVYRQTNLENLDQAFSVAERDLGV 379
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 2044209144 380 TRLLDPEDVDVPQPDEKSIITYVS 403
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
306-408 |
4.79e-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: 57.00 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 306 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHRPMLI-DMSKVYRQTNLENLDQAFSVAERDLGVTRLLD 384
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 2044209144 385 PEDVDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1522-1981 |
5.37e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 62.73 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1522 AHAQAKAQAEREAEELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVV 1601
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1602 RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA 1681
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1682 LEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQ 1761
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1762 AEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1841
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1842 RQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEE 1921
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1922 SRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAE 1981
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1595-2119 |
5.39e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 62.95 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1595 EEEIRVVRLQLEATER--QRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1672
Cdd:COG3899 699 GERDRAARLLLRAARRalARGAYAEALRYLE-RALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARAL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1673 REKQRALQALEDVRLQAEEAERRLRQAEADRARQV-QVALETAQRSAEVELQSK-RASFAEKTAQLERTLQEEHVAVAQL 1750
Cdd:COG3899 778 AALAALRHGNPPASARAYANLGLLLLGDYEEAYEFgELALALAERLGDRRLEARaLFNLGFILHWLGPLREALELLREAL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1751 REEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1830
Cdd:COG3899 858 EAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAA 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1831 RELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEV 1910
Cdd:COG3899 938 AAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAA 1017
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1911 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEAT 1990
Cdd:COG3899 1018 ALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAAL 1097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1991 RLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEE 2070
Cdd:COG3899 1098 AAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAA 1177
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2044209144 2071 ILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQL 2119
Cdd:COG3899 1178 LAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLL 1226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1824-2117 |
6.02e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1824 EEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAE--- 1900
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENElea 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1901 ------------LAKVRAEMEVLLASKARAEEESR-----------------STSEKSKQRLEAEASRFRELAEEAARLR 1951
Cdd:COG4717 239 aaleerlkearlLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1952 ALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAA 2029
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2030 QHKADIEERLAQLRKASENELERQKGLVEDTLRQR-RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 2108
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQEL 478
|
....*....
gi 2044209144 2109 AELEATRQR 2117
Cdd:COG4717 479 EELKAELRE 487
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1493-2053 |
6.76e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 62.57 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1493 RLAEQQRAEERERLAEVEAAlekQRQLAEAHAQAKAQAEREAEELQRRMQ-EEVARREEAAVDAQQQKRSIQEELQHLRQ 1571
Cdd:COG3899 674 RALEARGPEPLEERLFELAH---HLNRAGERDRAARLLLRAARRALARGAyAEALRYLERALELLPPDPEEEYRLALLLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1572 SSEAEIQAkaRQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGEL---QALRARAEEAEAQKRQAQEEAERLRRQVQ 1648
Cdd:COG3899 751 LAEALYLA--GRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgLLLLGDYEEAYEFGELALALAERLGDRRL 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1649 DESQRKRQAEAELALRVKAEAEAAREK--QRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKR 1726
Cdd:COG3899 829 EARALFNLGFILHWLGPLREALELLREalEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAA 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1727 ASFAEKTAQLERTLQEEHVAVAQ-LREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAE 1805
Cdd:COG3899 909 AAAALAAAELARLAAAAAAAAALaLAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAA 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1806 AEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQR 1885
Cdd:COG3899 989 AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAAL 1068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1886 EAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAE 1965
Cdd:COG3899 1069 LAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAA 1148
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1966 EDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 2045
Cdd:COG3899 1149 LLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLL 1228
|
....*...
gi 2044209144 2046 SENELERQ 2053
Cdd:COG3899 1229 AALALAAA 1236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1836-2197 |
7.90e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1836 QELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATH--KRQELEAELAKVRAEMEVLLA 1913
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1914 SKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLK 1993
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1994 TEAEIALKEKEAENERLRRLAE----------DEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQ 2063
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2064 RRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQrrreaeerVQKSLAAEEE 2143
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAGVEDEE 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 2144 AARQRKSALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQEAAQKRLQAEEKA 2197
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2302-2569 |
8.14e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.06 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2302 KQKQVADAEMEKHKKFAEQTLRQKAQVE----QELTtlRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEE--ELF 2375
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEisrmRELE--RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQkvEME 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2376 SVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaQQRALAEKM 2455
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2456 LKEKMQAVQEATRLKA--EAELLQQQKELAQEQARqlqedkeqmaqqlaqetqgfqRTLEAERQRQLEMSaEAERL--KL 2531
Cdd:pfam17380 501 LEERKQAMIEEERKRKllEKEMEERQKAIYEEERR---------------------REAEEERRKQQEME-ERRRIqeQM 558
|
250 260 270
....*....|....*....|....*....|....*...
gi 2044209144 2532 RVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQ 2569
Cdd:pfam17380 559 RKATEERSRLEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1482-1705 |
9.76e-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: 60.63 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAavdaqqqk 1559
Cdd:TIGR02794 67 QERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA-------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1560 rsiqeelqhlrqssEAEIQAKarqvEAAERSRvriEEEirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1639
Cdd:TIGR02794 139 --------------EAERKAK----EEAAKQA---EEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEE 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1640 ----AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRAR 1705
Cdd:TIGR02794 194 akakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1833-2064 |
1.02e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 60.63 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1833 LAEQELEKQRQLAEGTAQQrlvAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAelakvraemevll 1912
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKK---EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1913 askARAEEESRSTSEKSKQRLEAEASRfrelAEEAARLRALAEETKRQrqlAEEDAARQRAEAervlAEKLAaisEATRL 1992
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1993 KTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE----ERLAQLRKASENELERQKGLVEDTLRQR 2064
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1995-2444 |
1.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1995 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASENelerqkglvEDTLRQRRQVEEEILAL 2074
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQL---------LPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2075 KASFEKAAAGKAELElelgrirsNAEDTLRSKEQAELEAtrQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEE 2154
Cdd:COG4717 145 PERLEELEERLEELR--------ELEEELEELEAELAEL--QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2155 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAA 2234
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2235 EEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlKQKQVADAEMEKH 2314
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2315 KKFA------EQTLRQKAQVEQELTTLRLQLEETDHQ-KSILDEELQRLKAEVTEAARQR-NQVEEELFSVRVQMEELSK 2386
Cdd:COG4717 374 ALLAeagvedEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2387 LKARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEED 2444
Cdd:COG4717 454 ELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1454-1741 |
1.22e-08 |
|
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: 60.85 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1454 ESVIQEYVDLRTRYSELTTLTSQYIK---FIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA 1530
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQERAaygKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1531 EREAEELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATER 1610
Cdd:pfam19220 117 TAQAEALERQLAAETEQNRALE-EENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1611 QRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA-EAEAA-------------REKQ 1676
Cdd:pfam19220 196 RLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEAlTARAAateqllaearnqlRDRD 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1677 RALQALEDVRLQAE----EAERRLRQAEADRARQVQVALETAQRSAEVElqsKRAS-----FAEKTAQLERTLQ 1741
Cdd:pfam19220 276 EAIRAAERRLKEASierdTLERRLAGLEADLERRTQQFQEMQRARAELE---ERAEmltkaLAAKDAALERAEE 346
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1245-1610 |
1.29e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1245 AEEVLRAHEEQLKEAQAVPATL-PELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDVEVERWRE 1323
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1324 RVAPLLERWQAALAQTDVRQRELEQLGRQLRYYRESADPLGAWLqDAKQRQERIQAVPLANSQAVREQLQQEKELLE-EI 1402
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATErRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1403 ERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELttltsqyikfiR 1482
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL-----------S 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1483 ETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQAKAQAEREAEElqrrMQEEVARREEAAVDAQQQKRS 1561
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTLEE----AEALENKIEDDEEEARRRLKR 976
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1562 IQEELQHL---RQSSEAEIQAKA-------RQVEAAERSRVRIEEEIRvvRLQLEATER 1610
Cdd:TIGR02168 977 LENKIKELgpvNLAAIEEYEELKerydfltAQKEDLTEAKETLEEAIE--EIDREARER 1033
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1932-2172 |
1.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1932 RLEAEASRFRELAEEAARLRALAEETKRQR----QLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAEN 2007
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2008 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKAS 2077
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2078 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQlaaeeeqrrreaeervqkSLAAEEEAARQRKSAL-EEVE 2156
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR------------------ELEAEIASLERRKSNIpARLL 443
|
250
....*....|....*.
gi 2044209144 2157 RLKAKVEEARRLRERA 2172
Cdd:COG4913 444 ALRDALAEALGLDEAE 459
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1482-2118 |
1.70e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 61.35 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLAEQQRAEERERLAEVEAALE---KQRQL------AEAHAQAKAQAEREAEELQRRMQEEVARREEAA 1552
Cdd:PRK10246 252 LDELQQEASRRQQALQQALAAEEKAQPQLAALSlaqPARQLrphwerIQEQSAALAHTRQQIEEVNTRLQSTMALRARIR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1553 VDAQQQKRSIQEELQHLRQSseaeiqakarqveAAERSRVRIEEEirvvrlqleaterqrggaegELQALRARAEEAEAQ 1632
Cdd:PRK10246 332 HHAAKQSAELQAQQQSLNTW-------------LAEHDRFRQWNN--------------------ELAGWRAQFSQQTSD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1633 KRQAQEEAERLrrqvqDESQRKRQAEAELALRVKA-EAEAAREKQRALQALED--VRLQAEEAERRLRQAEADRARQvqv 1709
Cdd:PRK10246 379 REQLRQWQQQL-----THAEQKLNALPAITLTLTAdEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVAIQ--- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1710 ALETAQRSAEVELQSKRASFAEKTAQLE--RTLQEEHVAVAQLREEAERRAQQQA-----EAERAREEAEQELErwrLKA 1782
Cdd:PRK10246 451 NVTQEQTQRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAQLQAGQPcplcgSTSHPAVEAYQALE---PGV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1783 NEALRLRLQaEEVAQQKSlaqaEAEKQKEEAEREARRRGKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLVAEQELIRL 1862
Cdd:PRK10246 528 NQSRLDALE-KEVKKLGE----EGAALRGQLDALTKQLQRDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPW 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1863 RAETEQGEQQRQLLEEELArLQREAAAATHKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAE 1936
Cdd:PRK10246 602 LDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1937 ASRFRELAEEAARLRALAEetkrqrQLAEEDAArqRAEAERVLAEKLAAISEATrLKTEAEIALKEKEAENERlRRLAE- 2015
Cdd:PRK10246 681 QNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKa 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2016 ----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASENELERQKGLVEdtlrQRRQVEEEILALKASFEKAAAGKAE 2087
Cdd:PRK10246 751 qaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQ 826
|
650 660 670
....*....|....*....|....*....|....*.
gi 2044209144 2088 LELEL----GRIRSNAEDTLRSKEQAELEA-TRQRQ 2118
Cdd:PRK10246 827 IQQELaqlaQQLRENTTRQGEIRQQLKQDAdNRQQQ 862
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1827-2194 |
1.74e-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: 61.51 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1827 AVRQRELAEQELEKQRQLAeGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEE-------LARLQ---REAAAATHKRQE 1896
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQtalRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1897 LEAELAKVRAEMEVLLA---SKARAEEESRSTSEKSK----------QRLEA---------EASRFRELAEEAARLRALA 1954
Cdd:COG3096 356 LEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEVDslksqladyqQALDVqqtraiqyqQAVQALEKARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1955 EETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlrrlaeDEAFQR-RRLEEQAAQHKA 2033
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER------SQAWQTaRELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2034 dIEERLAQLRkASENELERQkglvedtLRQRRQVEEeilaLKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEA 2113
Cdd:COG3096 510 -LAQRLQQLR-AQLAELEQR-------LRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2114 TRQRqlaaEEEQRRREAEERVQKSLAAEEEAARQRKSALeevERLKAKVEEArrLRERAEQESARQLQLAQEAAQKRLQA 2193
Cdd:COG3096 577 VEQR----SELRQQLEQLRARIKELAARAPAWLAAQDAL---ERLREQSGEA--LADSQEVTAAMQQLLEREREATVERD 647
|
.
gi 2044209144 2194 E 2194
Cdd:COG3096 648 E 648
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
301-408 |
2.00e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.10 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 301 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHRPMLI-DMSKVYRQTNLENLDQAFSVAERDLGV 379
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 2044209144 380 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1855-2055 |
2.30e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1855 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1934
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1935 A---------------EASRFRELAEEAARLRALAEETKR---QRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEA 1996
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1997 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKG 2055
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1977-2713 |
2.56e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1977 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLRKASENELERQKGL 2056
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2057 VEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAED-TLRSKEQAELEATRQRQLAAEEEQRRREAEERVQ 2135
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2136 KSLAAEEEAARQRKSALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAA---------QKRLQAEEKAHAFAVQQKE 2206
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAelkeeledlRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2207 QELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEA 2286
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2287 EQEAARRAQAEQ--AALKQKQVADAEMEKHKKFAEQTLRQKAQVEQEL---------TTLRLQLEETDHQKSILDEELQR 2355
Cdd:TIGR02169 469 QELYDLKEEYDRveKELSKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgTVAQLGSVGERYATAIEVAAGNR 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2356 LKAEVTE----AARQRNQVEEE---------LFSVRVQMEELSKLKAR---------IEAENR-----------ALILRD 2402
Cdd:TIGR02169 549 LNNVVVEddavAKEAIELLKRRkagratflpLNKMRDERRDLSILSEDgvigfavdlVEFDPKyepafkyvfgdTLVVED 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2403 KDNTQRFLQ---------EEAEKMKQVA----EEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKM 2460
Cdd:TIGR02169 629 IEAARRLMGkyrmvtlegELFEKSGAMTggsrAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELS 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2461 QAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQEtqgfqrtLEAERQRQLEMSAEAERLklrvaemsraq 2540
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE-------IENVKSELKELEARIEEL----------- 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2541 araEEDAQRFRKQAEEIGEKLHRTELAtqekvtlvhtlEIQRQQSDHDAE--RLRAAIAELEREKEKLQEEATLLQQKSE 2618
Cdd:TIGR02169 771 ---EEDLHKLEEALNDLEARLSHSRIP-----------EIQAELSKLEEEvsRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2619 EmqvvqqeqllqetraLQESFLSEKDRLLQRERFIEQEKAKLEQLFRdEVAKAQKLREEQQRQQQQMEQEREQLVASMEE 2698
Cdd:TIGR02169 837 E---------------LQEQRIDLKEQIKSIEKEIENLNGKKEELEE-ELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
810
....*....|....*
gi 2044209144 2699 ARQRQREAEEGVRRK 2713
Cdd:TIGR02169 901 LERKIEELEAQIEKK 915
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1578-1799 |
2.71e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1578 QAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1657
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1658 EAELALRVKAEAEAAREKQRA-LQALEDVRLQAEEAERRLRQAEADRA-RQVQVALETAQRSAEVELQSKRASFAEKTAQ 1735
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1736 LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRL--RLQAEEVAQQK 1799
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2301-2759 |
2.91e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2301 LKQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQ 2380
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2381 MEELSKLKARIEAEnRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2460
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2461 QAVQEATRLKAEAELLQQQKE-LAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA 2539
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2540 QARAEEDAQRFRKQAEEIGEKLHRTE-----------------------------LATQEKVT----------------- 2573
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVDegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2574 -LVHTLEIQRQ--QSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRALQ-------------- 2636
Cdd:TIGR02168 550 vVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvd 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2637 --ESFLSEKDRLLQRERFI---------------------------EQEKAKLEQLFR---DEVAKAQKLREEQQRQQQQ 2684
Cdd:TIGR02168 630 dlDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktnssilerRREIEELEEKIEeleEKIAELEKALAELRKELEE 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 2685 MEQEREQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHRAALAHSEEI 2759
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1881-2042 |
2.94e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.50 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1881 ARLQREAAAAThKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEASRFRELAEEAARLRAlaEETKRQ 1960
Cdd:COG2268 206 AEAERETEIAI-AQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1961 RQLAEEDAARQR------AEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 2034
Cdd:COG2268 279 VQRQLEIAEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAI 358
|
....*...
gi 2044209144 2035 IEERLAQL 2042
Cdd:COG2268 359 LLMLIEKL 366
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1914-2185 |
3.20e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 59.96 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1914 SKARAEEESRSTSEKSKQRLEAEASRF-RELAEEAARLRALAEETKRQRQLAeEDAARQRAEAERVLAEKLAAISEATRL 1992
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREARHKKAAEARAAKDKDA-VAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1993 KTEAEIALKEKEAENERLRRLAEDEAfqrrrleEQAAQHKADIEERL--AQLRKASENELERQKGLVEDTlrQRRQVEEE 2070
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAA-------AAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2071 ILALKAsfEKAAAGKAELELElgrIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKS 2150
Cdd:PRK05035 586 IARAKA--KKAAQQAASAEPE---EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 2044209144 2151 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2185
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4453-4490 |
3.29e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 52.10 E-value: 3.29e-08
10 20 30
....*....|....*....|....*....|....*...
gi 2044209144 4453 QRLLEAQACTGGIIDPSSGERFPVTDAVSRGLVDKIMV 4490
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2318-2758 |
3.62e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2318 AEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRNQVEEELfSVRVQMEELSKLKARIEAENRA 2397
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2398 LI-LRDKDNTQRFLQEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2476
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2477 QQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARAEEDAQRFRKQAE 2555
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2556 EIGEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEmqvvqqeqlLQETRAL 2635
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE---------QEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2636 QESFLSEKDRLLQRERFIEQEKAKLEQLfrdEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQe 2715
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR- 452
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2044209144 2716 elqlleqqrqqqerllaEENQRLRERLQRLEEEHRAALAHSEE 2758
Cdd:COG4717 453 -----------------EELAELEAELEQLEEDGELAELLQEL 478
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2301-2834 |
3.76e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2301 LKQKQVADAEMEKHKkfaEQTLRQKAQVEQE--LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVR 2378
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNH---EGKAEAKAHVGQDegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAE 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2379 VQMEELSKLKaRIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAaQEAARLRQLAEEDLAQQRALAEKMLK- 2457
Cdd:PTZ00121 1119 EAKKKAEDAR-KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA-RKAEDAKKAEAARKAEEVRKAEELRKa 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2458 EKMQAVQEATRLKAEAELlqqqkelaqEQARQLQEDKEQMAQQLAQET-QGFQRTLEAERQRQLEMSAEAERLKLRVAEM 2536
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKA---------EEARKAEDAKKAEAVKKAEEAkKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2537 SRAQARAEEdaqrfRKQAEEIG---EKLHRTELATQEKVTLVHTLEIQrqqsdhdAERLRAAiAELEREKEKLQEEATLL 2613
Cdd:PTZ00121 1268 RQAAIKAEE-----ARKADELKkaeEKKKADEAKKAEEKKKADEAKKK-------AEEAKKA-DEAKKKAEEAKKKADAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2614 QQKSEEMQVVQQEQLLQETRALQESFLSEKDRLLQRERfIEQEKAKLEQLFR--DEVAKAQKLReeqqrqqqqmeqereq 2691
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKkaEEKKKADEAK---------------- 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2692 lvasmEEARQRQREAEEgVRRKQEELQLLEQQRQQqerllAEENQRLRERLQRLEEEHRAALAHSEEIAASQAAASKALP 2771
Cdd:PTZ00121 1398 -----KKAEEDKKKADE-LKKAAAAKKKADEAKKK-----AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 2772 NGRDVLDGPAAEAEPEHAFDGLRRKVPAQRLQevgilsAEELQRLAQGRTTVAELAQREDVRQ 2834
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKK------ADEAKKAAEAKKKADEAKKAEEAKK 1523
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1620-2016 |
4.65e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1620 QALRARAEEAEAQKRQA--QEEAERLRRQVQDESQRKRQAEAE-------LALRVKAEAEAAREKQ-------------R 1677
Cdd:PRK04863 287 EALELRRELYTSRRQLAaeQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRQQEKIERyqadleeleerleE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1678 ALQALEDVRLQAEEAERRLRQAEA--DRARQ----VQVALETAQRSAEVELQSKRAsfAEKTAQLertLQEEHVAVAQLr 1751
Cdd:PRK04863 367 QNEVVEEADEQQEENEARAEAAEEevDELKSqladYQQALDVQQTRAIQYQQAVQA--LERAKQL---CGLPDLTADNA- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1752 eeaerraqqqaeaerareeaEQELERWRLKANEALRLRLQAEevaQQKSLAQAEAEKQKEEAEREARRRG---------- 1821
Cdd:PRK04863 441 --------------------EDWLEEFQAKEQEATEELLSLE---QKLSVAQAAHSQFEQAYQLVRKIAGevsrseawdv 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 --KAEEQAVRQRELAEQELEKQRQLAEgtAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAthkRQELEA 1899
Cdd:PRK04863 498 arELLRRLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR---LESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 ELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEASRFRELAEEAARLRALAEET---------KRQRQLAEEDAAR 1970
Cdd:PRK04863 573 SVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEfedsqdvteYMQQLLERERELT 644
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2044209144 1971 QraEAERVLAEKLAAISEATRLkteaeiaLKEKEAENERLRRLAED 2016
Cdd:PRK04863 645 V--ERDELAARKQALDEEIERL-------SQPGGSEDPRLNALAER 681
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1490-1674 |
4.90e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1490 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAvdaqqQKRSIQEelqhl 1569
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-----KKKAEAE----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1570 rQSSEAEIQAKARQVEAAERsrvrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1649
Cdd:PRK09510 175 -AAKKAAAEAKKKAEAEAAA--------------KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 2044209144 1650 ESQRKRQAEAELALRVKAEAEAARE 1674
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1822-2042 |
4.90e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEkQRQLAEgtaQQRLVA-EQELIRLRAETEQGEQQRQLLEEElarlQREAAAAthKRQELEAE 1900
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQ-QKQAAE---QERLKQlEKERLAAQEQKKQAEEAAKQAALK----QKQAEEA--AAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1901 LAKVRAEMEVLLASKARAEEESrstseksKQRLEAEAsrfRELAEEAARLRALAEETKrqrQLAEEDAARQRAEAERVlA 1980
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEA-------KKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-A 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1981 EKLAAISEATRLKTEAEIALKEKEAEnerlrrlAEDEAFQRRRLEEQAAQHKADIEERLAQL 2042
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAA-------AEKAAAAKAAEKAAAAKAAAEVDDLFGGL 266
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2418-2620 |
5.81e-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: 58.62 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2418 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATRL--KAEAELLQQQKELA--QEQARQLQED 2493
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2494 KEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2573
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2044209144 2574 LVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEM 2620
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
186-290 |
5.98e-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: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 186 QKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHR 260
Cdd:cd21299 5 EERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQL 77
|
90 100 110
....*....|....*....|....*....|
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILH 290
Cdd:cd21299 78 KFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1486-1719 |
6.34e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.01 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKrsIQEE 1565
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER--IQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1566 LQHLRQSSEAEIQAKARQVEAAERSRVRI---------EEEIRVVRLQLEATERQRggAEGELQALRARAEEAEAQKRQA 1636
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1637 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQR 1716
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
...
gi 2044209144 1717 SAE 1719
Cdd:pfam13868 272 EDE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1634-2181 |
6.48e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1634 RQAQEEAERLRRQVQ-----DESQRKRQAEAELALRVKAEAEAAR--EKQRALQALEDvRLQAEEAERRLRQAEADRARQ 1706
Cdd:COG4913 238 ERAHEALEDAREQIEllepiRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEA-ELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1707 VQVALETAQRSAEVELQSkrasfaEKTAQLERtLQEEhvavaqlreeaerraqqqaeaerareeaeqeLERWRLKANEAL 1786
Cdd:COG4913 317 RLDALREELDELEAQIRG------NGGDRLEQ-LERE-------------------------------IERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1787 RLRLQAEEVAQQKSLAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAET 1866
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1867 EQGEQQRQLLEEELARLQRE-AAAATHKRQELE--AELAKVRAE-------MEVLLASKAR------------------- 1917
Cdd:COG4913 429 ASLERRKSNIPARLLALRDAlAEALGLDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrl 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1918 ---------------AEEESRSTSEKS-KQRLEAEASRFRE-LAEEAARLRALA-----EETKR---------------- 1959
Cdd:COG4913 509 hlrgrlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRAwLEAELGRRFDYVcvdspEELRRhpraitragqvkgngt 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1960 ------QRQLAEE-----DAARQRAEAERVLAEKLAAISEATRLKTEAEialKEKEAENERLRRLAEDEAFQRRRLEEQA 2028
Cdd:COG4913 589 rhekddRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALE---AELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2029 AQHK-ADIEERLAQLRKASeNELERQKglvedtlRQRRQVEEEILALKASFEKAAAGKAELELELGRIRsnaedtlrske 2107
Cdd:COG4913 666 AEREiAELEAELERLDASS-DDLAALE-------EQLEELEAELEELEEELDELKGEIGRLEKELEQAE----------- 726
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 2108 qaeleaTRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQ 2181
Cdd:COG4913 727 ------EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1476-1737 |
6.64e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 59.19 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1476 QYIKFIRETLRRMEEEERLAEQ--QRAEER-ERLAEVEAA-LEKQRQLAEAHAQAKAQA---------EREAEELQRRMQ 1542
Cdd:PRK05035 429 QYYRQAKAEIRAIEQEKKKAEEakARFEARqARLEREKAArEARHKKAAEARAAKDKDAvaaalarvkAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1543 EEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAA-ERSRVRIEEeirvvrlQLEATERQRGGAEGELQA 1621
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAA-------QQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1622 LRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAeaeaarekQRALQALEDVRLQAEEAERRLRQAEA 1701
Cdd:PRK05035 582 VAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA-RAKA--------KKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270
....*....|....*....|....*....|....*.
gi 2044209144 1702 DRARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1737
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
180-291 |
7.36e-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: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 180 DERDRVQ--KKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIA 253
Cdd:cd21222 9 EAPEKLAevKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLA 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 2044209144 254 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21222 84 LELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4184-4220 |
8.34e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 8.34e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 4184 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4220
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1618-2076 |
9.16e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1618 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeAEAAREKQRALQALEDVRLQAEEAERRLR 1697
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-----LEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1698 QAEADRARQVQvaLETAQRSAEVELQSKRASFAEKtaqLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELER 1777
Cdd:COG4717 150 ELEERLEELRE--LEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1778 WR--LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAvrqrELAEQELEKQRQLAEGTAQQRLVA 1855
Cdd:COG4717 225 LEeeLEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA----GVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1856 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRLEA 1935
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1936 EASrfrelAEEAARLRALAEETKRQRQLAEEdaarqRAEAERVLAEKLAAISEATRLKTEAEIalkekEAENERLRRLAE 2015
Cdd:COG4717 378 EAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEEL-----EEELEELEEELE 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2016 DEAFQRRRLEEQaaqhKADIEERLAQLrkASENELERQKGLVEDTLRQRRQVEEEILALKA 2076
Cdd:COG4717 443 ELEEELEELREE----LAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1640-2096 |
9.24e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 58.88 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1640 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAledvRLQAEEAERRLRQAEADRARQVQVALETAqrSAE 1719
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1720 VELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQK 1799
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1800 SLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEE 1879
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1880 LARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKR 1959
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1960 QRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERL 2039
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2040 AQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIR 2096
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1292-1691 |
1.06e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1292 ALRDELRGAQEVGERLQRQHGERDVEVERWRERVAPLLERWQAA-----LAQTDVRQREleQLGRqlryYRESADPLGAW 1366
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1367 LQDAKQRQERIQAVpLANSQAVREQLQQE-KELLEEIERYGEKVDECQQLAKQYINAIKDYE-LQLVTYKAQLEPVASPA 1444
Cdd:COG3096 363 LEEQEEVVEEAAEQ-LAEAEARLEAAEEEvDSLKSQLADYQQALDVQQTRAIQYQQAVQALEkARALCGLPDLTPENAED 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1445 KKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIrETLRRMeeeerlaeqqrAEERERlaevEAALEKQRQLAEAHA 1524
Cdd:COG3096 442 YLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKI-----------AGEVER----SQAWQTARELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1525 QAKAQAEREAE------ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEeei 1598
Cdd:COG3096 506 SQQALAQRLQQlraqlaELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE--- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1599 rvvrlqleaTERQRGGAEGELQALRARAEEAeaqkRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRA 1678
Cdd:COG3096 583 ---------LRQQLEQLRARIKELAARAPAW----LAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDEL 649
|
410
....*....|...
gi 2044209144 1679 LQALEDVRLQAEE 1691
Cdd:COG3096 650 AARKQALESQIER 662
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1797-1992 |
1.11e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1797 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLL 1876
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1877 EEELARLQREAAAATHKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEE 1956
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 2044209144 1957 TKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRL 1992
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| 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 2044209144 188 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQ 261
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARG 75
|
90 100
....*....|....*....|....*.
gi 2044209144 262 VKLVNIRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21286 76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1246-1436 |
1.51e-07 |
|
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: 55.14 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1246 EEVLRAHEEQLKEAQaVPATLPELEATKAALKKLRVQAEAQQPVFDALrdelrgaQEVGERLQRQHGERDVEVERWRERv 1325
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEIQERLEE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1326 apLLERWQAALAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDAKQRQERIQavPLANSQAVREQLQQEKELLEEIERY 1405
Cdd:cd00176 84 --LNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 2044209144 1406 GEKVDECQQLAKQYINAIKDYELQLVTYKAQ 1436
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1506-1918 |
1.54e-07 |
|
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: 58.33 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1506 LAEVEAALEKQRQLAEAHAQAkaqaeREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1574
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1575 --------AEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1646
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1647 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKR 1726
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1727 ASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEA 1806
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1807 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1886
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 2044209144 1887 AAAATHKRQELEAELAKVRAEMEVLLASKARA 1918
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1210-1658 |
1.63e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1210 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRVQAEAQQPV 1289
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1290 FDALRDELRGAQEVGERLQRQHGERDVEVERWRERVAPLL-------ERWQAALAQtdvRQRELEQLGRQLRYYRESADP 1362
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqdlaeelEELQQRLAE---LEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1363 LGAWLQDAKQRQERIQAVPLANSQAVREQLQ-QEKELLEEIERYGEKVDECQQLAKQYInaikdyelqLVTYKAQLEPVA 1441
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLgLGGSLLSLILTIAGVLFLVLGLLALLF---------LLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1442 SPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTsqyIKFIRETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAE 1521
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLS---PEELLELLDRIEELQEL-LREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1522 AHAQAKAQAEREAEELQRRmQEEVARREEAAVDAQQQKRSIQEELQHLRQSS-EAEIQAKARQVEAAERSRVRIEEEIRV 1600
Cdd:COG4717 379 AGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1601 VRLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAE 1658
Cdd:COG4717 458 LEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1556-2100 |
1.68e-07 |
|
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: 57.73 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1556 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1633
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1634 RQAQEEAERLRRQVQDESQRKRQAEAELALrVKAE--------AEAAREKQRALQALEDVRLQAEEAERRLRQ--AEADR 1703
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEEltIELIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1704 ARQvqvALETAqRSAEVELQSKRASFA----EKTAQLERTLQEEHVAVAQLREEAERRAQQQAeaerareeaeqelerwR 1779
Cdd:pfam05701 192 TKE---SLESA-HAAHLEAEEHRIGAAlareQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------K 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1780 LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAeeqAVRQRELAEQEL--EKQRqlaegtaqqrlvAEQ 1857
Cdd:pfam05701 252 LETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAAL---ASAKKELEEVKAniEKAK------------DEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1858 ELIRLRAETEQGEQQRQllEEELARLQREAAAATHKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAea 1937
Cdd:pfam05701 317 NCLRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1938 srfrelAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA--ENERLRRLAE 2015
Cdd:pfam05701 390 ------AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTN 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2016 DEAFQR-------------RRLEEQAAQHKADIEERLAQLRKASENELERQKGLvEDTLRQRRQVEEEILALKASFEKAA 2082
Cdd:pfam05701 464 QEDSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAK 542
|
570
....*....|....*...
gi 2044209144 2083 AGKAELELELGRIRSNAE 2100
Cdd:pfam05701 543 EGKLAAEQELRKWRAEHE 560
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2460-2615 |
1.69e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 57.72 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2460 MQAVQEATRlkaeaELLQQQKELA-------QEQ-ARQLQEDKEQMAQ-QLAQetQGFQRTLEAERQRQLEMSAEAERLK 2530
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAaARHQAELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2531 LRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVHTLEIQRQQSDHDAERlRAAIAELEREKEK-LQE 2608
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAKeLAD 784
|
....*...
gi 2044209144 2609 -EATLLQQ 2615
Cdd:PTZ00491 785 iEATKFER 792
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1556-1737 |
1.74e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1556 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRvvrlqleaterqrggaegelqalraraEEAEAQKRQ 1635
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1636 AQeEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADR---ARQVQVALE 1712
Cdd:PRK09510 120 AE-EAAKQAALKQKQAEEAAAKAAAAA-KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAA 197
|
170 180
....*....|....*....|....*
gi 2044209144 1713 TAQRSAEVELQSKRASFAEKTAQLE 1737
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1486-1747 |
1.84e-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: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVAR--REEAAVDAQQQKRSIQ 1563
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1564 EELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRvvrlqleaterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1643
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1644 RRQVQDESQR-KRQA-EAELALRVKAEAEAARE--KQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAE 1719
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 2044209144 1720 VELQSKRASFAEKTAQLERTLQEEHVAV 1747
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1496-1729 |
2.13e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1496 EQQRAEERERLAEVEAALEKQrqLAEAHAQAkAQAEREAEELQRrmQEEVARREEAAVDAQQQKRSIQEELQHLrQSSEA 1575
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQ--LPELRKEL-EEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEA-RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1576 EIQAKARQVEAAERSRVRIEEEIRVVRlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR-K 1654
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 1655 RQAEAELALRVKAEAEAAREKQRALQALEdvRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASF 1729
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLA--ELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2307-2507 |
2.26e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2307 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEE--- 2383
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2384 --------LSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2455
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2456 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQG 2507
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1496-1653 |
2.55e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1496 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRrmqeEVARREEAAVDAQQQKRSIQEELQHLRqsSEA 1575
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1576 EIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1653
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1877-2195 |
2.59e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.80 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1877 EEELARLQREAAAATHKRQ-ELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE 1955
Cdd:pfam02029 4 EEEAARERRRRAREERRRQkEEEEPSGQVTESVEP--NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1956 ETKRQRQLAEEDAARQRAEAERvlaeklaaisEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHkadi 2035
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAER----------KENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWST---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2036 eerlAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATR 2115
Cdd:pfam02029 148 ----EVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2116 QRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALE----------------EVERLKAKVEEARRLRERAEQ--ESA 2177
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKEseefeklrqkqqeaelELEELKKKREERRKLLEEEEQrrKQE 303
|
330
....*....|....*...
gi 2044209144 2178 RQLQLAQEAAQKRLQAEE 2195
Cdd:pfam02029 304 EAERKLREEEEKRRMKEE 321
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1191-1743 |
2.78e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1191 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLRAHEEQLKEaqaVPATLPELE 1270
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1271 ATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLqrqhgerdvevERWRERVAPLLERWQAaLAQTDVRQRELEQLG 1350
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-----------SRLEEEINGIEERIKE-LEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1351 RQLRYYRESADPLGAWLQDAKQRQERIQAVplaNSQAVREQLQQEKELLEEIERYGEKVDEcqqlakqYINAIKDYELQL 1430
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEELERL---KKRLTGLTPEKLEKELEELEKAKEEIEE-------EISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1431 VTYKAQLEPVASPAKKPKVQS---GSESVIQEYVDLRTRYSElttltsqYIKFIRETLRRMEEEERlaeqqraEERERLA 1507
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1508 EVEAALEKQRQLAEAHAQAKAQAEREaEELQRRMQEEVARREEAAvdaqqqkRSIQEELQHLrqssEAEIQAKARQVEAA 1587
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEY-------EKLKEKLIKL----KGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1588 ErsrvRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKA 1667
Cdd:PRK03918 552 E----ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KLEE 626
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 1668 EAEAAREK-QRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERtLQEE 1743
Cdd:PRK03918 627 ELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LKEE 702
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1593-1707 |
3.28e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.82 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1593 RIEEEIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------RQVQDESQRKR-QAEAELA 1662
Cdd:COG1566 87 QAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQQELDEARAALdAAQAQLE 165
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2044209144 1663 lRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQV 1707
Cdd:COG1566 166 -AAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1857-2584 |
3.39e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1857 QELIRLRAETEQGEQQRQLLEEELARLQ-REAAAATHK-RQELEAELAKVRAEM----EVLLASKARAEEESRSTSEKSK 1930
Cdd:pfam15921 187 QEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKiLRELDTEISYLKGRIfpveDQLEALKSESQNKIELLLQQHQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1931 QRLEAEASR----FRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE 2006
Cdd:pfam15921 267 DRIEQLISEheveITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2007 NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL-----RKASENELERQK-----------GLVEDTLRQR---RQV 2067
Cdd:pfam15921 347 LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEKEQnkrlwdrdtgnSITIDHLRRElddRNM 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2068 EEEIL-ALKASFEKAAAGkaELELELGRIRSNAEDTLR-SKEQAELEATRQrqlaaeEEQRRREAEERVQKSLAAEEEAA 2145
Cdd:pfam15921 427 EVQRLeALLKAMKSECQG--QMERQMAAIQGKNESLEKvSSLTAQLESTKE------MLRKVVEELTAKKMTLESSERTV 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2146 RQRKSALEEVER-LKAKVEEARRLRERAEQESARQLQLAQEAAQKR-LQAEEKAHAFAVQQKEQELQQTlqqeqsmlerl 2223
Cdd:pfam15921 499 SDLTASLQEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEIL----------- 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2224 raeaeaarraaeeaeeareraereaaqsRRQVEEAERLkqlaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalkq 2303
Cdd:pfam15921 568 ----------------------------RQQIENMTQL------------------------------------------ 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2304 kqvadaeMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT----EAARQRNQVEEELFSVRV 2379
Cdd:pfam15921 578 -------VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdlelEKVKLVNAGSERLRAVKD 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2380 QMEELSKLKARIEAENRAL--ILRDKDNTQRFLQEEAEKMKQVAEE-AARLSVAAQEAARLRQ-LAEEDLAQQRAL--AE 2453
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNtLKSMEGSDGHAMkvAM 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2454 KMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAqetqgfqrTLEAERQR---QLE-MSAEAERL 2529
Cdd:pfam15921 731 GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS--------TVATEKNKmagELEvLRSQERRL 802
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2530 KLRVAEMSRAQARAEedaqrfrKQAEEIGEKLHRTElatQEKV--TLVHTLEIQRQQ 2584
Cdd:pfam15921 803 KEKVANMEVALDKAS-------LQFAECQDIIQRQE---QESVrlKLQHTLDVKELQ 849
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1511-1687 |
3.96e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1511 AALEKQRQLAEAHA--QAKAQAEREAEELQRR---MQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVE 1585
Cdd:COG1579 1 AMPEDLRALLDLQEldSELDRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1586 AAER--SRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELal 1663
Cdd:COG1579 77 KYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL-- 154
|
170 180
....*....|....*....|....
gi 2044209144 1664 rvKAEAEAAREKQRALQALEDVRL 1687
Cdd:COG1579 155 --EAELEELEAEREELAAKIPPEL 176
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
763-855 |
4.19e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.18 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 763 HGFVAAATKELMWLSEKEEEEVGFDWGEHNSNMAGKKESYSALMRELEVKEKKIKEIQSTGDRLLREGHPARPTVESFQA 842
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 2044209144 843 ALQTQWSWMLQLC 855
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1822-2195 |
4.37e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.03 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLVAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRElaeeaarlralAEETKRQRQLAEEDAARQRAEAERVLAE 1981
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-----------EETEIREKEYQENKWSTEVRQAEEEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1982 KLAAISEATRLKTEAEIALKEK-EAENERLRRLAEDEAF--QRRRLEEQAAQhkadieerlaqlrkASENELERQKGLVE 2058
Cdd:pfam02029 159 EEDKSEEAEEVPTENFAKEEVKdEKIKKEKKVKYESKVFldQKRGHPEVKSQ--------------NGEEEVTKLKVTTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2059 DTLRQRRQVEEEilalkasfEKAAAGKAELELELGRIR-SNAEdtlrsKEQAELEATRQRQLAAEEEQRRREAEERVQKS 2137
Cdd:pfam02029 225 RRQGGLSQSQER--------EEEAEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRK 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 2138 LAAEEEaaRQRKSalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2195
Cdd:pfam02029 292 LLEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1342-1735 |
5.73e-07 |
|
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: 56.21 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1342 RQRELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYin 1421
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVC-- 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1422 aikdyeLQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRAE 1501
Cdd:TIGR00606 788 ------LTDVTIMERFQMELKDVERKIAQQAAKL---QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1502 ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAE---ELQRRMQEEVARREEAAVDAQQQKRSIQ--EELQHLRQSS--- 1573
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVElstEVQSLIREIKDAKEQDSPLETFLEKDQQekEELISSKETSnkk 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1574 -EAEIQAKARQVEAAERSRVRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ 1652
Cdd:TIGR00606 939 aQDKVNDIKEKVKNIHGYMKDIENKIQ------DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1653 RKRQAEAELALRVKAE--AEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFA 1730
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
....*
gi 2044209144 1731 EKTAQ 1735
Cdd:TIGR00606 1093 EPQFR 1097
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2085-2759 |
6.02e-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: 56.13 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2085 KAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEE 2164
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2165 ARRLRERAEQESARQLQLAQEAAQ-KRLQAEEKAHAfavqqkeqelqqtlqqeqsmlerlraeaeaarraaeeaeeARER 2243
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLE----------------------------------------ETQE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2244 AEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQK--QVADAEMEKHKKFAEQT 2321
Cdd:TIGR00618 285 RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllQTLHSQEIHIRDAHEVA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2322 LRQKAQVEQElTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAEnralilr 2401
Cdd:TIGR00618 365 TSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ------- 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2402 dkdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQkE 2481
Cdd:TIGR00618 437 -----QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS-C 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2482 LAQEQARQLQ----------EDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFR 2551
Cdd:TIGR00618 511 IHPNPARQDIdnpgpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2552 KQAEEI--------------GEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKS 2617
Cdd:TIGR00618 591 NITVRLqdlteklseaedmlACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2618 EEMQVVQQEQLLQETRALQESFLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASME 2697
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 2698 EARQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRER------LQRLEEEHRAALAHSEEI 2759
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLReedthlLKTLEAEIGQEIPSDEDI 818
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2947-2983 |
6.04e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 6.04e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 2947 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 2983
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3606-3642 |
6.04e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 6.04e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 3606 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 3642
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1870-2045 |
6.39e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1870 EQQRQLLEEELAR-LQREAAAATHKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEASrfrelAEEAA 1948
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1949 RLRALAEetkrqrQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 2028
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 2044209144 2029 AQHKADIEERLAQLRKA 2045
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1822-1977 |
7.00e-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: 54.85 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1902 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAE---EAARLRALAEETKRQRQLAeedAARQRAEAER 1977
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEAAKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1821-2063 |
7.38e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 55.34 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1821 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLVAEqelirlRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAE 1900
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAE------RAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1901 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeasrfrelaEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLA 1980
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1981 EKlaaiseatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVED 2059
Cdd:pfam15709 450 EK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQE 518
|
....
gi 2044209144 2060 TLRQ 2063
Cdd:pfam15709 519 QARQ 522
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1203-1880 |
7.82e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.96 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1203 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQG-AEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRV 1281
Cdd:PRK10246 164 AKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAqASGVALLTPEQVQSLTA------SLQVLTDEEKQLLT 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1282 QAEAQQPVFDAL--RDELrgAQEVGERLQRQHgerdvEVERWRERVAPLLERWQAALAQTDVR---QRELEQLGRqLRYY 1356
Cdd:PRK10246 238 AQQQQQQSLNWLtrLDEL--QQEASRRQQALQ-----QALAAEEKAQPQLAALSLAQPARQLRphwERIQEQSAA-LAHT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1357 RESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYElQLVTYKAQ 1436
Cdd:PRK10246 310 RQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQFSQQTSDRE-QLRQWQQQ 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1437 LE---------PVASPAKKPKVQSGSESVIQEYVDLRTRyseLTTLTSQYIKFIR------ETLRRMEEEERLAEQQRAE 1501
Cdd:PRK10246 389 LThaeqklnalPAITLTLTADEVAAALAQHAEQRPLRQR---LVALHGQIVPQQKrlaqlqVAIQNVTQEQTQRNAALNE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1502 ERERLAeveaalEKQRQLAEAHAQAKAQAEREAEELQRRMQEE------VARREEAAVDAQQQkrsiqeelqhlrqsseA 1575
Cdd:PRK10246 466 MRQRYK------EKTQQLADVKTICEQEARIKDLEAQRAQLQAgqpcplCGSTSHPAVEAYQA----------------L 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1576 EIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALrARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1655
Cdd:PRK10246 524 EPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSL-RQEEQALTQQWQAVCASLNITLQPQDDIQPWL 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1656 QAEAElalrvkaeaeaaREKQ-RALQALEDVRLQAEEAERRLRQAEADRArQVQVALETAQRSAEVELQSKRASFA---- 1730
Cdd:PRK10246 603 DAQEE------------HERQlRLLSQRHELQGQIAAHNQQIIQYQQQIE-QRQQQLLTALAGYALTLPQEDEEASwlat 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1731 -EKTAQLERTLQEEHVAV-AQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEK 1808
Cdd:PRK10246 670 rQQEAQSWQQRQNELTALqNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQK 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1809 QKEEAEREARRRGKA----------EEQAVRQRELAEQELEKQRQLAE---GTAQQRLVAEQ----ELIRLRAETEQGEQ 1871
Cdd:PRK10246 750 AQAQFDTALQASVFDdqqaflaallDEETLTQLEQLKQNLENQRQQAQtlvTQTAQALAQHQqhrpDGLDLTVTVEQIQQ 829
|
....*....
gi 2044209144 1872 QRQLLEEEL 1880
Cdd:PRK10246 830 ELAQLAQQL 838
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1527-1738 |
7.92e-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: 54.85 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1527 KAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRvRIEEEIRVVRLQLE 1606
Cdd:TIGR02794 28 KPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK-ELEQRAAAEKAAKQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1607 ATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrQVQDESQRKRQAEAelalRVKAEAEAAREKQRALQALEDVR 1686
Cdd:TIGR02794 107 AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAEAEA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1687 LQAEEAERRLRQAEADR--ARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1738
Cdd:TIGR02794 180 KAKAEAEAKAKAEEAKAkaEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4287-4315 |
9.21e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.21e-07
10 20
....*....|....*....|....*....
gi 2044209144 4287 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4315
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1342-1700 |
1.05e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.87 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1342 RQRELEQLGRQlryyRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEI----ERYGEKVDECQQLAK 1417
Cdd:pfam02029 12 RRRAREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTakreERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1418 QYINAIKDYElqlvtykaqlEPVASPAKKPKVQSGSESVIQEYVDLR-TRYSELTTLTSQyikfiRETLRRMEEEERLAE 1496
Cdd:pfam02029 88 EFDPTIADEK----------ESVAERKENNEEEENSSWEKEEKRDSRlGRYKEEETEIRE-----KEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1497 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AEELQRRMQEEVARREEAAVDAqqqkrsiqEELQHLRQSSEA 1575
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvKYESKVFLDQKRGHPEVKSQNG--------EEEVTKLKVTTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1576 EIQAKARQVEAAER-SRVRIEEEIRvvrlqLEATERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1653
Cdd:pfam02029 225 RRQGGLSQSQEREEeAEVFLEAEQK-----LEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQR 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2044209144 1654 KRQAEAElalRVKAEAEaarEKQRALQALEdvRLQAEEAERRLRQAE 1700
Cdd:pfam02029 300 RKQEEAE---RKLREEE---EKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2410-2601 |
1.06e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2410 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKAEAELLQQQKELAQEQAR 2488
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2489 QLQEDKEQMA----QQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2564
Cdd:COG4913 327 ELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180 190
....*....|....*....|....*....|....*..
gi 2044209144 2565 elatqekvtlVHTLEIQRQQSDHDAERLRAAIAELER 2601
Cdd:COG4913 407 ----------LAEAEAALRDLRRELRELEAEIASLER 433
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2308-2839 |
1.11e-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: 55.36 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2308 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKaevtEAARQRNQVEEELFSVRVQMEELSKL 2387
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2388 KARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLA------EEDLAQQRALAEKMLKEKM 2460
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2461 QAVQEATRLKAEAELLQQQKELAQeQARQLQEDKEQMAQQLAQETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQ 2540
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK------ELDILQREQATIDTRTSAFRDLQGQLAH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2541 ARAEEDAQRFRKQAEEigekLHRTELATQEKVTLVHTLEIQrQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEM 2620
Cdd:TIGR00618 429 AKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2621 QVVQQEQLLQETRALQESFLSEKDRLLQRerfIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVAsMEEAR 2700
Cdd:TIGR00618 504 CPLCGSCIHPNPARQDIDNPGPLTRRMQR---GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI-LTQCD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2701 QRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHRAALAHSEEiaasqaaaskalpngrdvldgp 2780
Cdd:TIGR00618 580 NRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC---------------------- 637
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2781 aaeaepehafdglrrkvpAQRLQEVGILSAEELQRLAQGRTTVAELAQREDVRQYLQGR 2839
Cdd:TIGR00618 638 ------------------SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1453-1741 |
1.21e-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: 54.84 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1453 SESVIQEyvDLRTRYSELTTLTSQYIKFIREtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-A 1526
Cdd:pfam15450 219 AESSLRE--ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1527 KAQAERE-AEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRV----RIEEEIRVV 1601
Cdd:pfam15450 295 KGQLEESqAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKDLSDHFLalswRLDLQEQTL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1602 RLQLEATERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlq 1680
Cdd:pfam15450 375 GLKLSEAKKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKAREFEVEA-- 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 1681 aledvrlqaeeaerrLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1741
Cdd:pfam15450 453 ---------------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1496-2175 |
1.50e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1496 EQQRAEERERLAEVEAALEKQRQLAE---AHAQAKAQAEREAEELQRRMQE------------------EVARREEAAVD 1554
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNeikALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyhnhqrTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1555 AQQQKRSIQEELQHLRQS-SEAEIQAKARQVEA---AERSRVRiEEEIRVVRLQLEATERQRgGAEGELQALRARAEEAE 1630
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEkTELLVEQGRLQLQAdrhQEHIRAR-DSLIQSLATRLELDGFER-GPFSERQIKNFHTLVIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1631 AQKRQAQeEAERLRRQVQDESQRKRQAEAELALRVKA--------------EAEAAREKQRALQALEDVRLQAEEAERRL 1696
Cdd:TIGR00606 402 RQEDEAK-TAAQLCADLQSKERLKQEQADEIRDEKKGlgrtielkkeilekKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1697 RQAEADrarqvqvaLETAQRSAEVELQSKRA-SFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQEL 1775
Cdd:TIGR00606 481 RKAERE--------LSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1776 ERWRLKANEALRL------RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE-LAEQELEKQRQLAEGT 1848
Cdd:TIGR00606 553 KIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVC 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1849 AQQRLvaEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQ----------ELEAELAKVRAEMEVLLASKARA 1918
Cdd:TIGR00606 633 GSQDE--ESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDK 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1919 EEESRSTSEKSKQR-------LEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATR 1991
Cdd:TIGR00606 711 LKSTESELKKKEKRrdemlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1992 LKTEAEIALKEKEAENERLRRLAE------DEAFQRRRLEEQAAQHKAD------------IEERLAQLR--KASENELE 2051
Cdd:TIGR00606 791 VTIMERFQMELKDVERKIAQQAAKlqgsdlDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQhlKSKTNELK 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2052 RQKGLVEDTLRQRRQVEE-------EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEE 2124
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV 950
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2125 QRRREAEERVQKSLaaEEEAARQRKSALEEVERLKAKVEEARRLRERAEQE 2175
Cdd:TIGR00606 951 KNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1482-1731 |
1.62e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 53.89 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLAEQQRAEERERL--AEVEAALEKQRQ---LAEAHAQAKAQAEREAEELQRRMqeevarrEEAAVDAQ 1556
Cdd:pfam15558 87 KQVIEKESRWREQAEDQENQRQEKLerARQEAEQRKQCQeqrLKEKEEELQALREQNSLQLQERL-------EEACHKRQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1557 QQKRSIQEELQHLRQSSEAEIQAKARQVEaaerSRVRIEEEIRvvRLQLE-----ATERQRGGAEGELQALRARAEEAEA 1631
Cdd:pfam15558 160 LKEREEQKKVQENNLSELLNHQARKVLVD----CQAKAEELLR--RLSLEqslqrSQENYEQLVEERHRELREKAQKEEE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1632 QKRQAQEEAERLRRQvQDESQRKRQAEAELALRvKAEAEAAREKQRALQALEDVRLQAEEAERRLRQ----AEADRARQV 1707
Cdd:pfam15558 234 QFQRAKWRAEEKEEE-RQEHKEALAELADRKIQ-QARQVAHKTVQDKAQRARELNLEREKNHHILKLkvekEEKCHREGI 311
|
250 260
....*....|....*....|....
gi 2044209144 1708 QVALETAQRSAEVELQSKRASFAE 1731
Cdd:pfam15558 312 KEAIKKKEQRSEQISREKEATLEE 335
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2303-2489 |
1.69e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 54.26 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2303 QKQVADAEMEKHKKFAEQTLRQkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTeaarqrnQVEEELFSVRVQME 2382
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQ--QREEELEELQEQLEDLESSIQELEKEIKKLESSIK-------QVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2383 ELSKLKARIEaenRAL-ILRDKDNT----QRFLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2454
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*..
gi 2044209144 2455 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQARQ 2489
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSRS 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1825-2556 |
1.70e-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: 54.73 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQlAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELAR-----LQREAAAATHKRQELEA 1899
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 ElakvraemevllaskaraEEESRSTSEKSKQRLEAEASRFRELAEEAARLR-----ALAEETKRQRQLaEEDAARQRAE 1974
Cdd:pfam05483 177 E------------------REETRQVYMDLNNNIEKMILAFEELRVQAENARlemhfKLKEDHEKIQHL-EEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1975 AERVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRRLEeQAAQHKADIEERLAQLRKASENELERQK 2054
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2055 GLVED---TLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEeqrrreae 2131
Cdd:pfam05483 314 ALEEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2132 erVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEK-AHAFAVQqkeqe 2208
Cdd:pfam05483 386 --LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ----- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2209 lqqtlqqeqsmlerlraeaeaarraaeeaeearerAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQ 2288
Cdd:pfam05483 459 -----------------------------------LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2289 EAARRAQAEQAALKQKQvadaEMEKHKKFAEQTLRQKAQVEQELTTLRLQLE--------ETDHQKSILD---EELQRLK 2357
Cdd:pfam05483 504 LTQEASDMTLELKKHQE----DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIE 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2358 AEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALilrDKDNTQRFLQEEAEKMKqVAEEAARLSVAAQEAARL 2437
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL---KKKGSAENKQLNAYEIK-VNKLELELASAKQKFEEI 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2438 RQLAEEDLAQQRALAEKMLKEKMQA---VQEATRLKAEAELLQQQKelAQEQARQLQEDKEQMAQQLAQETQ--GFQRTL 2512
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIDKRCQHK--IAEMVALMEKHKHQYDKIIEERDSelGLYKNK 733
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 2044209144 2513 EAErQRQLEMSAEAERLKLRVAEMS-RAQARAE-EDAQRFRKQAEE 2556
Cdd:pfam05483 734 EQE-QSSAKAALEIELSNIKAELLSlKKQLEIEkEEKEKLKMEAKE 778
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1846-2225 |
1.74e-06 |
|
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: 53.92 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1846 EGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEmevLLASKARAEEESRST 1925
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAA---LREAEAAKEELRIEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1926 SEKSKQRLEAEasrfRELAEEAARLRALAEETKRQR-QLAEEDAARQRAEAERVlaeklaaiseatrlkteaeialkeke 2004
Cdd:pfam19220 114 RDKTAQAEALE----RQLAAETEQNRALEEENKALReEAQAAEKALQRAEGELA-------------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2005 AENERLRRLAEDEAFQRRRLEEQAAqhkadieeRLAQL-RKASENElerqkGLVEDTLRQRRQVEEEILALKASFEKAAA 2083
Cdd:pfam19220 164 TARERLALLEQENRRLQALSEEQAA--------ELAELtRRLAELE-----TQLDATRARLRALEGQLAAEQAERERAEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2084 gKAELELELGRIRSNAEDTLRSKEQAELEATRQrqLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAkvE 2163
Cdd:pfam19220 231 -QLEEAVEAHRAERASLRMKLEALTARAAATEQ--LLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEA--D 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 2164 EARRLRERAEQESARQ-LQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRA 2225
Cdd:pfam19220 306 LERRTQQFQEMQRARAeLEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAA 368
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2326-2556 |
1.97e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2326 AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELfsvRVQMEELSKLKARIEAENralilrdkdn 2405
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL---EALQAEIDKLQAEIAEAE---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2406 tqrflQEEAEKMKQVAEEAARLSVAAQEAARLRQLAE----EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKE 2481
Cdd:COG3883 79 -----AEIEERREELGERARALYRSGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 2482 LAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2556
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1516-1644 |
1.98e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 53.13 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1516 QRQLAEAHAQ-AKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRVRI 1594
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1595 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1644
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4070-4107 |
2.01e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.01e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2044209144 4070 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 4107
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2395-2759 |
2.04e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2395 NRALILRDKDNTQRflQEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2469
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2470 -------KAEA-----ELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGF--QRTLEAERQRQLEMSAEAERLkLRVAE 2535
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2536 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVhtlEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQ 2615
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2616 KSEEMqvvqqeqllqetralqesflsekdrLLQRERFIEQEKAKLEQLFRdEVAKAQKLREEQQRQQQQMEQEREQLVAS 2695
Cdd:COG3096 505 RSQQA-------------------------LAQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2696 MEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQR------LRERLQRLEEEHRAALAHSEEI 2759
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEV 628
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1374-1738 |
2.08e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 53.96 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1374 QERIQAVPLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK-VQSG 1452
Cdd:pfam03528 7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKaVATV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1453 SESVIQEYVDLRTRYSELTTLTSQYIkfIRETLRRMEEE-ERLAEQQRAEererlaeveaalekqrqlaeaHAQAKAQAE 1531
Cdd:pfam03528 87 SENTKQEAIDEVKSQWQEEVASLQAI--MKETVREYEVQfHRRLEQERAQ---------------------WNQYRESAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1532 REAEELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQA-KARQVEAAERSRVRIEEEIRVVRLQLEATER 1610
Cdd:pfam03528 144 REIADLRRRLSE--GQEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlKAKLTEAEDKIKELEASKMKELNHYLEAEKS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1611 QRGGAEGELQALraraeeaEAQKRQAQEEAERLRRQVQDESqRKRQAEAELALRVKAEAEAAREkqralQALEDVRLQAE 1690
Cdd:pfam03528 222 CRTDLEMYVAVL-------NTQKSVLQEDAEKLRKELHEVC-HLLEQERQQHNQLKHTWQKAND-----QFLESQRLLMR 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2044209144 1691 EAERRLRQAEADRARQVqvalETAQRSAEVELQSKRASFAEKTAQLER 1738
Cdd:pfam03528 289 DMQRMESVLTSEQLRQV----EEIKKKDQEEHKRARTHKEKETLKSDR 332
|
|
| 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 2044209144 181 ERDRVQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIA 253
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2044209144 254 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 293
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1464-1583 |
2.27e-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: 52.68 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1464 RTRYSELTTLTSQYIKFIR----ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKaqaeREAEELqr 1539
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQEqlkiERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRR----RNEELL-- 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2044209144 1540 RMQEEVARREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKARQ 1583
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKE 177
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1486-1601 |
2.30e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.80 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-EREAEELQRRMQEEVARREEAAVD---------A 1555
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1556 QQQKR----SIQEELQHLRQSSEAEiqaKARQVEAAERsRVRIEEEIRVV 1601
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAE---EKARLEAEER-RQKEEEAARLA 508
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1856-1949 |
2.49e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 54.19 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1856 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEA 1935
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEITDQ 224
|
90
....*....|....
gi 2044209144 1936 EASRFrELAEEAAR 1949
Cdd:PRK11448 225 AAKRL-ELSEEETR 237
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1482-1743 |
2.52e-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: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLA-EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEElqrrMQEEVARREEAAVDAQQQKR 1560
Cdd:pfam07888 57 REKEKERYKRDREQwERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE----LSEEKDALLAQRAAHEARIR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1561 SIQEELQHLRQSS---EAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1637
Cdd:pfam07888 133 ELEEDIKTLTQRVlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1638 EEAERLRRQVQDESQRKRQAEAELA-LRVKAE----------------AEAAREKQRALQALEDVRLQAEEAERRLRQA- 1699
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAENEALLEeLRSLQErlnaserkveglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADAs 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2044209144 1700 ---EADRARQVQvALETAQRSAEVElQSKRASFAEKTAQLERTLQEE 1743
Cdd:pfam07888 293 lalREGRARWAQ-ERETLQQSAEAD-KDRIEKLSAELQRLEERLQEE 337
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2325-2750 |
2.67e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2325 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIE--AENRALILR 2401
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2402 DKDNTQRFLQEEAEKMKQVAEEA------ARLSVAAQEAARLRQlaeEDLAQQRALAEKMLKEKMQAVQEATRlkaEAEL 2475
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERddllaeAGLDDADAEAVEARR---EELEDRDEELRDRLEECRVAAQAHNE---EAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2476 LQQQKELAQEQARQLQEDkeqmAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2555
Cdd:PRK02224 347 LREDADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2556 EIGEKLhrTELATQEKvTLVHTLEIQRQ-----------QSDHDAERL------RAAIAELEREKEKLQEEATLLQQKSE 2618
Cdd:PRK02224 423 ELRERE--AELEATLR-TARERVEEAEAlleagkcpecgQPVEGSPHVetieedRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2619 EMQVVQQEQLLQETRALQESFLSEkdRLLQRERFIEQEKAKLEQLFR--DEVAKAQKLREEQQRQQQQMEQEREQLVASM 2696
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEE--LIAERRETIEEKRERAEELREraAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2697 EEARQRQREAEEGVRR------KQEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHR 2750
Cdd:PRK02224 578 NSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2311-2614 |
2.91e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2311 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKAR 2390
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2391 IEAENRAL------ILRDKDNTQRFLQEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2462
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2463 vqeatrlKAEAELLQQQKELaqeqaRQLQEDKEQMAQQLAQETqgfqrtLEAERQRQLEmsaEAERLKLRVAEMSRAQAR 2542
Cdd:TIGR04523 528 -------KLESEKKEKESKI-----SDLEDELNKDDFELKKEN------LEKEIDEKNK---EIEELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2543 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQ 2614
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1333-1593 |
2.97e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1333 QAALAQTDVRQRELEQLGRQLRYYREsadplgaWLQDAKQRQERIQavplansQAVREQLQQEKELLEEIERYGEKVDEC 1412
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEK-------ELAALKKEEKALL-------KQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1413 QQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKpkvqsgsesviqeyvdlRTRYSELTTLTSQyiKFIRETLRRMEEEE 1492
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYR-----------------LGRQPPLALLLSP--EDFLDAVRRLQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1493 RLAeQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQs 1572
Cdd:COG4942 143 YLA-PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ- 220
|
250 260
....*....|....*....|.
gi 2044209144 1573 SEAEIQAKARQVEAAERSRVR 1593
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAE 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1821-2095 |
3.15e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1821 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAE 1900
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1901 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEE-TKRQRQLAEEDAARQR---AEAE 1976
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEELAALEQELQAlseAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1977 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGL 2056
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270
....*....|....*....|....*....|....*....
gi 2044209144 2057 VEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRI 2095
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1913-2112 |
4.65e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1913 ASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQrqlaEEDAARQRAEAERVLAEKLAAISEATRL 1992
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1993 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEIL 2072
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2044209144 2073 ALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 2112
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2418-2620 |
4.68e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.16 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2418 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQM 2497
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2498 AQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVHT 2577
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2044209144 2578 LEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEM 2620
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1925-2196 |
4.93e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.23 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1925 TSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEA-EIALKEK 2003
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2004 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKAsfeKAAA 2083
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2084 GKAELELELGRIRSNAEDTLRSKEQAElEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAK-V 2162
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270
....*....|....*....|....*....|....
gi 2044209144 2163 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2196
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE 290
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1825-2461 |
5.27e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEgtAQQRLvAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKV 1904
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAA--ARERL-AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1905 RAEMEVLLAS--------KARAEEESRSTsEKSKQRLEAEASRFRELAEeAARLRALAEETKRQRQLAEEDAARQRAEAE 1976
Cdd:COG4913 322 REELDELEAQirgnggdrLEQLEREIERL-ERELEERERRRARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1977 RVLAEklAAISEATRLKTEAEIALKEKEAENERLRR----LAEDEAFQRRRLEEQAAQHKADI----------------- 2035
Cdd:COG4913 400 LEALE--EALAEAEAALRDLRRELRELEAEIASLERrksnIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwr 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2036 -----------------EERLAQLRKASENELERQK---GLVEDTLR--QRRQVEEEILALKASFEKAAAGkAELELELG 2093
Cdd:COG4913 478 gaiervlggfaltllvpPEHYAAALRWVNRLHLRGRlvyERVRTGLPdpERPRLDPDSLAGKLDFKPHPFR-AWLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2094 R----IRSNAEDTLRSKEQAeleATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLR 2169
Cdd:COG4913 557 RrfdyVCVDSPEELRRHPRA---ITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2170 ERAEQEsarqlqlaQEAAQKRLQAEEKAHAFAVQQKEQElqqtlqqeqsmlerlraeaeaarraaeeaeeareraereaa 2249
Cdd:COG4913 634 EALEAE--------LDALQERREALQRLAEYSWDEIDVA----------------------------------------- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2250 QSRRQVEEAERlkqlaeeqaqaqaqaqaaaeklrkeaeqeaarraqaEQAALKQKQVADAEMEkhkkfaeqtlRQKAQVE 2329
Cdd:COG4913 665 SAEREIAELEA------------------------------------ELERLDASSDDLAALE----------EQLEELE 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2330 QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEelfsvRVQMEELSKLKARIEAENRALILRD-KDNTQR 2408
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED-----LARLELRALLEERFAAALGDAVERElRENLEE 773
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2409 FLQEEAEKMKQVAEEAARL-----------------SVAAQE--AARLRQLAEEDLAQQRALAEKMLKEKMQ 2461
Cdd:COG4913 774 RIDALRARLNRAEEELERAmrafnrewpaetadldaDLESLPeyLALLDRLEEDGLPEYEERFKELLNENSI 845
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2401-2556 |
6.05e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2401 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRlkaeaellQQQK 2480
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERAR--------QQQE 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2481 ELaQEQARQLQEDKEQMAQQLAQETQGFQRTLE---AERQRQLEMSAEAERLKLRvAEMSRAQARAEEDAQRFRKQAEE 2556
Cdd:pfam15709 427 EF-RRKLQELQRKKQQEEAERAEAEKQRQKELEmqlAEEQKRLMEMAEEERLEYQ-RQKQEAEEKARLEAEERRQKEEE 503
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1923-2089 |
7.43e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1923 RSTSEKSKQRLEAEASRFRELAEEAArlralaEETKRQRQL-AEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALK 2001
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2002 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasenELERQKGLVEDTLRQR--RQVEEEILALKASFE 2079
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 2044209144 2080 KAAAGKAELE 2089
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1447-1640 |
7.57e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1447 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQ- 1525
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1526 -AKAQAEREAEELQRRMQEEVARREE---AAVDAQQQ----KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEE 1597
Cdd:COG3206 263 pVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQiaalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2044209144 1598 IRV---VRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1640
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1942-2177 |
9.30e-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: 51.30 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1942 ELAEEAARLRALAEETKRQRQLAEEdAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRlaedeafQR 2021
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2022 RRLEEQAAQHKADIEERLAQLRKASENE----LERQKGlVEDTLRQRRQVEEEILALKASFEKAAAGKAELElelgRIRS 2097
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPplalLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELA----ALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2098 NAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESA 2177
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1584-1709 |
9.61e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.07 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1584 VEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRAR--------AEEAEAQKRQAQEEAERLRRQVQDEsqrkr 1655
Cdd:COG1193 520 IEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEkeeilekaREEAEEILREARKEAEELIRELREA----- 594
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1656 qaeaelalrvKAEAEAAREKQRALQALEDvRLQAEEAERRLRQAEADRARQVQV 1709
Cdd:COG1193 595 ----------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAKPAKPPEELKV 637
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1506-1600 |
9.90e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.26 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1506 LAEVEAALEKQRQLAEAHAQAKAQAEREAEelqrRMQEEVARREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKARQV 1584
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAE----AQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 2044209144 1585 EAAERSRVRI---EEEIRV 1600
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1514-1734 |
1.00e-05 |
|
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: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1514 EKQRQLAEAHAQaKAQAEREAEELqrrmQEEVARREEAAVDAQQQKRSIQEELQHLRQS-SEAEIQAKARQVEAAERSRV 1592
Cdd:COG3883 20 AKQKELSELQAE-LEAAQAELDAL----QAELEELNEEYNELQAELEALQAEIDKLQAEiAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1593 RIEEEIRVVRL--------------QLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAE 1658
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1659 AELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTA 1734
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1971-2361 |
1.01e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1971 QRAEAERVLAEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasENEL 2050
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2051 ERQKglVEDTLRQRRQVEEEILALKASFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEATRQRQLAaeeeqrrre 2129
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2130 aeervqkslaaEEEAARQRKSALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQE 2208
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2209 LQQTLQQEQsmlerlraeaeaarrAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKlRKEAeq 2288
Cdd:pfam17380 477 LELEKEKRD---------------RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-RREA-- 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 2289 eaarraqaeqaalKQKQVADAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT 2361
Cdd:pfam17380 539 -------------EEERRKQQEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1829-2615 |
1.09e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1829 RQRELAE-----QELEKQRQLAEGTAQQRLVAEQELIRLRAETEQG--EQQRQLL----------EEELARLQREAAAAT 1891
Cdd:TIGR00606 253 RLKEIEHnlskiMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGtdEQLNDLYhnhqrtvrekERELVDCQRELEKLN 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1892 HKRQELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLEAEASRFRELAEEAARLRAlAEETKRQRQlaeEDAAR 1970
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERGPFSERQIKN-FHTLVIERQ---EDEAK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1971 QRAEAERVLAEKLAAISEA------------TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2038
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQadeirdekkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2039 LAQLRKASENELERQKGLVE---DTLRQRRQVEEEILAL------KASFEKAAAGKAELELELGRIRSNAEDTLRSK--- 2106
Cdd:TIGR00606 489 KAEKNSLTETLKKEVKSLQNekaDLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgy 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2107 --EQAELEATRQRQlaAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEarrlrERAEQESARQLQLAQ 2184
Cdd:TIGR00606 569 fpNKKQLEDWLHSK--SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED-----KLFDVCGSQDEESDL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2185 EAAQKRLQAEEKAHAfavqqkeqelqqtlqqeqsMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEE-AERLKQ 2263
Cdd:TIGR00606 642 ERLKEEIEKSSKQRA-------------------MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEfISDLQS 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2264 LAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQA-ALKQKQVADAEmEKHKKFAEQTLRQKAQVEQELTTLRLQLEET 2342
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIiDLKEKEIPELR-NKLQKVNRDIQRLKNDIEEQETLLGTIMPEE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2343 DHQKSILDEE--LQRLKAEVTEAARQRNQVEEELFSVRVQM-------------EELSKLKARIEaENRALIlrdkDNTQ 2407
Cdd:TIGR00606 782 ESAKVCLTDVtiMERFQMELKDVERKIAQQAAKLQGSDLDRtvqqvnqekqekqHELDTVVSKIE-LNRKLI----QDQQ 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2408 RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKaeaELLQQQKEL--AQE 2485
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE---KDQQEKEELisSKE 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2486 QARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEmsaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIG------E 2559
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD-----DYLKQKETELNTVNAQLEECEKHQEKINEDMRlmrqdiD 1008
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2560 KLHRTELATQEKVTLV----HTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQ 2615
Cdd:TIGR00606 1009 TQKIQERWLQDNLTLRkrenELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKR 1068
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1564-1938 |
1.09e-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: 51.43 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1564 EELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1643
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1644 RRQVQDESQRKRQAEAELALRVKA-EAEAAREKQRALQA---LEDVRLQAEEAERRLRQAEADRaRQVQVALETAQ---R 1716
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLEReteLERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1717 SAEVELQSKRASFAEKTAQLERtLQEEhvaVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVA 1796
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-LQDT---ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1797 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLL 1876
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 1877 EEELArlqREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAS 1938
Cdd:pfam07888 345 EVELG---REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4072-4110 |
1.11e-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: 1.11e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 4072 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 4110
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1495-1936 |
1.19e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.45 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1495 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQE-----ELQHL 1569
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEirarlLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1570 RQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1649
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1650 ESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASF 1729
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1730 AEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQ 1809
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1810 KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAA 1889
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2044209144 1890 ATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAE 1936
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4529-4566 |
1.20e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.20e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2044209144 4529 QRFLEAQYLTGGLIEPDVPGRVPLDEALQRGMVDARTA 4566
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2413-2572 |
1.24e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.41 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2413 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARQLQE 2492
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2493 DKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2572
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1661-1909 |
1.26e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1661 LALRVKAEAEAAREKQRALQALEDvRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1740
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1741 QEEHVAVAQLREEAERRAQQQAEAerareeaeqelerWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1820
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1821 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlvaeqeliRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAE 1900
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 2044209144 1901 LAKVRAEME 1909
Cdd:COG4942 229 IARLEAEAA 237
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1623-1798 |
1.32e-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: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1623 RARAEEAEAQ------KRQAQEEAerlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALEDVRLQAEEAER-- 1694
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1695 -RLRQAEADRARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERARE 1769
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKA 490
|
170 180 190
....*....|....*....|....*....|....
gi 2044209144 1770 EAEQelERWRLKANEALRLRL-----QAEEVAQQ 1798
Cdd:pfam15709 491 RLEA--EERRQKEEEAARLALeeamkQAQEQARQ 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2302-2511 |
1.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2302 KQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRNQVEEELFSVRV 2379
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2380 QMEELSKLKARIEAENRaLILRDKD--NTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2456
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKaELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 2457 KEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRT 2511
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
301-408 |
1.52e-05 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 47.11 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 301 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHRPMLI-DMSKVYRQTNLENLDQAFSVAERDLGV 379
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 2044209144 380 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 408
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2312-2756 |
1.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2312 EKHKKFAEQTlRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQM----- 2381
Cdd:COG4913 259 ELAERYAAAR-ERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgngg 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2382 EELSKLKARIEAENRALilRDKDNTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2460
Cdd:COG4913 338 DRLEQLEREIERLEREL--EERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2461 QAVQEATRLKAE-AELLQQQKELAQEQarqlqedkEQMAQQLAQETQGFQRTLE--------AERQRQLEMSAEA----E 2527
Cdd:COG4913 416 DLRRELRELEAEiASLERRKSNIPARL--------LALRDALAEALGLDEAELPfvgelievRPEEERWRGAIERvlggF 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2528 RLKLRVAEMSRAQARAEEDAQRFRK--QAEEIGEKLHRTELATQEKVTLVHTLEIQ------------RQQSDH----DA 2589
Cdd:COG4913 488 ALTLLVPPEHYAAALRWVNRLHLRGrlVYERVRTGLPDPERPRLDPDSLAGKLDFKphpfrawleaelGRRFDYvcvdSP 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2590 ERLR--------------------------------------AAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQE 2631
Cdd:COG4913 568 EELRrhpraitragqvkgngtrhekddrrrirsryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2632 T--RALQESFLSEKDrLLQRERFIEQEKAKLEQLFR--DEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAE 2707
Cdd:COG4913 648 EalQRLAEYSWDEID-VASAEREIAELEAELERLDAssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2044209144 2708 EGVRRKQEELQLLEQQRQQQERLLAEEnQRLRERLQRLEEEHRAALAHS 2756
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEER 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2415-2752 |
1.75e-05 |
|
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: 51.22 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2415 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARQLQED 2493
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2494 keqmAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2573
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2574 LVHTLEIQRQQSDHDAERLRAAIAELEREkekLQEEATLLQQKSEEMQVVQQEQLLQETRALQES--FLSEKDRLLQRER 2651
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDkeFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2652 FIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQqmeqereqLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLL 2731
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELAD--------LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340
....*....|....*....|....
gi 2044209144 2732 AEENQ---RLRERLQRLEEEHRAA 2752
Cdd:TIGR02169 465 SKYEQelyDLKEEYDRVEKELSKL 488
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1454-1665 |
1.86e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1454 ESVIQEYVD--LRTRYSElttlTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ---RQLAEAHAQ-AK 1527
Cdd:COG3206 155 NALAEAYLEqnLELRREE----ARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKlllQQLSELESQlAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1528 AQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSsEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEA 1607
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1608 -TERQRGGAEGELQALRARAEEAEAQKRQAQEEA----------ERLRRQVQ-------DESQRKRQAEAELALRV 1665
Cdd:COG3206 310 eAQRILASLEAELEALQAREASLQAQLAQLEARLaelpeleaelRRLEREVEvarelyeSLLQRLEEARLAEALTV 385
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1938-2195 |
1.99e-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: 50.66 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1938 SRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 2017
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2018 AFQRRRLEEQAAQHKADIEE------RLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELE 2091
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2092 LGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRreaeervqkslaAEEEAARQRKSALEevERLKAKVEEARRLRER 2171
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE------------AENEALLEELRSLQ--ERLNASERKVEGLGEE 259
|
250 260
....*....|....*....|....
gi 2044209144 2172 AEQESARQLQLAQEAAQKRLQAEE 2195
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQARLQAAQ 283
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2327-2620 |
2.03e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.91 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2327 QVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEaENRALILRDKDNT 2406
Cdd:pfam07111 335 QLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAE-EQLKFVVNAMSST 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2407 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK-----------------EKMQAVQEATRL 2469
Cdd:pfam07111 414 QIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEscpppppappvdadlslELEQLREERNRL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2470 KAE----AELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRT-------LEAERQRQLEMSAEAERLKLRVAEMSR 2538
Cdd:pfam07111 494 DAElqlsAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlasvgqqLEVARQGQQESTEEAASLRQELTQQQE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2539 A-----QARAEEDAQRFRKQAEEIGEKLHRTEL---------------ATQEKVTLVHTLEIQRQQSDHDAERLRAAIAE 2598
Cdd:pfam07111 574 IygqalQEKVAEVETRLREQLSDTKRRLNEARReqakavvslrqiqhrATQEKERNQELRRLQDEARKEEGQRLARRVQE 653
|
330 340
....*....|....*....|....*.
gi 2044209144 2599 LEREKE----KLQEEATLLQQKSEEM 2620
Cdd:pfam07111 654 LERDKNlmlaTLQQEGLLSRYKQQRL 679
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1836-1993 |
2.07e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.17 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1836 QELEKQRQLA--------EGTAQQrlVAEqelirLRAETEQGEQQRQLLEEELarlqrEAAAATHKRQELEAELAKVRAe 1907
Cdd:PTZ00491 647 DSLQKSVQLAieittksqEAAARH--QAE-----LLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1908 mevllASKARAEEESRSTSEKSKQRLEAEASRFRelaEEAARLRALAE-ETKRQRQLAEEDAARQRAEAERVLAEKLAAI 1986
Cdd:PTZ00491 714 -----SGQSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI 785
|
....*..
gi 2044209144 1987 sEATRLK 1993
Cdd:PTZ00491 786 -EATKFE 791
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2405-2872 |
2.17e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 50.74 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2405 NTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2484
Cdd:COG4995 7 LALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2485 EQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2564
Cdd:COG4995 87 LALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2565 ELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRALQESFLSEKD 2644
Cdd:COG4995 167 ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2645 RLLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQEELQLLEQQR 2724
Cdd:COG4995 247 AAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2725 QQQERLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQAAASkalpngrdvldgpAAEAEPEHAFDGLRRKVPAQRLQE 2804
Cdd:COG4995 327 LAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLL-------------LLAALLALLLEALLLLLLALLAAL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2805 VGILSAEELQRLAQGRTTVAELAQREDVRQYLQGRSGIAGLLLKP--ANEKLSIYAALRRQLLSPGTALI 2872
Cdd:COG4995 394 LLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1547-1900 |
2.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1547 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1626
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1627 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQ 1706
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1707 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEAL 1786
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1787 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAET 1866
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 2044209144 1867 EQGEQQRQLLEEELARLQREAAAATHKRQELEAE 1900
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2304-2506 |
2.20e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.37 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2304 KQVADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDHQksildeelqrlkAEVTEAARQRNQVEEELF 2375
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2376 SVRVqmeELSKLKARIEA----------------ENRALILRDK-----DNTQRFLQEEAEKMKQ--------VAEEAAR 2426
Cdd:NF012221 1617 AVTK---ELTTLAQGLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2427 LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQ 2506
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1491-1719 |
2.22e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1491 EERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELqhlr 1570
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1571 qsSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1650
Cdd:PRK07735 86 --TEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1651 SQRKRQAEAelalrVKAEAeAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAE 1719
Cdd:PRK07735 164 KAKAKAAAA-----AKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQG 226
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1495-1656 |
2.37e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 50.67 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1495 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1574
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1575 AEIQAKARQVEAAERSRVRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDESQRK 1654
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 2044209144 1655 RQ 1656
Cdd:PRK12678 216 EE 217
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3867-3900 |
2.46e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.46e-05
10 20 30
....*....|....*....|....*....|....
gi 2044209144 3867 LLEAQAATGFLLEPVKGERLTVDEAVRKGLVGPE 3900
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1470-1709 |
2.50e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1470 LTTLTSQYIKFIREtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAEELQRrMQEEVAR 1547
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1548 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRggAEGELQALRAR-A 1626
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1627 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEaAREKQRALQALEDVRLQAEEAERRLRQAEADRARQ 1706
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
...
gi 2044209144 1707 VQV 1709
Cdd:COG3206 388 VRV 390
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1478-1718 |
2.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1478 IKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQ 1557
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1558 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALR-------AraeEAE 1630
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1631 AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVA 1710
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....*...
gi 2044209144 1711 LETAQRSA 1718
Cdd:COG3883 255 AGAAAGSA 262
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1520-1735 |
2.75e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1520 AEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrvRIEEEIR 1599
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1600 VVRLQLEATERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDESQRKRQAEA 1659
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1660 ELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1735
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1821-1943 |
2.83e-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: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1821 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATHKR 1894
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1895 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEASRFREL 1943
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1968-2199 |
2.88e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1968 AARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE 2047
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2048 NELERQKGLVEDTL----RQRRQVEEEILALKASFEKAAAGKAELElELGRIRSNAEDTLRsKEQAELEATRQRQLAAee 2123
Cdd:COG4942 97 AELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELR-ADLAELAALRAELEAE-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 2124 eqrrreaeervQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2199
Cdd:COG4942 173 -----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1822-2038 |
2.88e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlvAEQELIRLRAETEQGEQQRQLLEEElarlqreAAAATHkrqe 1896
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE-------SRAVTK---- 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1897 leaELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEASRF----RELAEEAARLRAL 1953
Cdd:NF012221 1621 ---ELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1954 AEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 2033
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDES 1777
|
....*
gi 2044209144 2034 DIEER 2038
Cdd:NF012221 1778 DKPNR 1782
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3941-3977 |
3.11e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.11e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 3941 LRLLDAQLATGGIVDPHLGFHLPLEVAYQRGYLNKDT 3977
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3494-3529 |
3.57e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.57e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2044209144 3494 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3529
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3494-3532 |
3.64e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.47 E-value: 3.64e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3494 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3532
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2407-2707 |
3.68e-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: 49.53 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2407 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2486
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2487 ARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2566
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2567 ATQEKvtlvhtleIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMqvvqqeqllqetraLQESFLSEKDRL 2646
Cdd:pfam13868 191 AQQEK--------AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQE--------------LQQAREEQIELK 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2647 LQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAE 2707
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAE 309
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2310-2747 |
3.85e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2310 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRNQVEEELFSVRVQMEE 2383
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2384 LSKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2461
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2462 AVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2536
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2537 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEeatll 2613
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK----- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2614 qqkseemqvvqqeqllqeTRALQESFLSEkdrlLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLV 2693
Cdd:PRK03918 537 ------------------LKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2694 ASMEEARQRQ---REAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRERLQRLEE 2747
Cdd:PRK03918 595 KELEPFYNEYlelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4419-4452 |
3.86e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.86e-05
10 20 30
....*....|....*....|....*....|....
gi 2044209144 4419 EETGPVAGILDTETLEKVSITEAMRRNLVDNITG 4452
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1371-1690 |
3.95e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1371 KQRQERIQAVPLANSQAVREQLQQEKELLEEIErygekvdECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ 1450
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERK-------GSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1451 SGSESVIQEYVDLRTRYSELTTLTSQYikfiRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA 1530
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQE----QDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1531 ereaeelqrrMQEEVARReEAAVDaqqqkrsiQEELQHLRQSSEAEIqakAR-QVEAAERSRVRIEEEIRVVRLQLEaTE 1609
Cdd:PRK10929 178 ----------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQALRNQLN-SQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1610 RQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL---ALRVKAEA----EAAREKQRALQAL 1682
Cdd:PRK10929 235 RQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQAL 302
|
....*...
gi 2044209144 1683 EDVRLQAE 1690
Cdd:PRK10929 303 NTLREQSQ 310
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4280-4308 |
4.05e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.05e-05
10 20
....*....|....*....|....*....
gi 2044209144 4280 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4308
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2321-2553 |
4.18e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.07 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2321 TLRQKAQVEQELTTLRLQleetdhQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALIL 2400
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2401 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2474
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2475 LLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2553
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2330-2662 |
4.25e-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: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2330 QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKL--KARIEAENRALILRDK---- 2403
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAAlrEAEAAKEELRIELRDKtaqa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2404 DNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLA---QQRALAEkmlkekmqavQEATRLKAEAEllQQQK 2480
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELAtarERLALLE----------QENRRLQALSE--EQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2481 ELAqEQARQLQEDKEQMAQQLAQ--ETQGFQRTLEAERQR---QLEMSAEAERLKLRVAEM--SRAQARAE-------ED 2546
Cdd:pfam19220 189 ELA-ELTRRLAELETQLDATRARlrALEGQLAAEQAERERaeaQLEEAVEAHRAERASLRMklEALTARAAateqllaEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2547 AQRFRKQAEEIGEKLHRTELATQEKVTLVHTLEiqrqQSDHDAERLRAAIAELEREKEKLQEEATLLQQkseemqvVQQE 2626
Cdd:pfam19220 268 RNQLRDRDEAIRAAERRLKEASIERDTLERRLA----GLEADLERRTQQFQEMQRARAELEERAEMLTK-------ALAA 336
|
330 340 350
....*....|....*....|....*....|....*.
gi 2044209144 2627 QLLQETRALqESFLSEKDRLLQRERFIEQEKAKLEQ 2662
Cdd:pfam19220 337 KDAALERAE-ERIASLSDRIAELTKRFEVERAALEQ 371
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2422-2758 |
4.30e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2422 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQL 2501
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2502 AQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVH 2576
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2577 TLEIQRQQSDHdAERLRAAIAELEREKeKLQEEATLLQQKSEEMQVVQQEQLLQETRALQESFLSEKDRLLQRERFIEQE 2656
Cdd:pfam02463 319 SEKEKKKAEKE-LKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2657 KAKLEQLFRdEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQ 2736
Cdd:pfam02463 397 LELKSEEEK-EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|..
gi 2044209144 2737 RLRERLQRLEEEHRAALAHSEE 2758
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEE 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1572-1785 |
4.32e-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: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1572 SSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1649
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1650 -ESQRKRQAEAELAL------------RVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADrARQVQVALETAQR 1716
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1717 saevELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEA 1785
Cdd:COG3883 172 ----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2365-2509 |
4.50e-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: 48.73 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2365 RQRNQVEEELFSV---RVQMEE-LSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQL 2440
Cdd:cd16269 149 EDREKLVEKYRQVprkGVKAEEvLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----REL 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2441 AEEDLAQQRALAE--KMLKEKMQavQEATRLKAEAELLQQQKElaQEQARQLQEDKEQMAQQLAQETQGFQ 2509
Cdd:cd16269 225 EQKLEDQERSYEEhlRQLKEKME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1825-2106 |
4.60e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKV 1904
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1905 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLA 1984
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1985 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQR 2064
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2044209144 2065 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSK 2106
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1547-1686 |
4.76e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.89 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1547 RREEAAVD-AQQQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRVRIEEEI-RVVRLQleateRQRGGAEGELQAL 1622
Cdd:COG1566 79 TDLQAALAqAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEA 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1623 RARAEEAEAQKRQAQEEAERLRRQVQDESQrKRQAEAELalrvkAEAEAAREKQRALQALEDVR 1686
Cdd:COG1566 154 RAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQAELNLARTTIR 211
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1964-2617 |
5.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1964 AEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRRLEEQAAQHKADIEERLAQLR 2043
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2044 KASENELERQKGLVEDT--LRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAA 2121
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2122 EEEQrrreaeerVQKSLAAEEEAArqrksalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2201
Cdd:PRK03918 346 KLKE--------LEKRLEELEERH-------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2202 VQQKEQELQQTLQQEQSMLERLRAEAEAARraaeeaeeareraereaaqSRRQVEEAERLKQLAEEQAqaqaqaqaaaeK 2281
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKCPV-------------------CGRELTEEHRKELLEEYTA-----------E 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2282 LRKEAeqeaarraqaeqaalKQKQVADAEMEKHKKFAEQtLRQKAQVEQELTTLRL---QLEETDHQ-KSILDEELQRLK 2357
Cdd:PRK03918 461 LKRIE---------------KELKEIEEKERKLRKELRE-LEKVLKKESELIKLKElaeQLKELEEKlKKYNLEELEKKA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2358 AEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALilrdkdntqRFLQEEAEKMKQVAEEAARLSVAAQEA--A 2435
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL---------DELEEELAELLKELEELGFESVEELEErlK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2436 RLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELaqeqaRQLQEDKEQMAQQLAQETQgfqrtlEAE 2515
Cdd:PRK03918 596 ELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL-----EELRKELEELEKKYSEEEY------EEL 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2516 RQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKlhRTELatqekvtlvhtleiqrqqsdhdaERLRAA 2595
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA--KKEL-----------------------EKLEKA 719
|
650 660
....*....|....*....|..
gi 2044209144 2596 IAELEREKEKLQEEATLLQQKS 2617
Cdd:PRK03918 720 LERVEELREKVKKYKALLKERA 741
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1870-2748 |
5.23e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1870 EQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEAEASRFRE------- 1942
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-KNALQEQLQAETELCAEAEEMRARLAARKQELEEilheles 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1943 -LAEEAARLRALAEETKR--------QRQLAEEDAARQRAEAERVLAE-KLAAISEATRLKTEAEIAL-KEKEAENERLR 2011
Cdd:pfam01576 83 rLEEEEERSQQLQNEKKKmqqhiqdlEEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2012 RLA------EDEAFQRRRLEEQAAQHKADIEERLAQLRK-------------ASENELERQ----KGLVEDTLRQRRQVE 2068
Cdd:pfam01576 163 EFTsnlaeeEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqelekakrkleGESTDLQEQiaelQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2069 EEILALKASFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2145
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2146 RQRKsalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRA 2225
Cdd:pfam01576 323 SKRE---QEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2226 EAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEaeqeaarraqaeqaalkQKQ 2305
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL-----------------SKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2306 VADAEMEKH--KKFAEQTLRQK-------AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQrnqVEEELFS 2376
Cdd:pfam01576 463 VSSLESQLQdtQELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDAGT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2377 VrvqmEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQeaaRLRQLAEEDLAQQRALAEKML 2456
Cdd:pfam01576 540 L----EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTK-NRLQQELDDLLVDLD---HQRQLVSNLEKKQKKFDQMLA 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2457 KEKMQAVQEA-TRLKAEAELLQQQKElAQEQARQLQEdkeqmAQQLAQETQGFQRTLEAERQrqlEMSAEAERLKLRVAE 2535
Cdd:pfam01576 612 EEKAISARYAeERDRAEAEAREKETR-ALSLARALEE-----ALEAKEELERTNKQLRAEME---DLVSSKDDVGKNVHE 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2536 MSRAQARAEEDAQRFRKQAEEIGEKLHRTELAtqeKVTLVHTLEIQRQQSDHDaerlraaiaeLEREKEKLQEEATLLQQ 2615
Cdd:pfam01576 683 LERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQFERD----------LQARDEQGEEKRRQLVK 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2616 KSEEMQVVQQEQLLQETRALQESFLSEKDrLLQRERFIEQEKAKLEQLFRdEVAKAQKLREEQQRQQQQMEQEREQLVAS 2695
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELD-LKELEAQIDAANKGREEAVK-QLKKLQAQMKDLQRELEEARASRDEILAQ 827
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2696 MEEARQRQREAEEGVRRKQEELQLLEQQRQQQER-----------------LLAEENQRLRERLQRLEEE 2748
Cdd:pfam01576 828 SKESEKKLKNLEAELLQLQEDLAASERARRQAQQerdeladeiasgasgksALQDEKRRLEARIAQLEEE 897
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1246-1962 |
5.37e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1246 EEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRVQAEAqqpvfdaLRDELRGAQEVGERLQRQHGERDVEVERW-RER 1324
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1325 VAPLLERWQAALAQTDVRQRELEQLGRQLRYYRESadplgawlqDAKQRQERIQAVPLANSQ--AVREQLQQEKELLEEI 1402
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAG---------EAKQLAEAQKEAELLRKQlsKTQEELEAQVTLVESL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1403 ERY-GEKV------DECQQLAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTS 1475
Cdd:pfam07111 224 RKYvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1476 QYIKFIRETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAEeLQRRMQEEVARREEAAVD 1554
Cdd:pfam07111 299 EFPKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDKAAEVEVERMS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1555 AqqqkRSIQEELQHlrqsseaeiqakarqveaAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQkr 1634
Cdd:pfam07111 375 A----KGLQMELSR------------------AQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVAR-- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1635 qAQEEAERLRRQVQDESQRKRQAEAELAL-RVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEAD-RARQVQVALE 1712
Cdd:pfam07111 431 -IPSLSNRLSYAVRKVHTIKGLMARKVALaQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQlSAHLIQQEVG 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1713 TAQRSAEVElqskRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRlrlqa 1792
Cdd:pfam07111 510 RAREQGEAE----RQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQ----- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1793 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlvaEQELIRLRAETEQGEQQ 1872
Cdd:pfam07111 581 EKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEAR---KEEGQRLARRVQELERD 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1873 RQLLeeeLARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRLEAEASRFRELAEEA 1947
Cdd:pfam07111 658 KNLM---LATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSLTVLLDNLQGLSEAI 734
|
730
....*....|....*
gi 2044209144 1948 ARLRALAEETKRQRQ 1962
Cdd:pfam07111 735 SREEAVCQEDNQDTC 749
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2329-2558 |
5.47e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2329 EQELTTLRLQLEE----TDHQKSILDEELQRLKAEVTEAARQR-----NQVEEELFSVRVQMEELSKLKARI-EAENRal 2398
Cdd:COG3096 450 EQQATEEVLELEQklsvADAARRQFEKAYELVCKIAGEVERSQawqtaRELLRRYRSQQALAQRLQQLRAQLaELEQR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2399 iLRDKDNTQRFLQEEAEKMKQVAEEAARLsvaaqeaarlrqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2478
Cdd:COG3096 528 -LRQQQNAERLLEEFCQRIGQQLDAAEEL--------------EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2479 Q-KEL---------AQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQ 2548
Cdd:COG3096 593 RiKELaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
250
....*....|
gi 2044209144 2549 RFRKQAEEIG 2558
Cdd:COG3096 673 RLLALAERLG 682
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
183-287 |
5.72e-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: 45.72 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 183 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHR 260
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAK 84
|
90 100
....*....|....*....|....*..
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1965-2618 |
6.01e-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: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1965 EEDAARQRAEAERVLAEKLAAISEaTRLKTEAEIALKEKEaenerlrrLAEDEAFQRRRLEEQAAQhKADIEERLAQLRK 2044
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFN-TLESAELRLSHLHFG--------YKSDETLIASRQEERQET-SAELNQLLRTLDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2045 asenelerQKGLVEDTLRQRrqveeeilaLKASFEKAAAGKAELELelgrirsnAEDTLRSKEQAELEatrQRQLAAEEE 2124
Cdd:pfam12128 298 --------QWKEKRDELNGE---------LSAADAAVAKDRSELEA--------LEDQHGAFLDADIE---TAAADQEQL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2125 QRRREAEERVQKSLAAEEEAARqrkSALEEVERLKAKV-EEARRLRERAEQESArqlqlAQEAAQKRLQAEEKAHafaVQ 2203
Cdd:pfam12128 350 PSWQSELENLEERLKALTGKHQ---DVTAKYNRRRSKIkEQNNRDIAGIKDKLA-----KIREARDRQLAVAEDD---LQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2204 QKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLR 2283
Cdd:pfam12128 419 ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2284 KEAEQEAARRAQAEQAALKQKQVADAemekhkkfAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQR--LKAEVT 2361
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDE--------LELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRtdLDPEVW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2362 EAARQRnqvEEELFSVRVQMEEL---------SKLKARIEAENRALilrdkdNTQRFLQEEAEK-MKQVAEEAARLSVAA 2431
Cdd:pfam12128 571 DGSVGG---ELNLYGVKLDLKRIdvpewaaseEELRERLDKAEEAL------QSAREKQAAAEEqLVQANGELEKASREE 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2432 QEAARLRQLAEEDLAQ------------QRALAEkmlkEKMQAVQEATRLKAEAELL-QQQKELAQEQARQLQEDKEQMA 2498
Cdd:pfam12128 642 TFARTALKNARLDLRRlfdekqsekdkkNKALAE----RKDSANERLNSLEAQLKQLdKKHQAWLEEQKEQKREARTEKQ 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2499 QQLaqetqgfqRTLEAERQRQL---------EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgEKLHRT----- 2564
Cdd:pfam12128 718 AYW--------QVVEGALDAQLallkaaiaaRRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI-RTLERKieria 788
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2565 ---ELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSE 2618
Cdd:pfam12128 789 vrrQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE 845
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1168-1697 |
6.84e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.35 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1168 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRSTQGAEE 1247
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1248 VLRAHEEQLKEAQAVPATLPELEATKAALkklrvQAEAQQpVFDALRDELRGAQEVGERLQRQHGERDVEVERWRERVAP 1327
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1328 LLERWQAA---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLQDAKQRQERIqavplansqavrEQLQQEKE-LLE 1400
Cdd:pfam05557 144 LKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI------------PELEKELErLRE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1401 EIERYGEKVDECQQLAKQyinaIKDYELQLVTY-KAQLEPVASPAKKPKVQS---GSESVIQEY-------VDLRTRYSE 1469
Cdd:pfam05557 212 HNKHLNENIENKLLLKEE----VEDLKRKLEREeKYREEAATLELEKEKLEQelqSWVKLAQDTglnlrspEDLSRRIEQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1470 L-----------TTLTSQyIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL------------------ 1519
Cdd:pfam05557 288 LqqreivlkeenSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgyrailesyd 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1520 ----AEAHAQAKAQAEREAEELQRRMQ---EEVARR----EEAAVDAQQQKRSIQEELQHLRQ--------SSEAEIQAK 1580
Cdd:pfam05557 367 keltMSNYSPQLLERIEEAEDMTQKMQahnEEMEAQlsvaEEELGGYKQQAQTLERELQALRQqesladpsYSKEEVDSL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1581 ARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DESQRKRQAE 1658
Cdd:pfam05557 447 RRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKRLLKKLEDD 526
|
570 580 590
....*....|....*....|....*....|....*....
gi 2044209144 1659 AELALRVKAEAEAAREKQralqaLEDVRLQAEEAERRLR 1697
Cdd:pfam05557 527 LEQVLRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2340-2620 |
7.26e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2340 EETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDntqrfLQEEAEKMKQ 2419
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS-----KRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2420 VAEeaarlsvaaqeaaRLRQLAEEdlaqqralaEKMLKEKmqaVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQ 2499
Cdd:PRK03918 264 LEE-------------RIEELKKE---------IEELEEK---VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2500 qLAQETQGFQRTL-EAErqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFrkqaEEIGEKLHRTElatqekvtlvhtl 2578
Cdd:PRK03918 319 -LEEEINGIEERIkELE-----EKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELE------------- 375
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2044209144 2579 EIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEM 2620
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2363-2553 |
7.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2363 AARQRNQVEEELFSVRVQMEELSKLKARIEAENRAliLRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQlAE 2442
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDA--LQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDA-SS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2443 EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQG-----FQRTLEAERQ 2517
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlleerFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|....*.
gi 2044209144 2518 RQLEMSAEAERLKLRvAEMSRAQARAEEDAQRFRKQ 2553
Cdd:COG4913 765 RELRENLEERIDALR-ARLNRAEEELERAMRAFNRE 799
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2353-2566 |
7.40e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2353 LQRLKAEVTEAARQRNQVEEElfsvrvQMEELSKLKARIEAENRALilrdkdnTQRFLQEEAEKmKQvAEEAARLSVAAQ 2432
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL-------EKERLAAQEQK-KQ-AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2433 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAEllQQQKELAQEQARQLQEDKEQM---AQQLAQETQGFQ 2509
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAE--AKKKAEAEAAKKAAAEAKKKAeaeAAAKAAAEAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2510 RTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2566
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1822-2037 |
8.32e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.79 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEE--------QAVRQRELAEQElEKQRQLAEGTAQQRLVAEQE-LIRLRAETEQGEQQRQLLEEEL--------ARLQ 1884
Cdd:PRK05035 447 KAEEakarfearQARLEREKAARE-ARHKKAAEARAAKDKDAVAAaLARVKAKKAAATQPIVIKAGARpdnsaviaAREA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1885 REAAAATHKRQELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAsrfrelaeeAARLRALAEetKR 1959
Cdd:PRK05035 526 RKAQARARQAEKQAAAaadpkKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKAK--KA 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1960 QRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 2037
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1402-1742 |
8.37e-05 |
|
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: 48.80 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1402 IERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAK-KPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF 1480
Cdd:COG5185 154 GEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKaEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 IRETLRRMEEEERLAEQQrAEERERLAEVEAAL---------EKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEA 1551
Cdd:COG5185 234 ALKGFQDPESELEDLAQT-SDKLEKLVEQNTDLrleklgenaESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1552 AVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAE---GELQALRARAEE 1628
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEeldSFKDTIESTKES 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1629 AEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEdvrlqaEEAERRLRQAEADrarqVQ 1708
Cdd:COG5185 393 LDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELI------SELNKVMREADEE----SQ 462
|
330 340 350
....*....|....*....|....*....|....
gi 2044209144 1709 VALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1742
Cdd:COG5185 463 SRLEEAYDEINRSVRSKKEDLNEELTQIESRVST 496
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1856-2039 |
8.51e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1856 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSeKSKQrlea 1935
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1936 easrfrelaeeaarLRALAEEtkrqrqlaEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE-----NERL 2010
Cdd:COG1579 91 --------------YEALQKE--------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekkAELD 148
|
170 180
....*....|....*....|....*....
gi 2044209144 2011 RRLAEDEAfQRRRLEEQAAQHKADIEERL 2039
Cdd:COG1579 149 EELAELEA-ELEELEAEREELAAKIPPEL 176
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1567-1855 |
8.61e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.79 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1567 QHLRQSsEAEIQAKARQVEAAERSRVRIEEeirvvrlqleateRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1646
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1647 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVEL---- 1722
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiar 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1723 -QSKRASFAEKTAQLERTLQEEHVAVAQlREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSL 1801
Cdd:PRK05035 557 aKAKKAAQQAANAEAEEEVDPKKAAVAA-AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANA 635
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1802 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVA 1855
Cdd:PRK05035 636 EPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2472-2758 |
9.04e-05 |
|
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: 48.97 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2472 EAELLQQQKELAQEQA----RQLQEDKEQMAQQ-LAQETQGFQRtlEAERQRQLEMS-----AEAERLKLRVAEMSRAQA 2541
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQErLRQEKEEKAR--EVERRRKLEEAekarqAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2542 RAEEDAQRFRKQAEEI-GEKLHRTELATQ-EKVTLVHTLEIQRQQSDhdaERLRAAIAELEREKEKLQEEATLLQQKSEE 2619
Cdd:pfam17380 345 ERERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2620 MQVvqqeqllqeTRALQESFLSEKDRLLQRERFIEQEKAKLEQLfrdevakaqklreeqqRQQQQMEQEREQLVASMEEA 2699
Cdd:pfam17380 422 MEQ---------IRAEQEEARQREVRRLEEERAREMERVRLEEQ----------------ERQQQVERLRQQEEERKRKK 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2700 RQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEEnQRLRERLQRLEEEHRAALAHSEE 2758
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE-ERKRKLLEKEMEERQKAIYEEER 534
|
|
| 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 2044209144 186 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDY 256
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNS 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2044209144 257 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 298
Cdd:cd21323 104 ASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3828-3864 |
9.16e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 9.16e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 3828 RYLYGTGCVAGVYLPGSRQTLTIYQALKKGLLNAEVA 3864
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1823-2091 |
9.17e-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: 48.53 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1823 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLV-------------AEQELIRLRAETEQGEQQRQLLEEELARLQR---- 1885
Cdd:pfam19220 106 KEELRIELRDKTAQAEALERQLAAETEQNRALeeenkalreeaqaAEKALQRAEGELATARERLALLEQENRRLQAlsee 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1886 ---EAAAATHKRQELEAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEASRFR-ELAEEAARLRALAEETKRQR 1961
Cdd:pfam19220 186 qaaELAELTRRLAELETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1962 QLAEEDAARQRaeaervlaEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQ 2041
Cdd:pfam19220 262 QLLAEARNQLR--------DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEM 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 2042 LRKA---SENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAG-KAELELE 2091
Cdd:pfam19220 330 LTKAlaaKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRlKEELQRE 383
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1483-1650 |
9.44e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1483 ETLRRMEEEERLAEQQRA---EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEevarreeaavdaqqQK 1559
Cdd:PRK00409 492 EIAKRLGLPENIIEEAKKligEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE--------------KK 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1560 RSIQEELQHLRQssEAEIQAKARqVEAAERSRVRIEEEIRVVRlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1639
Cdd:PRK00409 558 EKLQEEEDKLLE--EAEKEAQQA-IKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
170
....*....|.
gi 2044209144 1640 AERLrrQVQDE 1650
Cdd:PRK00409 634 QEEL--KVGDE 642
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3275-3311 |
9.62e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 9.62e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 3275 LRLLDAQLSTGGIVDPSKSHRVPMDVAYARGYLDQET 3311
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1539-1702 |
9.79e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.33 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1539 RRMQEEVARREEAAVDAQQQKRSIQEElQHLRQSSEAEIQAKaRQVEAAERSRVriEEEIRVVRlqleaterqrggAEGE 1618
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQE-REIETARIAEA--EAELAKKK------------AEER 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1619 LQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElalrvKAEAEAAREKQRAlqaleDVRLQAEeAERRLRQ 1698
Cdd:COG2268 255 REAETARAE-AEAAYEIAEANAEREVQRQLEIAEREREIELQ-----EKEAEREEAELEA-----DVRKPAE-AEKQAAE 322
|
....
gi 2044209144 1699 AEAD 1702
Cdd:COG2268 323 AEAE 326
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1825-2020 |
9.89e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEgTAQQRLVA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEASRFRELAEEAARLRALAEETKRQRQLAEE 1966
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 1967 DAARQRAEAERVLAEKLAAIS-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 2020
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2252-2609 |
1.02e-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: 48.35 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2252 RRQVEEAERlkqlaeeqaqaqaqaqaaaeklrkeaeQEAARRAQAEQAALKQKQVADAEMEKHKKFAeQTLRQKAQVEQE 2331
Cdd:pfam07888 79 ESRVAELKE---------------------------ELRQSREKHEELEEKYKELSASSEELSEEKD-ALLAQRAAHEAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2332 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRAL--ILRDKDNTQRF 2409
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2410 LQEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ--- 2484
Cdd:pfam07888 211 LQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltl 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2485 ---EQARQLQEDKEQMaqqlAQETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrkqaeeigEKL 2561
Cdd:pfam07888 287 qlaDASLALREGRARW----AQERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER---------EKL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2044209144 2562 hRTELATQEKVTLVhtleiQRQQSDHDAERLRAAIAELEREKEKLQEE 2609
Cdd:pfam07888 345 -EVELGREKDCNRV-----QLSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3238-3274 |
1.11e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 3238 KLLSAEKAVTGYKDPYSGQSVSLFQALKKGLIPREQG 3274
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1341-1706 |
1.14e-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: 48.81 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1341 VRQRELEQLGRQLRYYRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQ-- 1418
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQea 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1419 YINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYvDLRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQ 1498
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK-EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1499 RAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVAR-REEAAVDAQQQKRSIQEELQHLRQSSEAEI 1577
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERlEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1578 QAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAErLRRQVQDESQRKRQA 1657
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEN-NKEEEEERNKRLLLA 968
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2044209144 1658 EAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQ 1706
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1821-2002 |
1.15e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1821 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVA--EQELIRLRAETEQGEQQRQLLEEELARLQREAaaathkrQELE 1898
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEERELTeeEEEIRRLEEQVERLEAEVEELEAELEEKDERI-------ERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1899 AELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEASRF-RELAEEAARLRALAEETKRQRQLAEEDaarqrAEAER 1977
Cdd:COG2433 448 RELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGEL 510
|
170 180
....*....|....*....|....*
gi 2044209144 1978 VLAEKLAAISEATRLKTEAEIALKE 2002
Cdd:COG2433 511 VPVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2411-2583 |
1.15e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2411 QEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR-LKAEAELLQQQKELAQEQARQ 2489
Cdd:TIGR02794 75 QQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAkAKAEAEAERKAKEEAAKQAEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2490 LQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRV-AEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAT 2568
Cdd:TIGR02794 155 EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAeAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAEL 234
|
170
....*....|....*
gi 2044209144 2569 QEKVTLVHTLEIQRQ 2583
Cdd:TIGR02794 235 GDIFGLASGSNAEKQ 249
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1486-1674 |
1.17e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAE----REAEELQRRMQEEVARreEAAVDAQQQKRS 1561
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEerqrQEEEERKQRLQLQAAQ--ERARQQQEEFRR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1562 IQEELQHLRQSSEAEiqakarqvEAAERSRVRIEEEIRVvrlqleaterqrgGAEGELQALRARAEEAEAQKRQaqEEAE 1641
Cdd:pfam15709 431 KLQELQRKKQQEEAE--------RAEAEKQRQKELEMQL-------------AEEQKRLMEMAEEERLEYQRQK--QEAE 487
|
170 180 190
....*....|....*....|....*....|....*
gi 2044209144 1642 RLRRQVQDESQRKRQAEAELALR--VKAEAEAARE 1674
Cdd:pfam15709 488 EKARLEAEERRQKEEEAARLALEeaMKQAQEQARQ 522
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
186-299 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 186 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIAL 254
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2044209144 255 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 299
Cdd:cd21325 102 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1682-2148 |
1.22e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 48.48 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1682 LEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEvelqskRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQ 1761
Cdd:COG3903 470 LETVREYAAERLAEAGERAAARRRHADYYLALAERAAA------ELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAEL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1762 AEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1841
Cdd:COG3903 544 ALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAAL 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1842 RQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEE 1921
Cdd:COG3903 624 LLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1922 SRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALK 2001
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2002 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKA 2081
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2082 AAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQR 2148
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAA 930
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4110-4144 |
1.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.22e-04
10 20 30
....*....|....*....|....*....|....*
gi 2044209144 4110 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4144
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2325-2750 |
1.33e-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: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2325 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaevtEAARQRNQVEEELFSVRVQMEELSKLKARIE-AENRALILRDK 2403
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK------EINDKEKQVSLLLIQITEKENKMKDLTFLLEeSRDKANQLEEK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2404 DNTQ-RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ--- 2479
Cdd:pfam05483 277 TKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfea 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2480 -----KELAQEQARQLQEDKEQMaQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQA 2554
Cdd:pfam05483 357 ttcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQF 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2555 EEIGEKLHRTE------LATQEKVtlVHTLEIQ----RQQSDHDAERLRAAIAELEREKEK---LQEEATLLQQKSEEMQ 2621
Cdd:pfam05483 428 EKIAEELKGKEqeliflLQAREKE--IHDLEIQltaiKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKELT 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2622 VVQQEQLLQETRAlQESFLSEKDrllQRERFIEQekakLEQLFRDEVAKAQKLREEqqrqqqqmeqeREQLVASMEEARQ 2701
Cdd:pfam05483 506 QEASDMTLELKKH-QEDIINCKK---QEERMLKQ----IENLEEKEMNLRDELESV-----------REEFIQKGDEVKC 566
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2044209144 2702 RQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHR 2750
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1481-1696 |
1.35e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 IRETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAEELQrrmqEEVARREEAAVDAQQQKR 1560
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEAR------QALAQVIANQK-RLERQLEELE----AEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1561 siqeelQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1640
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1641 ERLRRQVQDESQRKRQAEAELALRVKAEAEAAREK--QRALQALEdvrlQAEEAERRL 1696
Cdd:COG1842 157 GIDSDDATSALERMEEKIEEMEARAEAAAELAAGDslDDELAELE----ADSEVEDEL 210
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1838-2205 |
1.36e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1838 LEKQRQLAE-GTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHK--RQELEAELAKVRAEMEVLLAS 1914
Cdd:pfam07888 9 LEEESHGEEgGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKrdREQWERQRRELESRVAELKEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1915 KARAEEESRSTSEKSKqrlEAEASRFRELAEEAARLRALAEETKRQRQLaEEDAarqRAEAERVLaeklaaiseatrlkt 1994
Cdd:pfam07888 89 LRQSREKHEELEEKYK---ELSASSEELSEEKDALLAQRAAHEARIREL-EEDI---KTLTQRVL--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1995 eaeialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASEnELERQKGLVEDTLRQRRQVEEEILAL 2074
Cdd:pfam07888 147 -------ERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK-EFQELRNSLAQRDTQVLQLQDTITTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2075 KASFEKAAAGKAELELELGRIRSNAE-------------------DTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQ 2135
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2136 KSLAAEEEAARQRKSALE---------EVERLKAKVEEARRLRERAEQESARQ--LQLAQEAAQKRLQAEEKAhAFAVQQ 2204
Cdd:pfam07888 299 RARWAQERETLQQSAEADkdrieklsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQ 377
|
.
gi 2044209144 2205 K 2205
Cdd:pfam07888 378 K 378
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2404-2549 |
1.48e-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: 48.08 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2404 DNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-----KMQAVQE-------ATRLKA 2471
Cdd:pfam05262 202 DLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEaknlpKPADTSSpkedkqvAENQKR 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2472 EAELLQQQkelAQEQARQLQEDKEQMAQQLAQETQGF-----QRTLEAERQRqLEMSAEAERLKlrvaEMSRAQARAEED 2546
Cdd:pfam05262 282 EIEKAQIE---IKKNDEEALKAKDHKAFDLKQESKASekeaeDKELEAQKKR-EPVAEDLQKTK----PQVEAQPTSLNE 353
|
...
gi 2044209144 2547 AQR 2549
Cdd:pfam05262 354 DAI 356
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1504-1867 |
1.48e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1504 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQhlrqSSEAEIQAKARQ 1583
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1584 VEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA- 1662
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEs 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1663 ----LRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1738
Cdd:COG4372 162 lqeeLAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1739 TLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREAR 1818
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2044209144 1819 RRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETE 1867
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1495-1913 |
1.54e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1495 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEElqhlrqsse 1574
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1575 aeiqaKARQVEAAERSRVRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1654
Cdd:COG3064 75 -----AAKKLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1655 RQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTA 1734
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1735 QLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1814
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1815 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKR 1894
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADV 383
|
410
....*....|....*....
gi 2044209144 1895 QELEAELAKVRAEMEVLLA 1913
Cdd:COG3064 384 EEAAGAGILAAAGGGGLLG 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1709-1977 |
1.56e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1709 VALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERwrLKANEALRL 1788
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--LAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1789 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE--QAVRQRELAEQELEKQRQLAEgtaqqrlvaeqeliRLRAET 1866
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAE--------------ELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1867 EQGEQQRQLLEEELARLQREAAAATHKRQELEAElakvraemevllaskaraEEESRSTSEKSKQRLEAEASRFRELAEE 1946
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEAL------------------KAERQKLLARLEKELAELAAELAELQQE 221
|
250 260 270
....*....|....*....|....*....|.
gi 2044209144 1947 AARLRALAEETKRQRQLAEEDAARQRAEAER 1977
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2323-2603 |
1.66e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.37 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2323 RQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALILRD 2402
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2403 KDNTQRFLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEKMQAVQeaTRLKAEAELLQQQKE 2481
Cdd:pfam19220 205 DATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMKLEALT--ARAAATEQLLAEARN 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2482 LAQEQARQLQEdKEQMAQQLAQETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIG 2558
Cdd:pfam19220 270 QLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERI 348
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2044209144 2559 EKLhrtelatQEKV-TLVHTLEIQRQQSDHDAERLRaaiAELEREK 2603
Cdd:pfam19220 349 ASL-------SDRIaELTKRFEVERAALEQANRRLK---EELQRER 384
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2318-2496 |
1.70e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2318 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAarQRNQVEEELFSVRVQME-ELSKLKARIEAENR 2396
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2397 ALilrdkdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2476
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|
gi 2044209144 2477 QQQKELAQEQARQLQEDKEQ 2496
Cdd:COG3206 364 RELYESLLQRLEEARLAEAL 383
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1623-1799 |
1.76e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1623 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaeaELALRVKAEAEAAREKQRALQALEDVRLQAEeAERRLRQAEAD 1702
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAEAN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1703 RARQVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQEEHVAVAQlreeaerraqqqaeaerareEAEqelERWRLKA 1782
Cdd:COG2268 275 AEREVQRQLEIAEREREIELQEKEA--EREEAELEADVRKPAEAEKQ--------------------AAE---AEAEAEA 329
|
170
....*....|....*..
gi 2044209144 1783 nEALRLRLQAEEVAQQK 1799
Cdd:COG2268 330 -EAIRAKGLAEAEGKRA 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1848-2195 |
1.89e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1848 TAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTS- 1926
Cdd:PRK04863 277 HANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQAd 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1927 -EKSKQRLEAEAsrfrELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLaeklaaISEATRlkteaeiALKEKEA 2005
Cdd:PRK04863 357 lEELEERLEEQN----EVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAL------DVQQTR-------AIQYQQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2006 EN--ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLrkaseNELERQKGLVEDTLRQRRQVEEEILALKASFEKAAA 2083
Cdd:PRK04863 420 VQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEL-----LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2084 GKAELELELGRIRSNAEDTLRSKEQAELEATRQR-QLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKV 2162
Cdd:PRK04863 495 WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
330 340 350
....*....|....*....|....*....|...
gi 2044209144 2163 EEArrlRERAEQESARQLQLAQEAAQKRLQAEE 2195
Cdd:PRK04863 575 SEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1489-1750 |
1.91e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1489 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEE-------VARREEAAVDAQQQKRS 1561
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1562 IQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEI--RVVRLQLEATE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1638
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1639 EAERLRRQV-QDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQR- 1716
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFl 244
|
250 260 270
....*....|....*....|....*....|....*
gi 2044209144 1717 SAEVELQSKRASFAEKTAQ-LERTLQEEHVAVAQL 1750
Cdd:pfam02029 245 EAEQKLEELRRRRQEKESEeFEKLRQKQQEAELEL 279
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
666-760 |
1.91e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.47 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 666 LRYLQDLLAWVEENQRRVDSAEWGGDLPSVEAQLGSHRGLHQSIDEFRAKIERARADEGQL---SPAPRGTYRDCLGRLD 742
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 2044209144 743 LQYAKLLNSSKARLRSLE 760
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1831-2238 |
1.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1831 RELAEQELEKQR-QLAEGTAQQRLVAEQELIRLRAETEQGEQQrqllEEELARLQREAAAATHKRQELEAELAKVRAEME 1909
Cdd:COG4717 44 RAMLLERLEKEAdELFKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1910 VLlaSKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEA 1989
Cdd:COG4717 120 KL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1990 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqhKADIEERLAQLRkASENELERQKGLVEDTLRQRRQVEE 2069
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE--AAALEERLKEAR-LLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2070 EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK 2149
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2150 SALEEVERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ----QKEQELQQTLQQEQSMLERL 2223
Cdd:COG4717 355 EAEELEEELQLEELEQEIaaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQleelLGELEELLEALDEEELEEEL 434
|
410
....*....|....*
gi 2044209144 2224 RAEAEAARRAAEEAE 2238
Cdd:COG4717 435 EELEEELEELEEELE 449
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
328-405 |
1.98e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 43.45 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 328 DNFTSSWRDGRLFNAIIHRHRPMLIDMSKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 405
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1269-1891 |
2.00e-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: 47.79 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1269 LEATKAALKKLRVQAEAQqpvfdalRDELR-GAQEVGERLQRQHGERDVEVERWRERVAPLLerwqaalAQTDVRQRELE 1347
Cdd:pfam05483 192 IEKMILAFEELRVQAENA-------RLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL-------IQITEKENKMK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1348 QLGRQLRYYRESADPLgawlqdakQRQERIQAVPLANSQAVREQLQQEkelLEEIERYGEKVDECQQLAKQYINAIKDYE 1427
Cdd:pfam05483 258 DLTFLLEESRDKANQL--------EEKTKLQDENLKELIEKKDHLTKE---LEDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1428 LQLVTYK-AQLEPV--ASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRAEERE 1504
Cdd:pfam05483 327 CQLTEEKeAQMEELnkAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1505 rLAEVEAAL-EKQRQLAEahaqaKAQAEREAEELQRRMQEEVA---RREEAAVDAQQQKRSIQEELQH-LRQSSEAEIQ- 1578
Cdd:pfam05483 407 -LEELKKILaEDEKLLDE-----KKQFEKIAEELKGKEQELIFllqAREKEIHDLEIQLTAIKTSEEHyLKEVEDLKTEl 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1579 --AKARQVEAAERSRVRIEEEIRVVR------LQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR---QV 1647
Cdd:pfam05483 481 ekEKLKNIELTAHCDKLLLENKELTQeasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiQK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1648 QDESQRKRQAEAELALRVKAEAEAAREKQRALQ-ALEDVRLQAEEAERRLRQ-AEADRARQVQVALETAQRSA------- 1718
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILEnKCNNLKKQIENKNKNIEElHQENKALKKKGSAENKQLNAyeikvnk 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1719 -EVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEaerraqqqaeaerareeaeqeLERWRLKANEALRLRLQAEEVAQ 1797
Cdd:pfam05483 641 lELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE---------------------VEKAKAIADEAVKLQKEIDKRCQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1798 QKslaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLvaEQELIRLRAETEQGEQQRQLLE 1877
Cdd:pfam05483 700 HK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL--EIELSNIKAELLSLKKQLEIEK 766
|
650
....*....|....
gi 2044209144 1878 EELARLQREAAAAT 1891
Cdd:pfam05483 767 EEKEKLKMEAKENT 780
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1495-1599 |
2.00e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.96 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1495 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ---AKAQAEREAEELQRRM---------QEEVARREEAAVDAQQQKRSI 1562
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110
....*....|....*....|....*....|....*....
gi 2044209144 1563 QEELQHLRQ--SSEAEIQAKARQVEAAERSRVRIEEEIR 1599
Cdd:COG1566 168 QAQLAQAQAglREEEELAAAQAQVAQAEAALAQAELNLA 206
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1555-1756 |
2.20e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1555 AQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrvRIEEEIRVVRLqleateRQRGGAEGELQALRARAEEAEAQKR 1634
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ---RAAEQARQKEL------EQRAAAEKAAKQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1635 QAQEEAErlrrqvQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERrlrQAEADRArqvqvALETA 1714
Cdd:TIGR02794 120 QAEEAKA------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK---KAEAEAK-----AKAEA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2044209144 1715 QRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAER 1756
Cdd:TIGR02794 186 EAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1812-1975 |
2.21e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1812 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREaaaat 1891
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE----- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1892 HKRQELEAELaKVRAEmevllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEedAARQ 1971
Cdd:COG2268 301 REEAELEADV-RKPAE-----AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEA 372
|
....
gi 2044209144 1972 RAEA 1975
Cdd:COG2268 373 AAKP 376
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3161-3198 |
2.26e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2044209144 3161 RRALRGTSVIAGVWLEEAGQRLSIYEALKKDLLPPEVA 3198
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1822-1989 |
2.27e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAathkrqelEAEL 1901
Cdd:TIGR02794 99 AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKK--------KAEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEvllaSKARAEEESRSTSEKSKQRLE-AEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLA 1980
Cdd:TIGR02794 171 AKKKAEAE----AKAKAEAEAKAKAEEAKAKAEaAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
....*....
gi 2044209144 1981 EKLAAISEA 1989
Cdd:TIGR02794 247 EKQGGARGA 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1485-2025 |
2.30e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1485 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQE 1564
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1565 ELQHLRQSSE------AEIQAKARQVEAAERSRVRIEEEIR--VVRLQLEA-------TERQRGGAEGELQALRARAEEA 1629
Cdd:pfam05557 133 ELEELQERLDllkakaSEAEQLRQNLEKQQSSLAEAEQRIKelEFEIQSQEqdseivkNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1630 EAQKRQAQEEAERLRRQVQDESQRKRQAEaelalrvKAEAEAAR---EKQRALQALEDVRLQAEEAERRLRQAEADRARQ 1706
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREE-------KYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1707 VQValetaqRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERraqqqaeaerareeaeqelERWRLKANEAL 1786
Cdd:pfam05557 286 EQL------QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED-------------------LNKKLKRHKAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1787 RLRLQAEEVAQQKS-------LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA----QQRLVA 1855
Cdd:pfam05557 341 VRRLQRRVLLLTKErdgyraiLESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggykQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1856 EQELIRLRAETEQGEQQRQllEEELARLQREAaaathkrQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK---QR 1932
Cdd:pfam05557 421 ERELQALRQQESLADPSYS--KEEVDSLRRKL-------ETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLS 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1933 LEAEASRFRELAEEAARLRALAEETKRQRQLAEEDaarqraeaervlAEKLAAISEATRLKTEAEIA--LKEKEAENERL 2010
Cdd:pfam05557 492 MNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDD------------LEQVLRLPETTSTMNFKEVLdlRKELESAELKN 559
|
570
....*....|....*
gi 2044209144 2011 RRLaeDEAFQRRRLE 2025
Cdd:pfam05557 560 QRL--KEVFQAKIQE 572
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1791-1974 |
2.32e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1791 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLVAEQELIRLRAET 1866
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1867 EQGEQQRQLLEEELARLQREAAAathkRQELEAElAKVRAEMEvllaSKARAEEESRSTSEK-SKQRLEAEASRFRELAE 1945
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEA----KKKAEAE-AAAKAAAE----AKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*....
gi 2044209144 1946 EAArlRALAEETKRQRQLAEEDAARQRAE 1974
Cdd:PRK09510 232 AEA--KAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1486-1656 |
2.38e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEE 1565
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1566 LQHLRQSSEAEIQAKARQVEAAERSRVRieeeiRVVRLQLEATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRR 1645
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 2044209144 1646 QVQDESQRKRQ 1656
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| 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 2044209144 181 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQ 251
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCN 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2044209144 252 IALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 294
Cdd:cd21329 73 YAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1097-1533 |
2.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1097 QAEREYGSCSRHYQQLLQSAEQGAQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRIAE 1169
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1170 QQKAQAEVEGLGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVL 1249
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1250 R------AHEEQLKEAQAVPATLPELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDVEVERWRE 1323
Cdd:COG4717 233 EneleaaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1324 RVAPLLERWQAALAQTDVRQREleqlgrQLRYYRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEK--ELLEE 1401
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgvEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1402 IERYGEKVDECQQLAKQYinaiKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTtltsQYIKFI 1481
Cdd:COG4717 387 LRAALEQAEEYQELKEEL----EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR----EELAEL 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1482 RETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE 1533
Cdd:COG4717 459 EAELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1476-1670 |
2.75e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1476 QYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqakAQAEREaEELQRRMQEEVARREEAAVDA 1555
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD---------EKAERD-ELRAKLYQEEQERKERQKERE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1556 QQQKRsiQEELQHLRQSSEAEIQAKARQvEAAERSRVRIEEEiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1635
Cdd:pfam13868 226 EAEKK--ARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 2044209144 1636 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1670
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2396-2592 |
2.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2396 RALILRDKDNTQRFLQEEAEKMKQVAEEAarLSVAAQEAARLRQLAEEDLAQQRalaekmlkEKMQAVQEatRLKAEAEL 2475
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERR--------NELQKLEK--RLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2476 LQQQKELAQEQARQLQEDKEQMAQQlaqetqgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR----------AEE 2545
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQK--------QQELEKKEEELEELIEEQLQELERISGLTAEEAKeillekveeeARH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2044209144 2546 DAQRFRKQAEEIGEklhrtELATQE-KVTLVHTleIQRQQSDHDAERL 2592
Cdd:PRK12704 170 EAAVLIKEIEEEAK-----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2345-2745 |
2.93e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2345 QKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALilRDKDNTQRFLQEEAEKMKQVAEEA 2424
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA--SDHLNLVQTALRQQEKIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2425 ARLSVAAQEAARLRQLAEEDLAQQRALAEkmlkekmQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKE--QMAQQL- 2501
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQalERAKQLc 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2502 ------AQETQGFQRTLEAERQRQLEMSAEAERlKLRVAEMSRAQAraEEDAQRFRKQAEEIGEklhrtELATQEKVTLV 2575
Cdd:PRK04863 431 glpdltADNAEDWLEEFQAKEQEATEELLSLEQ-KLSVAQAAHSQF--EQAYQLVRKIAGEVSR-----SEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2576 HTLEIQRQQSDHdAERLRAAIAELEREKEKLQEEATLLQ---QKSEEMQVVQQEQLLQETR--ALQESFLSEKDRLLQRE 2650
Cdd:PRK04863 503 RRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQRAERLLAefcKRLGKNLDDEDELEQLQEEleARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2651 RFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVAS--MEEARQRQREAEEGVRRkqeelqlleqqrqqQE 2728
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSqdVTEYMQQLLERERELTV--------------ER 647
|
410
....*....|....*..
gi 2044209144 2729 RLLAEENQRLRERLQRL 2745
Cdd:PRK04863 648 DELAARKQALDEEIERL 664
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1510-2010 |
3.03e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1510 EAALEKQRQLAEAhAQAKAQAErEAEELQRRMQEeVARREEAAVDAQQQKRSIQE---ELQHLRQSSEAEiqakarqvea 1586
Cdd:PRK10929 25 EKQITQELEQAKA-AKTPAQAE-IVEALQSALNW-LEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1587 aersrvriEEEIRVVRLQLEAterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRRQVQDESQ-RKRQAEAELALrv 1665
Cdd:PRK10929 92 --------RDEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAREISDSLSQlPQQQTEARRQL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1666 kAEAEaarekqRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSA--EVELQSKRASFAEK-TAQLERTLQe 1742
Cdd:PRK10929 154 -NEIE------RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1743 ehvavaqlreeaerraqqqaeaerareeaeqelerwrlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgk 1822
Cdd:PRK10929 226 ------------------------------------------ALRNQLNSQ----------------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1823 aeeqavRQRElAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATHK-RQELEA-- 1899
Cdd:PRK10929 235 ------RQRE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlr 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 ----ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEASRFRelaeeAARLR--ALAEETKRQRQLAEEDAARQRA 1973
Cdd:PRK10929 307 eqsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTA 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1974 EAERVLAEKLAA---------------ISEATRLK---TEAEIALKE-KEAENERL 2010
Cdd:PRK10929 376 EQNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1158-1798 |
3.10e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1158 EPARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIYlEKLKTISL 1237
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHTR-QQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1238 VIRSTQGAEEVLRAHeeQLKEAQAVPATLPELEATKAALKKLRVqaeaqqpvfdaLRDELRGAQEVGERLQRQHgerdVE 1317
Cdd:PRK10246 319 RLQSTMALRARIRHH--AAKQSAELQAQQQSLNTWLAEHDRFRQ-----------WNNELAGWRAQFSQQTSDR----EQ 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1318 VERWRERVAPLLERWQAALAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLQDAKQRQERIQAvplANSQAVREQL 1392
Cdd:PRK10246 382 LRQWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNVTQEQT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1393 QQEKELLEEIERYGEKVDE-------CQQLAKqyinaIKDyelqLVTYKAQLEPvASPAkkPKVQSGSESVIQEYVDLrt 1465
Cdd:PRK10246 458 QRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKD----LEAQRAQLQA-GQPC--PLCGSTSHPAVEAYQAL-- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1466 rysELTtltsqyikfirETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQAER----------EAE 1535
Cdd:PRK10246 524 ---EPG-----------VNQSRLDALEKEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQEEQaltqqwqavcASL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1536 ELQRRMQEEVARREEAAVDAQQQKRSIQEelQHLRQSSEAEIQAKARQVEAA-ERSRVRIEEEIRVVRLQLEAterqrgg 1614
Cdd:PRK10246 589 NITLQPQDDIQPWLDAQEEHERQLRLLSQ--RHELQGQIAAHNQQIIQYQQQiEQRQQQLLTALAGYALTLPQ------- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1615 AEGELQALRARAEEAeAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQR------ALQAlEDVRLQ 1688
Cdd:PRK10246 660 EDEEASWLATRQQEA-QSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQvheqclSLHS-QLQTLQ 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1689 AEEAErrlrqaEADRARQVQVALETAqrsaeveLQSKRasFAEKTAQLERTLQEEhvAVAQLREEAERRAQQQAEAERAR 1768
Cdd:PRK10246 738 QQDVL------EAQRLQKAQAQFDTA-------LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLV 800
|
650 660 670
....*....|....*....|....*....|
gi 2044209144 1769 EEAEQELERWRLKANEALRLRLQAEEVAQQ 1798
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQE 830
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1590-1800 |
3.17e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1590 SRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEA 1669
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1670 EAAREKQRALQALE--DVRLQAEEAERRLRQAEA-DRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVA 1746
Cdd:COG3883 90 ERARALYRSGGSVSylDVLLGSESFSDFLDRLSAlSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1747 VAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKS 1800
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1514-1645 |
3.18e-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: 44.26 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1514 EKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1591
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1592 VRIEEEIRVVRLQLEATERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1645
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1507-1714 |
3.20e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1507 AEVEAALEKQRQLAEAHAQAKAQAEREAEELQ--RRMQEEVARREEAAVDAQQQKRSIQE-----------ELQHLRQSS 1573
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1574 EAE------IQAKARQVEAAERSRVRIEEEIRVVrLQLEATERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1640
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1641 ERLRRQVQDESQRKRQAEAELAL-RVKAEAEAAREKQRALQAL--------EDVRLQAEeaerrlrQAEADRARQVQVAL 1711
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALaathgynpRDFRKRAE-------QALAANAKTATLAL 1378
|
...
gi 2044209144 1712 ETA 1714
Cdd:PHA03247 1379 EAA 1381
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1492-1738 |
3.22e-04 |
|
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: 47.12 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1492 ERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEEL-QHLR 1570
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVeQKKE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1571 QSSEAEIQA-KARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK---------------R 1634
Cdd:pfam10174 532 ECSKLENQLkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdkkiaelesltlR 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1635 QAQEEAERLR--RQVQDESQRKRQAEAELALRVK-AEAEAAREKQRA--LQALEDVRLQAEEAERRLRQAE--------- 1700
Cdd:pfam10174 612 QMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSSTQqslaekdgh 691
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1701 -----ADRARQVQVALETAQRS------------AEVEL-QSKRASFAEKTAQLER 1738
Cdd:pfam10174 692 ltnlrAERRKQLEEILEMKQEAllaaisekdaniALLELsSSKKKKTQEEVMALKR 747
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3530-3565 |
3.59e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2044209144 3530 TLLLEAQAATGFLIDPVRNQRLYVHEAVKAGVVGPE 3565
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1495-1567 |
3.59e-04 |
|
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: 43.58 E-value: 3.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044209144 1495 AEQQRAEERERLAEVEAALEKQRQLAEA-HAQAKAQAEREAEELQRRMQEEVAR-REEAAVDAQQQKRSIQEELQ 1567
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEiIEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQEKEKALAELR 116
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2305-2465 |
3.82e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2305 QVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQmEEL 2384
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2385 SKLKARIEAENRALILRDKDnTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2464
Cdd:COG1579 92 EALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
.
gi 2044209144 2465 E 2465
Cdd:COG1579 171 K 171
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1525-1710 |
3.85e-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: 45.88 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1525 QAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrvrieeeirvvrlQ 1604
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQA--------------Q 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1605 LEATERQrggaegeLQALRARAEEAEAQKRQAQeEAERLRRQVQDES-QRKRQAEAELALRVKAEAEAAREkqrALQALE 1683
Cdd:pfam00529 119 LAQAQID-------LARRRVLAPIGGISRESLV-TAGALVAQAQANLlATVAQLDQIYVQITQSAAENQAE---VRSELS 187
|
170 180
....*....|....*....|....*..
gi 2044209144 1684 DVRLQAEEAERRLRQAEADRARQVQVA 1710
Cdd:pfam00529 188 GAQLQIAEAEAELKLAKLDLERTEIRA 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2323-2670 |
4.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2323 RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRvqmEELSKLKARIEAENRALilrd 2402
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR---EELEQLEEELEQARSEL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2403 kdntqrflQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKEL 2482
Cdd:COG4372 76 --------EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2483 AQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLH 2562
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2563 RTELATQEKVTLVHT--LEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRALQESFL 2640
Cdd:COG4372 228 EAKLGLALSALLDALelEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
330 340 350
....*....|....*....|....*....|
gi 2044209144 2641 SEKDRLLQRERFIEQEKAKLEQLFRDEVAK 2670
Cdd:COG4372 308 SLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2385-2619 |
4.16e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2385 SKLKARIEAENRALILRdkdntQRFlqeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQ 2464
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAK-----ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2465 EATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV 2533
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2534 -AEMSRAQAR---AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEE 2609
Cdd:PRK05035 583 aAAIARAKAKkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQ 662
|
250
....*....|
gi 2044209144 2610 ATLLQQKSEE 2619
Cdd:PRK05035 663 QQANAEPEEA 672
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1520-1706 |
4.42e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1520 AEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEiR 1599
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK-A 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1600 VVRLQLEATERQRGGAEGELQAlRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAEaelalrvkaeaEAAREKQRAL 1679
Cdd:PRK12678 146 GEGGEQPATEARADAAERTEEE-ERDERRRRGDREDRQAEAERGERG--RREERGRDGD-----------DRDRRDRREQ 211
|
170 180
....*....|....*....|....*..
gi 2044209144 1680 QALEDVRLQAEEAERRLRQAEADRARQ 1706
Cdd:PRK12678 212 GDRREERGRRDGGDRRGRRRRRDRRDA 238
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1362-1562 |
4.57e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1362 PLGAWLQDAKQRQERIQAVPLANSQAVREQLQQEKELLEE-------IERYGEKVDECQ----QLAKQY--INA-IKDYE 1427
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQlkkqeeaISQASRKLRETQntlnQLNKQIdeLNAsIAKLE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1428 LQLVTYK----AQLEPVASPAKKPKVQ---SGSESviQEYVDLRTRYSELTTLTSQYIKFIRET-----LRRMEEEERLA 1495
Cdd:PRK11637 117 QQQAAQErllaAQLDAAFRQGEHTGLQlilSGEES--QRGERILAYFGYLNQARQETIAELKQTreelaAQKAELEEKQS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1496 EQQ----------------RAEERERLAEVEAALEK-QRQLAE--------------AHAQAKAQAEREAEELQR-RMQE 1543
Cdd:PRK11637 195 QQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAARvRDKQ 274
|
250
....*....|....*....
gi 2044209144 1544 EVARREEAAVDAQQQKRSI 1562
Cdd:PRK11637 275 KQAKRKGSTYKPTESERSL 293
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1094-1664 |
4.58e-04 |
|
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: 46.65 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1094 DRLQAEREYGSCSRHYQQLLQSAEQGAQEESrcqrcISELKDIRL-QLEACETRTVHRLRlpldkepaRECAQRIAEQQK 1172
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR--------RELDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1173 AQAEVEGL-----GKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEE 1247
Cdd:pfam15921 431 LEALLKAMksecqGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1248 VLRAHEEQ-----------LKEAQAVPATLPELEATKAALKKLRVQAEAQQPVFDALRDELRG-AQEVGerlqrQHGerd 1315
Cdd:pfam15921 511 AIEATNAEitklrsrvdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmTQLVG-----QHG--- 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1316 veverwRERVAPLLERWQaalAQTDVRQRELEQlgRQLRYYRESADPLGAWLQdAKQRQERIQAVPLANS-----QAVRE 1390
Cdd:pfam15921 583 ------RTAGAMQVEKAQ---LEKEINDRRLEL--QEFKILKDKKDAKIRELE-ARVSDLELEKVKLVNAgserlRAVKD 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1391 QLQQEKELLEEIERYGEKVDecqqlakqyiNAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTRYSEL 1470
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNELN----------SLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSEL 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1471 TTltsqyikfIRETLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKAqaereaeelqrrMQEEVARREE 1550
Cdd:pfam15921 709 EQ--------TRNTLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1551 AAVDAQQQKRSIQEELQHLRQsseaeiqakarqveaaersrvrieeeirvvRLQLEATERQRggAEGELQALRA---RAE 1627
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQ------------------------------ELSTVATEKNK--MAGELEVLRSqerRLK 803
|
570 580 590
....*....|....*....|....*....|....*..
gi 2044209144 1628 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR 1664
Cdd:pfam15921 804 EKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1496-1702 |
4.59e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1496 EQQRAEERERLAEVEAAL-----------EKQRQLAEAHAQAKAQAEREAEELQRRMQEEVA------RREEAAVDAQQQ 1558
Cdd:PRK00409 526 EELERELEQKAEEAEALLkeaeklkeeleEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYASVK 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1559 KRSIQEELQHLRQSSEAEIQAKARQVEAAErsRVRIEEEIRVVRLqleaterqrgGAEGELQALRaraeeaeaQKRQAQE 1638
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL----------GQKGEVLSIP--------DDKEAIV 665
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 1639 EAERLRRQVQ-DESQRKRQAEAELALRVKAEAEAAREKQRALqaleDVR-LQAEEAERRLRQAEAD 1702
Cdd:PRK00409 666 QAGIMKMKVPlSDLEKIQKPKKKKKKKPKTVKPKPRTVSLEL----DLRgMRYEEALERLDKYLDD 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1565-1713 |
4.67e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1565 ELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIrvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQA-------- 1636
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1637 -QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALET 1713
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1486-1741 |
4.69e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREaeelqrrmqeevarREEAAVDAQQQKRSIQE 1564
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1565 ELQhLRQSSEAEIQAKARQVEAAERSRVRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQAQEEAERLR 1644
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNHEEEVRELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1645 RQVQDESqrkrqaeaelalrVKAEAEAAReKQRALQALEDVRLQAEE-AERRLRQAEAdrarQVQVALETAQRSAEVELQ 1723
Cdd:pfam00038 149 AQVSDTQ-------------VNVEMDAAR-KLDLTSALAEIRAQYEEiAAKNREEAEE----WYQSKLEELQQAAARNGD 210
|
250
....*....|....*...
gi 2044209144 1724 SKRASfAEKTAQLERTLQ 1741
Cdd:pfam00038 211 ALRSA-KEEITELRRTIQ 227
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1836-2117 |
4.79e-04 |
|
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: 46.00 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1836 QELEKQRQLAEgtaqqrlVAEQELIRLRAETEQGEQQRQllEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASK 1915
Cdd:pfam03148 10 REAEAQRNDAE-------RLRQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1916 ARAEEESRSTSEK---SKQRLEAEASRF----------RELAEEA-------ARLRALAEETkrQRQLAEEDAARQRAEA 1975
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1976 ErvLAEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLRKASEN 2048
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2049 ELERQKGLVEDTLRQRrqVEEeilalkasFEKAaagKAELELELGRIRsnaedtlrsKEQAELEATRQR 2117
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTL---------QEIAELEKNIEA 283
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2316-2483 |
4.86e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.00 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2316 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRNQVEEELFSVRVQMEELSKlkarieaen 2395
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALRS--------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2396 ralILRDKDNTQRFLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2473
Cdd:COG3524 243 ---YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 2044209144 2474 EllQQQKELA 2483
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1873-2185 |
4.87e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1873 RQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEASRFRELAEEAARLRA 1952
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1953 LAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 2032
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2033 ADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 2112
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 2113 ATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2185
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2407-2563 |
4.95e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2407 QRFLQEEaEKMKQVAEEAARLSVAAQEAArlrqlaEEDLAQQRALAEKMLK-----EKMQAVQEATRLKAEAEllQQQKE 2481
Cdd:cd16269 145 QLYLEDR-EKLVEKYRQVPRKGVKAEEVL------QEFLQSKEAEAEAILQadqalTEKEKEIEAERAKAEAA--EQERK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2482 LAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEmsaEAERLklrVAEMSRAQARAEEdaQRFRKQAEEIGEKL 2561
Cdd:cd16269 216 LLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK---EQERA---LESKLKEQEALLE--EGFKEQAELLQEEI 287
|
..
gi 2044209144 2562 HR 2563
Cdd:cd16269 288 RS 289
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1487-1674 |
5.16e-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: 46.15 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1487 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEEL 1566
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1567 QHLRQSSEAEIQAKARQVeaaersrvrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1646
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 2044209144 1647 VQDESQR-KRQAEAElalrVKAEAEAARE 1674
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1479-1678 |
5.32e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 46.47 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1479 KFIRETLRRMEEEER---LAEQQRAEererlaeveaaLEKQRQLAEAHAQAKAQAEREAEELQRRMQ----------EEV 1545
Cdd:PLN03188 1048 KLEQERLRWTEAESKwisLAEELRTE-----------LDASRALAEKQKHELDTEKRCAEELKEAMQmamegharmlEQY 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1546 ARREEAAVDAQQQKRSIQEELQHLRQsseAEIQAKARQVE-------AAERS--RVRIEEEIRVVRLQLEATERQ-RGGA 1615
Cdd:PLN03188 1117 ADLEEKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISalKVEREKERRYLRDENKSLQAQlRDTA 1193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1616 E-----GELQALRARAEEA--EAQKR--QAQEEAERLRRQVqDESQRKRQAEAELALRVKAEAEAAREKQRA 1678
Cdd:PLN03188 1194 EavqaaGELLVRLKEAEEAltVAQKRamDAEQEAAEAYKQI-DKLKRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1870-2080 |
5.35e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1870 EQQRQLLEeeLARLQREAAAATHKRQELEAELAKVRAEMEvllaskaraeeesrstsekskqrleaeasrfrELAEEAAR 1949
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELA--------------------------------ALEARLEA 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1950 LRALAEETKRQRQLAEEDAARQRAEAERvLAEKLAAISEATrlktEAEIALKEKEAeNERLRRLAEDEAFQRRRLEEQAA 2029
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNK----EYEALQKEIES-LKRRISDLEDEILELMERIEELE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2030 QHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEK 2080
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2451-2743 |
5.40e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2451 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQ---ETQGFQRTLEAERQRQLEMSAEAE 2527
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQareELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2528 RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlvhtLEIQRQQSDHDAERLRAAIAELEREKEKLQ 2607
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD-------LEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2608 EEATLLQQKSEEMQVVQQEQLLQETRALQESFLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQ 2687
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 2688 EREQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLLAEENQRLRERLQ 2743
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1462-1714 |
5.64e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 45.80 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1462 DLRTRYSELTTLTSQyIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQaKAQAEREAEELQRRM 1541
Cdd:COG1538 77 EVAQAYFDLLAAQEQ-LALAEENLALAEELLELARARYEAGLASRLDVLQA---EAQLAQARAQ-LAQAEAQLAQARNAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1542 QEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA------EIQAKARQVEAAERsRVRIEEEIRVVRLQLEATERQRGGA 1615
Cdd:COG1538 152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEalerrpDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1616 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ 1676
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1677 RALQALE--------------DVRLQAEEAERRLRQAEADRArQVQVALETA 1714
Cdd:COG1538 311 EALELARaryraglaslldvlDAQRELLQAQLNLIQARYDYL-LALVQLYRA 361
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2910-2946 |
6.04e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.04e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 2910 KLLSAERAVTGYKDPYTGEQISLFQAMKKELIVRDHG 2946
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1822-1981 |
6.19e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLvAEQELIRLRAEteqgEQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDL-AREALERKAEL----EAQAEALEAQLAQLEEQVEKLKEALRQLESKL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE---ETKRQRQLAEE-DAARQRAEAER 1977
Cdd:COG1842 129 EELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEVED 208
|
....
gi 2044209144 1978 VLAE 1981
Cdd:COG1842 209 ELAA 212
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2312-2545 |
6.21e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2312 EKHKKFAEQTLrqkAQVEQELTTLRLQLE-----ETDHQKSILDEELQRLKAEVTEAAR-QRNQVEEElfsVRVQMEELS 2385
Cdd:COG2268 147 EDREKFAEKVQ---EVAGTDLAKNGLELEsvaitDLEDENNYLDALGRRKIAEIIRDARiAEAEAERE---TEIAIAQAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2386 KLKARIEAENRALIL--------RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlK 2457
Cdd:COG2268 221 REAEEAELEQEREIEtariaeaeAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-A 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2458 EKMQAVQEAT-RLKAEAEllqqqKELAQEQARQlqeDKEQMAQQLAQETQGFQRTLEAERqrqlEMSAEAERLKL--RVA 2534
Cdd:COG2268 300 EREEAELEADvRKPAEAE-----KQAAEAEAEA---EAEAIRAKGLAEAEGKRALAEAWN----KLGDAAILLMLieKLP 367
|
250
....*....|.
gi 2044209144 2535 EMSRAQARAEE 2545
Cdd:COG2268 368 EIAEAAAKPLE 378
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1571-1725 |
6.29e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1571 QSSEAEIQAKARQVEAA---ERSRV--RIE-EEIRVVRLQLEATerqrgGAEGELQAlRARAE-EAEAQKRQAQEEAErl 1643
Cdd:PTZ00491 664 QEAAARHQAELLEQEARgrlERQKMhdKAKaEEQRTKLLELQAE-----SAAVESSG-QSRAEaLAEAEARLIEAEAE-- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1644 rrqVQDESQRKRqaeaelALRVKAEAEAAREKQRALQALEDVRLQAE---EAERRLRQAEADRARQVQVAL--ET--AQR 1716
Cdd:PTZ00491 736 ---VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATKFERIVEALgrETliAIA 806
|
....*....
gi 2044209144 1717 SAEVELQSK 1725
Cdd:PTZ00491 807 RAGPELQAK 815
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1519-1698 |
6.36e-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: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1519 LAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqSSEAEIQAKARQVeaaersrvrieeei 1598
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGIL--DPEATAEALLQLI-------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1599 rvvrLQLEAterQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL--------RVKAEAE 1670
Cdd:COG3524 224 ----ATLEG---QLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLasllaeyeRLELERE 296
|
170 180
....*....|....*....|....*....
gi 2044209144 1671 -AAREKQRALQALEDVRLqaeEAERRLRQ 1698
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 2044209144 186 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIAL 254
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2044209144 255 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 298
Cdd:cd21324 102 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1496-1623 |
6.75e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1496 EQQRAEERERLAEVEAALEKQRQLAEAHAQAkaqaerEAEELQRRMQEEVARREEaaVDAQQQKRSIQEELQHLRQSSEA 1575
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2044209144 1576 EIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRggaegELQALR 1623
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1620-1750 |
6.77e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1620 QALRARAEEAEAQKRQAQEEAERLRRQVqDESQRKRQA--EAELALRVKAEAEAAREKQRALQA-LEDVRLQAEEAERRL 1696
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1697 RQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1750
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1497-1691 |
6.80e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.74 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1497 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE 1576
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1577 IQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKR 1655
Cdd:PRK07735 156 EEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSgDEDA 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 2044209144 1656 QAEAELALRVKAEAeAAREKQRALQALEDVRLQAEE 1691
Cdd:PRK07735 236 KAKAIAAAKAKAAA-AARAKTKGAEGKKEEEPKQEE 270
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1322-1569 |
6.93e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1322 RERVAPLLERWQAALAQTDVRQRELEQLGRQLRYYR------ESADP-LGAW---------LQDAKQRQERIQAVPLA-- 1383
Cdd:COG0497 157 LEEYREAYRAWRALKKELEELRADEAERARELDLLRfqleelEAAALqPGEEeeleeerrrLSNAEKLREALQEALEAls 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1384 -NSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEpvASPakkpkvqsgsesviQEYVD 1462
Cdd:COG0497 237 gGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLE--FDP--------------ERLEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1463 LRTRYSELTTLTSQYikfiretlrRMEEEERLAEQQRAeeRERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQrrmq 1542
Cdd:COG0497 301 VEERLALLRRLARKY---------GVTVEELLAYAEEL--RAELAELENSDERLEELEAELAEAEAELLEAAEKLS---- 365
|
250 260
....*....|....*....|....*..
gi 2044209144 1543 eevARREEAAVDAQQQkrsIQEELQHL 1569
Cdd:COG0497 366 ---AARKKAAKKLEKA---VTAELADL 386
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1454-1742 |
7.05e-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: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1454 ESVIQEYVDLRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEV--------------EAALEKQRQL 1519
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELeediktltqrvlerETELERMKER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1520 AEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEaEIQAKARQVEAAERSRVRIE---E 1596
Cdd:pfam07888 159 AKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQD-TITTLTQKLTTAHRKEAENEallE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1597 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA-----LRVKAEAEA 1671
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAqeretLQQSAEADK 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 1672 AR--EKQRALQALEDvRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1742
Cdd:pfam07888 318 DRieKLSAELQRLEE-RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1961-2190 |
7.16e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1961 RQLAEEDAARQRAEAERVLAEklaAISEATRLKTEAEIALKEkeaENERLRRLAEDEAFQRRR-LEEQaaqhkadiEERL 2039
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNeLQKL--------EKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2040 AQlrkaSENELERQKGLVEDTLRQRRQVEEEILALKASFEKAaagKAELElelgrirsnaedTLRSKEQAELEatrqrql 2119
Cdd:PRK12704 92 LQ----KEENLDRKLELLEKREEELEKKEKELEQKQQELEKK---EEELE------------ELIEEQLQELE------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2120 aaeeeqrrreaeerVQKSLAAEEeaARQRksALEEVERlKAKVEEARRLRErAEQEsarqlqlAQEAAQKR 2190
Cdd:PRK12704 146 --------------RISGLTAEE--AKEI--LLEKVEE-EARHEAAVLIKE-IEEE-------AKEEADKK 189
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2301-2565 |
7.46e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2301 LKQKQVADAEMEKHKKfaeqtlrQKAQVEQELTTLRLQLEETDHQKSILDEELQRLK-------AEVTEAARQRNQVEEE 2373
Cdd:COG1340 14 EEKIEELREEIEELKE-------KRDELNEELKELAEKRDELNAQVKELREEAQELRekrdelnEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2374 LFSVRVQMEEL--------------SKLKARIEA-------------ENRALILRDKDntqrfLQEEAEKMKQVAEEAAR 2426
Cdd:COG1340 87 LNELREELDELrkelaelnkaggsiDKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2427 LSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLaq 2503
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL-- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2504 etqgfqrtleaerqRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2565
Cdd:COG1340 240 --------------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1482-1654 |
7.77e-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: 45.22 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLAEQQRAE---ERERLAEVEAALEKQRQlAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQ 1558
Cdd:TIGR02794 112 KQAEEKQKQAEEAKAKQAAEakaKAEAEAERKAKEEAAKQ-AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1559 KRSIQEELQHLRQSSEAEIQAKARQVEAAersrvrieeeirvvrlqLEATERQRGGAEGELQALRARAEEAEAQK----- 1633
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAA-----------------AAAAEAERKADEAELGDIFGLASGSNAEKqggar 253
|
170 180
....*....|....*....|..
gi 2044209144 1634 -RQAQEEAERLRRQVQDESQRK 1654
Cdd:TIGR02794 254 gAAAGSEVDKYAAIIQQAIQQN 275
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1822-2118 |
8.10e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.72 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQElekQRQLAEGTAQqrlvaeqelIRLRAETEQGEQQRQLLEE--ELARLQREAAAAThkrQELEA 1899
Cdd:COG5185 279 RLNENANNLIKQFENT---KEKIAEYTKS---------IDIKKATESLEEQLAAAEAeqELEESKRETETGI---QNLTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1900 ELAKVRAEMEVLLaSKARAEEESRSTS---EKSKQRLEAEASRFRELAEEaarLRALAEETKRQRQLAEEDAARQRAEAE 1976
Cdd:COG5185 344 EIEQGQESLTENL-EAIKEEIENIVGEvelSKSSEELDSFKDTIESTKES---LDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1977 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA-----QHKADIEERLAQL-RKASE--N 2048
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrsvrSKKEDLNEELTQIeSRVSTlkA 499
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2049 ELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA--EDTLRSKEQAELEATRQRQ 2118
Cdd:COG5185 500 TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELiqASNAKTDGQAANLRTAVID 571
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1822-1989 |
8.10e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.78 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQR-ELAEQE----LEKQRQLAEGTAQQrlvAEQELIRLRAETEQGEQQRQlleeelARLQREAAAathkrqe 1896
Cdd:PTZ00491 662 KSQEAAARHQaELLEQEargrLERQKMHDKAKAEE---QRTKLLELQAESAAVESSGQ------SRAEALAEA------- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1897 lEAELAKVRAEMEVLlASKARAEE-ESRSTSEKSKQRLEAEASRFRELAEEaarlralaeETKRQRQLAEEDAARQRAEA 1975
Cdd:PTZ00491 726 -EARLIEAEAEVEQA-ELRAKALRiEAEAELEKLRKRQELELEYEQAQNEL---------EIAKAKELADIEATKFERIV 794
|
170
....*....|....
gi 2044209144 1976 ERVLAEKLAAISEA 1989
Cdd:PTZ00491 795 EALGRETLIAIARA 808
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1293-1661 |
8.29e-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: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1293 LRDELRGAQEVGERLQRQHGERDVEVERWRERVAPLLERWQAALAQTDVRQRELEQLgrqLRYYRESADPLGAWLQDAKQ 1372
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1373 RQERIQAVPLANSQAVREQLQQEKELLEEIERYGEKV-------DECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAK 1445
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1446 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfIRETLRRMEEEERLAEQQRAeERERLAEVEAALEKQRQLAEAH 1523
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQK----LTTAHRKEAENEALLEELRS-LQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1524 AQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEiRVVRL 1603
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 1604 QLEAT-ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1661
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2302-2550 |
8.31e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2302 KQKQvADAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRN------QVEE 2372
Cdd:PRK11281 50 KQKL-LEAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2373 ELFSVRVQmeeLSKLKARIEAENRALIlrdkdnTQRFLQEEAEkmkqvaeeaARLSVAAQEAARLRQLAEEDLAQQRALA 2452
Cdd:PRK11281 129 RLAQTLDQ---LQNAQNDLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2453 EKmLKEKMQAVQEATrlkaEAELLQQQKELaqEQARQLQEdkeqmaqqLAQEtqgfQRTLEAERQRQLEMSAEA------ 2526
Cdd:PRK11281 191 PS-QRVLLQAEQALL----NAQNDLQRKSL--EGNTQLQD--------LLQK----QRDYLTARIQRLEHQLQLlqeain 251
|
250 260
....*....|....*....|....*
gi 2044209144 2527 -ERLKLrvAEMSRAQARAEEDAQRF 2550
Cdd:PRK11281 252 sKRLTL--SEKTVQEAQSQDEAARI 274
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1482-1672 |
8.34e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLAEQQRAEERERLAEVEAALekqrqlaeAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRS 1561
Cdd:PRK05035 523 REARKAQARARQAEKQAAAAADPKKAAVAAAI--------ARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1562 IQEELQHLRQSSEAEIQAKARQVEAA-ERSRVRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQAQEEA 1640
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEP 669
|
170 180 190
....*....|....*....|....*....|..
gi 2044209144 1641 ErlrrqvQDESQRKRQAEAELAlRVKAEAEAA 1672
Cdd:PRK05035 670 E------EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1588-1706 |
8.50e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 43.41 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1588 ERSRVRIEEEIRvvrlqlEATERQRGGAegelQALraraeeAEAQKR--QAQEEAERLRRQVQDESQRKR-----QAEAE 1660
Cdd:PRK07352 49 EERREAILQALK------EAEERLRQAA----QAL------AEAQQKlaQAQQEAERIRADAKARAEAIRaeiekQAIED 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2044209144 1661 LA-LRVKAEAEAAREKQRALQAL--EDVRLQAEEAERRLRQAEADRARQ 1706
Cdd:PRK07352 113 MArLKQTAAADLSAEQERVIAQLrrEAAELAIAKAESQLPGRLDEDAQQ 161
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1480-1542 |
8.59e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 45.63 E-value: 8.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 1480 FIRETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAEREAEELQRRMQ 1542
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1462-1797 |
8.62e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1462 DLRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAEELQRRM 1541
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1542 QEEVARREEAAvDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQA 1621
Cdd:COG4372 94 AELAQAQEELE-SLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1622 LRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEA 1701
Cdd:COG4372 169 LEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1702 DRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLK 1781
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|....*.
gi 2044209144 1782 ANEALRLRLQAEEVAQ 1797
Cdd:COG4372 327 KLELALAILLAELADL 342
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3201-3234 |
9.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 9.22e-04
10 20 30
....*....|....*....|....*....|....
gi 2044209144 3201 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPE 3234
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1822-2015 |
9.66e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAE 1981
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 2044209144 1982 KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 2015
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1822-2091 |
1.05e-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: 44.91 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:pfam13868 67 RKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAE-ASRFRELAEEAARLRALAEETKRQR-QLAEEDAARQRAEAERVL 1979
Cdd:pfam13868 147 KEEEREEDERILEYLKEKAEREEEREAEREEIEEEkEREIARLRAQQEKAQDEKAERDELRaKLYQEEQERKERQKEREE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1980 AEKLAAISEATRLKTEAEIALKEKEAENERlrrlAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVED 2059
Cdd:pfam13868 227 AEKKARQRQELQQAREEQIELKERRLAEEA----EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEER 302
|
250 260 270
....*....|....*....|....*....|..
gi 2044209144 2060 TLRQRRQVEEEILALKASFEKAAAGKAELELE 2091
Cdd:pfam13868 303 EEQRAAEREEELEEGERLREEEAERRERIEEE 334
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1619-1718 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1619 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEsQRKRQAEAElALRVKAEAEAAREKQRALQALEdvrlqaEEAERR 1695
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 2044209144 1696 LRQAEADRARQVQVALETAQRSA 1718
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1862-2113 |
1.12e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1862 LRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAemevlLASKARAEEEsrstsekskqrLEAEasrfR 1941
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA-----AALQPGEEEE-----------LEEE----R 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1942 ELAEEAARLRALAEETkrQRQLAEED--------AARQRAEAERVLAEKLAAISEATRlktEAEIALKEKEAEnerLRRL 2013
Cdd:COG0497 216 RRLSNAEKLREALQEA--LEALSGGEggaldllgQALRALERLAEYDPSLAELAERLE---SALIELEEAASE---LRRY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2014 AEDEAFQRRRLEEqaaqhkadIEERLAQLRKaseneLERQKGL-VEDTLRQRRQVEEEILALKASFEKAAAGKAELELEL 2092
Cdd:COG0497 288 LDSLEFDPERLEE--------VEERLALLRR-----LARKYGVtVEELLAYAEELRAELAELENSDERLEELEAELAEAE 354
|
250 260
....*....|....*....|...
gi 2044209144 2093 GRIRSNAED--TLRSKEQAELEA 2113
Cdd:COG0497 355 AELLEAAEKlsAARKKAAKKLEK 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2085-2561 |
1.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2085 KAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERvQKSLAAEEEAARQRKSALEEVERLKAKVEE 2164
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2165 ARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARERA 2244
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2245 EREAAQSRRQVEEAER---LKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKHKKFAEQT 2321
Cdd:COG4717 214 ELEEAQEELEELEEELeqlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2322 LRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAArqrnqveEELFSVRVQMEELSKLKARIE-AENRALIL 2400
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLREAEeLEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2401 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmqAVQEATRLKAEAELLQQQK 2480
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2481 ELAQEQARQLQEDKEQMAQQLAQ-ETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEEDAQ-RFRKQA 2554
Cdd:COG4717 442 EELEEELEELREELAELEAELEQlEEDGELAELLQELEELKaelrELAEEWAALKLALELLEEAREEYREERLpPVLERA 521
|
....*..
gi 2044209144 2555 EEIGEKL 2561
Cdd:COG4717 522 SEYFSRL 528
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1877-2017 |
1.12e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 45.31 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1877 EEELARLQREAAAATH-----KRQELEAELAKVRAEM--EVLLASKARAEEesrstseKSKQRLEAEASRFR---ELAEE 1946
Cdd:pfam04147 131 EEEDGQLDLKRVRRAHfgggeDDEEEEPERKKSKKEVmeEVIAKSKLHKYE-------RQKAKEEDEELREEldkELKDL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1947 AARLRALAEETKRQRQLAEEDAARQRAEAE-----RVLA-EKLAAISEatRLKTEAEIALKEKE----AENERLRRLAED 2016
Cdd:pfam04147 204 RSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydklvRELAfDKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRMRGE 281
|
.
gi 2044209144 2017 E 2017
Cdd:pfam04147 282 E 282
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2362-2514 |
1.18e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2362 EAARQRNQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRflQEEAEKMKQVAEEAARLSVAAQEAARLRQLA 2441
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR--QEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2442 EEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL-----------QQQKELAQEQARQLQED---KEQMAQQLAQETQG 2507
Cdd:pfam15709 434 ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLmemaeeerleyQRQKQEAEEKARLEAEErrqKEEEAARLALEEAM 513
|
....*..
gi 2044209144 2508 FQRTLEA 2514
Cdd:pfam15709 514 KQAQEQA 520
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2353-2620 |
1.21e-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: 45.02 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2353 LQRLKAEVTEAARQRNQVEEELFSVRVQMEE-----LSKLKARIEAENRALILRDKDNTQRFLQEEAE--KMKQVAEEAA 2425
Cdd:pfam05667 209 LERNAAELAAAQEWEEEWNSQGLASRLTPEEyrkrkRTKLLKRIAEQLRSAALAGTEATSGASRSAQDlaELLSSFSGSS 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2426 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATrlkaeaelLQQQKELA--QEQARQLQEDKEQMAQQLAQ 2503
Cdd:pfam05667 289 TTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQ--------QQREEELEelQEQLEDLESSIQELEKEIKK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2504 ETQGFQRTLEAERQRQLEMSAEAE--RLKLRVAEMSraqaraeedaqrfrKQAEEIGEKLHRTELATQEKVtlvhtLEIQ 2581
Cdd:pfam05667 361 LESSIKQVEEELEELKEQNEELEKqyKVKKKTLDLL--------------PDAEENIAKLQALVDASAQRL-----VELA 421
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2044209144 2582 RQQSDHdaerlRAA-IAELEREKEKLQEEATLLQQKSEEM 2620
Cdd:pfam05667 422 GQWEKH-----RVPlIEEYRALKEAKSNKEDESQRKLEEI 456
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1458-1593 |
1.27e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1458 QEYVDLRTRYS---------ELTTlTSQYIKFIRETLRRMEEEERLAEQQR-------AEERERLAEVEAALEKQRQLAE 1521
Cdd:PTZ00491 638 VEPVDERTRDSlqksvqlaiEITT-KSQEAAARHQAELLEQEARGRLERQKmhdkakaEEQRTKLLELQAESAAVESSGQ 716
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 1522 AHAQAKAQA-----EREAEELQRRMQEEVARREEAAVDAQQQKRSIQeELQHLRQSSEAEIqAKARQVEAAERSRVR 1593
Cdd:PTZ00491 717 SRAEALAEAearliEAEAEVEQAELRAKALRIEAEAELEKLRKRQEL-ELEYEQAQNELEI-AKAKELADIEATKFE 791
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1480-1567 |
1.27e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 42.30 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1480 FIRETLRRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAEREAEELQRR-----MQEEVARREE 1550
Cdd:PRK07353 26 FYKPVGKVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEalaeaQAEAQASKEK 105
|
90
....*....|....*..
gi 2044209144 1551 AAVDAQQQKRSIQEELQ 1567
Cdd:PRK07353 106 ARREIEQQKQAALAQLE 122
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2322-2609 |
1.28e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2322 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFsvrvQMEELSKLKARIEAEnraliL 2400
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2401 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2480
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2481 ELAQEQARQLQEDKEQMAQQLAQET--QGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2558
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2559 EKLHRTE-----LATQEKVTLVHTLEIQR--------------------QQSDH-------DAERLRAAIAELEREKEKL 2606
Cdd:PRK01156 416 VKLQDISskvssLNQRIRALRENLDELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
...
gi 2044209144 2607 QEE 2609
Cdd:PRK01156 496 DEK 498
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2382-2510 |
1.30e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2382 EELSKLKARIEAENRALILRDKDNTQrfLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2461
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2462 AVQEATRLKAEA----ELLQQQKELAQEQARQLQ--------EDKEQMAQ----------QLAQETQGFQR 2510
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1830-1923 |
1.30e-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: 41.44 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1830 QRELAEQELEKQRQLAEGTAQQRLVAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEME 1909
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 2044209144 1910 VLLASKARAEEESR 1923
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1654-2027 |
1.42e-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: 45.00 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1654 KRQAEAELALRVKAEAEAAREKqralqaledvrLQAEEAERRLRQAEADRArqvqvaLETAQRSAEVELQSKRASFAEKT 1733
Cdd:NF033838 108 KEKSEAELTSKTKKELDAAFEQ-----------FKKDTLEPGKKVAEATKK------VEEAEKKAKDQKEEDRRNYPTNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1734 AQ-LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERwrlKANEALRL------RLQAEEvaqqkslaqaea 1806
Cdd:NF033838 171 YKtLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVES---KKAEATRLekiktdREKAEE------------ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1807 ekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRL----------------VAEQEL--IRLRAETEQ 1868
Cdd:NF033838 236 ---------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPatpdkkendakssdssVGEETLpsPSLKPEKKV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1869 GEQQRQLLE-EELARLQREA-----AAATHKRQELE-AEL-AKVR-AEMEVLLASKARAEEEsrstsEKSKQRLEAEASR 1939
Cdd:NF033838 307 AEAEKKVEEaKKKAKDQKEEdrrnyPTNTYKTLELEiAESdVKVKeAELELVKEEAKEPRNE-----EKIKQAKAKVESK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1940 frelAEEAARLralaEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAF 2019
Cdd:NF033838 382 ----KAEATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAE 453
|
410
....*....|
gi 2044209144 2020 Q--RRRLEEQ 2027
Cdd:NF033838 454 EdyARRSEEE 463
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1329-1612 |
1.44e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1329 LERWQAALAQTDVRQRELEQLGRQLryyrESADplgawlQDAKQRQERIQAVPLANSQAVREQLqqEKELLEEIERygeK 1408
Cdd:PRK11281 65 LEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES---R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1409 VDECQQLAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFIRETLR-R 1487
Cdd:PRK11281 130 LAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPSQRvL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1488 MEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAEREAEELQ------RRMQ-EEVARREEAAVDAQQ 1557
Cdd:PRK11281 197 LQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQeainskRLTLsEKTVQEAQSQDEAAR 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1558 QKRS--IQEELQHLRQSSEaeiqakaRQVEAAERSRVRIEEEIRvVRLQLE-ATERQR 1612
Cdd:PRK11281 274 IQANplVAQELEINLQLSQ-------RLLKATEKLNTLTQQNLR-VKNWLDrLTQSER 323
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1516-1678 |
1.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1516 QRQLAEAHAQAK---AQAEREAEELqrrmqeevarREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRV 1592
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAI----------KKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1593 RIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA--------QEEA-ERLRRQVQDEsqrkrqAEAELAL 1663
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEE------ARHEAAV 173
|
170
....*....|....*..
gi 2044209144 1664 RVKAEAEAARE--KQRA 1678
Cdd:PRK12704 174 LIKEIEEEAKEeaDKKA 190
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1482-1578 |
1.49e-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: 43.54 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1482 RETLRRMEEEERLAEQQRAEERERLAEV---------------EAALEKQRQLAEAHAQAKAQAEREAEE---------- 1536
Cdd:pfam13904 68 RQKELQAQKEEREKEEQEAELRKRLAKEkyqewlqrkarqqtkKREESHKQKAAESASKSLAKPERKVSQeeakevlqew 147
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2044209144 1537 LQRRMQEEVARREEaavdAQQQKRSIQEELQHLRQSSEAEIQ 1578
Cdd:pfam13904 148 ERKKLEQQQRKREE----EQREQLKKEEEEQERKQLAEKAWQ 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2380-2752 |
1.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2380 QMEELSKLKARieaeNRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQlAEEDLAQQRALAEKML--- 2456
Cdd:COG4717 54 EADELFKPQGR----KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-ELEELREELEKLEKLLqll 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2457 ---KEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRV 2533
Cdd:COG4717 129 plyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2534 AEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK------------VTLVHTLEIQRQQSDHDAERLRAAIAELER 2601
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2602 EKEKLQEEATLLQQKSEEMQVVQQEQLLqeTRALQESFLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQ 2681
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 2682 QQQMEQE---REQLVASMEEARQRQREAEEGV----RRKQEELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHRAA 2752
Cdd:COG4717 367 ELEQEIAallAEAGVEDEEELRAALEQAEEYQelkeELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL 444
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2873-2906 |
1.54e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.54e-03
10 20 30
....*....|....*....|....*....|....
gi 2044209144 2873 LLEAQAATGFLLDPVQNRRLTVNEAVKEGVVGPE 2906
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1351-1563 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1351 RQLRYYRESADPLGAWLQD--AKQRQEriqavpLANSQAVREQLQQEKELLEEIERYGEKVDECQQLAKQYINA---IKD 1425
Cdd:COG3206 164 QNLELRREEARKALEFLEEqlPELRKE------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1426 YELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------IRETLRRMEEEERLAEQQ 1498
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1499 RAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEE-------VARREEAAVDAQQQKRSIQ 1563
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2327-2554 |
1.54e-03 |
|
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: 44.63 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2327 QVEQELTTLRLQLEETDHQKSILD---EELQRLKAEVteAARQRNQVEEELFSVRVQMEELSKLKARIeaenralilrdk 2403
Cdd:pfam05701 230 QAEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAEL--AAYMESKLKEEADGEGNEKKTSTSIQAAL------------ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2404 DNTQRFLQEEAEKMKQVAEEAARLSVAAqeaARLRqlaeEDLAQQRA-LAEKMLKEKMQAVQEATrLKAEAELLQQQKEL 2482
Cdd:pfam05701 296 ASAKKELEEVKANIEKAKDEVNCLRVAA---ASLR----SELEKEKAeLASLRQREGMASIAVSS-LEAELNRTKSEIAL 367
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2483 AQEQARQLQEDKEQMAQQLAQETQgfqrtlEAERQRQLEMSAEAErlkLRVAEMSRAQARAEEDAQRFRKQA 2554
Cdd:pfam05701 368 VQAKEKEAREKMVELPKQLQQAAQ------EAEEAKSLAQAAREE---LRKAKEEAEQAKAAASTVESRLEA 430
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3829-3867 |
1.56e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 3829 YLYGTGCVAGVYLPGSRQTLTIYQALKKGLLNAEVARFL 3867
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1604-1729 |
1.56e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1604 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREK------- 1675
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVellnqqi 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1676 ---QRALQALEDVrLQAEEAERRLRQAE-ADRARQVQVALetAQRSAevELQSKRASF 1729
Cdd:PRK09039 147 aalRRQLAALEAA-LDASEKRDRESQAKiADLGRRLNVAL--AQRVQ--ELNRYRSEF 199
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1413-1735 |
1.62e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.62 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1413 QQLAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRYseLTTLTSQYIKFIRETLRRMEEEE 1492
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEY--LYELNVLKEKSEAELTSKTKKEL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1493 RLAEQQRAEERERLAEVEAalEKQRQLAEAHAQAKAQAEREAE----------ELQRRMQE-EVARREEAAVDAQQQKRS 1561
Cdd:NF033838 124 DAAFEQFKKDTLEPGKKVA--EATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEPR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1562 IQEELQHLRQSSEAEiQAKARQVEAAERSRVRIEEEIR---------------VVRLQLEATERQRGGAEGELQ------ 1620
Cdd:NF033838 202 DEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEAKrradaklkeaveknvATSEQDKPKRRAKRGVLGEPAtpdkke 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1621 ------------------ALRARAEEAEAQKRqaQEEAERLRRQVQDESQRKRQA------------------EAELALr 1664
Cdd:NF033838 281 ndakssdssvgeetlpspSLKPEKKVAEAEKK--VEEAKKKAKDQKEEDRRNYPTntyktleleiaesdvkvkEAELEL- 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 1665 VKAEAEAAREKQRALQALEDVRLQAEEAErRLRQAEADRARqvqvALETAQRSAEVELQSKrasfaEKTAQ 1735
Cdd:NF033838 358 VKEEAKEPRNEEKIKQAKAKVESKKAEAT-RLEKIKTDRKK----AEEEAKRKAAEEDKVK-----EKPAE 418
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2316-2758 |
1.68e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.51 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2316 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAEN 2395
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2396 RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2475
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2476 LQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2555
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2556 EIGEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQETRAL 2635
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2636 QESFLSEKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRKQE 2715
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2044209144 2716 ELQLLEQQRQQQERLLAEENQRLRERLQRLEEEHRAALAHSEE 2758
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2515-2839 |
1.73e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2515 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2575
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2576 HTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQLLQEtRALQESFLSEKDRLLQRERFIEQ 2655
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2656 EKAKLEQL------FRDEVAKAQKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEEGVRRkqeelqlleqqrqqqer 2729
Cdd:TIGR02168 335 LAEELAELeekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS----------------- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2730 lLAEENQRLRERLQRLEEEHRAALAHSEEiaasqaAASKALPNGRDVLDGPAAEAEPEHAFDGLRRKVPAQRLQEVGILS 2809
Cdd:TIGR02168 398 -LNNEIERLEARLERLEDRRERLQQEIEE------LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350
....*....|....*....|....*....|
gi 2044209144 2810 AEELQRLAQGRTTVAELAQREDVRQYLQGR 2839
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2301-2666 |
1.74e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2301 LKQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLE-ETDHQKSIL--DEELQRLKAEVTEAARQRNQVEEEL-FS 2376
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvELEELKKILaeDEKLLDEKKQFEKIAEELKGKEQELiFL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2377 VRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVaEEAARLSVAAQEAARLRQLA----------EEDLA 2446
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNI-ELTAHCDKLLLENKELTQEAsdmtlelkkhQEDII 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2447 QQRALAEKMLKEKMQAVQEATRLKAE-----AELLQQQKEL------AQEQARQLQ------------------------ 2491
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLRDElesvrEEFIQKGDEVkckldkSEENARSIEyevlkkekqmkilenkcnnlkkqi 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2492 EDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLrvaEMSRAQARAEEDAQRFRKQAEEigEKLHRTELATQEK 2571
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL---ELASAKQKFEEIIDNYQKEIED--KKISEEKLLEEVE 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2572 VTLVHTLEIQRQQSDHDaERLRAAIAELE--REKEKLQEEATLLQQKSEEMQVVQQEQLLQETRALQESFLSE-KDRLLQ 2648
Cdd:pfam05483 679 KAKAIADEAVKLQKEID-KRCQHKIAEMValMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNiKAELLS 757
|
410
....*....|....*...
gi 2044209144 2649 RERFIEQEKAKLEQLFRD 2666
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKME 775
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2464-2542 |
1.88e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.93 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044209144 2464 QEATRLKAEAELLQQQkeLAQEQARQLQeDKEQMAQQLAQETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2542
Cdd:PRK10920 60 QQAQNQTATNDALANQ--LTALQKAQES-QKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3164-3201 |
1.89e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2044209144 3164 LRGTSVIAGVWLEEAGQRLSIYEALKKDLLPPEVAVAL 3201
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1861-2113 |
1.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1861 RLRAETEQGEQQRQLLEEELARLQREAAAAthkrqelEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEAEAsrf 1940
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARA--- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1941 rELAEEAARLRALaeetkrQRQLAEEDAARQRAEAERVLAEKLAAISEAtrlktEAEIAlkekeaeneRLRRLAEDEAFQ 2020
Cdd:COG3206 234 -ELAEAEARLAAL------RAQLGSGPDALPELLQSPVIQQLRAQLAEL-----EAELA---------ELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2021 RRRLEEQaaqhKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAE 2100
Cdd:COG3206 293 VIALRAQ----IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
250
....*....|...
gi 2044209144 2101 DTLRSKEQAELEA 2113
Cdd:COG3206 369 SLLQRLEEARLAE 381
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1486-1730 |
2.01e-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: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEE 1565
Cdd:COG3064 60 AKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1566 LQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1645
Cdd:COG3064 140 ERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLAL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1646 QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSK 1725
Cdd:COG3064 220 AVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDD 299
|
....*
gi 2044209144 1726 RASFA 1730
Cdd:COG3064 300 SAALA 304
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2835-2873 |
2.01e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.01e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2044209144 2835 YLQGRSGIAGLLLKPANEKLSIYAALRRQLLSPGTALIL 2873
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1393-1552 |
2.04e-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: 42.99 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1393 QQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRtrySELTT 1472
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ---KEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1473 LTSQyikfiretLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAEELQRRMQEEVARREEAA 1552
Cdd:COG1579 101 LKRR--------ISDLEDEILELMERIEELEEELAELEAELAE---LEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1480-1696 |
2.10e-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: 42.74 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1480 FIRETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAEELQRRMQEEVARREEAAVDAQQQ- 1558
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRLEQQTEQAKKLEEKAQAALTKGNEEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1559 KRSIQEELQHLRQSSEAEIQAKARQVEAAERsrvrieeeirvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1638
Cdd:pfam04012 85 AREALAEKKSLEKQAEALETQLAQQRSAVEQ-----------LRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1639 EAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQaLEDVRLQAEEAERRL 1696
Cdd:pfam04012 154 LGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1512-1682 |
2.10e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1512 ALEKQRQLA--------EAHAQAKAQA-EREAE-ELQR-RMQEEVArreeaavdAQQQKRSIQEeLQHLRQSSEAEIQAK 1580
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARgRLERqKMHDKAK--------AEEQRTKLLE-LQAESAAVESSGQSR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1581 ARQVEAAERSRVRIEEEIRVVRLQLEAterQRGGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDESQR-KRQAE 1658
Cdd:PTZ00491 719 AEALAEAEARLIEAEAEVEQAELRAKA---LRIEAEAELEKLRKRQElELEYEQAQNELEIAKAKELADIEATKfERIVE 795
|
170 180
....*....|....*....|....*
gi 2044209144 1659 AELALRVKAEAEAAREKQ-RALQAL 1682
Cdd:PTZ00491 796 ALGRETLIAIARAGPELQaKLLGGL 820
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
1619-1728 |
2.13e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 42.03 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1619 LQALRARAEeaeaQKRQAQEEAERLRRQVQD---ESQRKR-QAEAELALRV-KAEAEAAREKQRALQALED-VRLQAEEA 1692
Cdd:PRK09173 28 ARSLDARAD----RIKNELAEARRLREEAQQllaEYQRKRkEAEKEAADIVaAAEREAEALTAEAKRKTEEyVARRNKLA 103
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2044209144 1693 ERRLRQAEAD-----RARQVQVALETAQRSAEVELQSKRAS 1728
Cdd:PRK09173 104 EQKIAQAETDainavRSSAVDLAIAAAEKLLAEKVDAKAAS 144
|
|
| 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 2044209144 213 LYEDLRDGHNLISLLEvlsgDSLP-------------REKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 279
Cdd:cd21294 38 LFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113
|
....*....
gi 2044209144 280 TLGLIWTII 288
Cdd:cd21294 114 ILGLIWQII 122
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1850-2059 |
2.25e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.94 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1850 QQRLvaeQELIRLRAETEQGEQQRQL---------------LEEELARLQREAAAATHKRQELEAELAKVRAEMEVLlas 1914
Cdd:pfam03528 7 QQRV---AELEKENAEFYRLKQQLEAefnqkrakfkelylaKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENI--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1915 KARAeeesrSTSEKSKQrlEAEASRFRELAEEAARLRALAEETKRQ------RQLAEEDA--ARQRAEAERVLAEKLAAI 1986
Cdd:pfam03528 81 KAVA-----TVSENTKQ--EAIDEVKSQWQEEVASLQAIMKETVREyevqfhRRLEQERAqwNQYRESAEREIADLRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 1987 SEATRlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVED 2059
Cdd:pfam03528 154 SEGQE-EENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRTD 225
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3569-3605 |
2.28e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.28e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2044209144 3569 KLLSAEKAVTGYKDPYSGSTISLFQAMKKGLVLREHG 3605
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1240-1534 |
2.31e-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: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1240 RSTQGAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRVQAEAQQPVFDALRDELRG-------AQEVGERLQRQHG 1312
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKrelerirQEEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1313 ERDVEVERWR--ERVAPLLERWQAALAQTDVRQRELEQLGRQLRYYR----ESADPLGAWLQDAKQRQ-ERIQAVPLANS 1385
Cdd:pfam17380 380 LERLQMERQQknERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRaeqeEARQREVRRLEEERAREmERVRLEEQERQ 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1386 QAVrEQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQlVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRT 1465
Cdd:pfam17380 460 QQV-ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 1466 RYSElttltsqyikfiRETLRRMEEEERLAEQQR--AEERERLAEVEAALEKQRQLAEAHaqaKAQAEREA 1534
Cdd:pfam17380 538 AEEE------------RRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMMRQIVESE---KARAEYEA 593
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2303-2562 |
2.33e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2303 QKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVR 2378
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2379 VQMEELSKL-----KARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQ 2447
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdelraKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2448 QRALAEKMLKEKMQAVQEATRL----KAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMS 2523
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRqelqQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2044209144 2524 AE---------AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLH 2562
Cdd:pfam13868 293 RElekqieereEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2330-2616 |
2.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2330 QELTTLRLQLEETDHQKSILDEELQRLKaevteaaRQRNQVEEELFSVRVQMEEL-SKLKARIEAENRALILRDKDNTQr 2408
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELK-------EKRDELNEELKELAEKRDELnAQVKELREEAQELREKRDELNEK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2409 fLQEEAEKMKQVAEEAARLSvaaQEAARLRQLAEEDLAQQRALAEkmLKEKMQAVQ-----EATRLKAEAELLQQQKELA 2483
Cdd:COG1340 73 -VKELKEERDELNEKLNELR---EELDELRKELAELNKAGGSIDK--LRKEIERLEwrqqtEVLSPEEEKELVEKIKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2484 QE-QARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAqaraeedAQRFRKQAEEigekLH 2562
Cdd:COG1340 147 KElEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-------ADELRKEADE----LH 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2563 RTELATQEKVTLVHTLEIQRQQSDHD------AERLRAAIAELEREKEKLQEEATLLQQK 2616
Cdd:COG1340 216 KEIVEAQEKADELHEEIIELQKELRElrkelkKLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| 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 2044209144 186 QKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALD 255
Cdd:cd21292 25 EKVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALN 102
|
90 100 110
....*....|....*....|....*....|...
gi 2044209144 256 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 288
Cdd:cd21292 103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1264-1674 |
2.45e-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: 43.90 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1264 ATLPELEATKAALKKLRVQAEAQQPVFDALRDELRGaqevgerLQRQHGERDVEVERWRERVAPLlerwQAALAQTDVRQ 1343
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAG-------LTRRLSAAEGELEELVARLAKL----EAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1344 RELEQLGRQLRYYRESADplgawlQDAKQRQERIQAVPLANsQAVREQLQQEKELLEEIERYGEKVDECQQLAKQyinai 1423
Cdd:pfam19220 107 EELRIELRDKTAQAEALE------RQLAAETEQNRALEEEN-KALREEAQAAEKALQRAEGELATARERLALLEQ----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1424 kdyelqlvtykaqlepvaspaKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIRETLRRMEEEERLAEQQRA--- 1500
Cdd:pfam19220 175 ---------------------ENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAqle 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1501 EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAK 1580
Cdd:pfam19220 234 EAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLERR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1581 ARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaeAE 1660
Cdd:pfam19220 310 TQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER---AE 386
|
410
....*....|....
gi 2044209144 1661 LALrVKAEAEAARE 1674
Cdd:pfam19220 387 RAL-AQGALEIARE 399
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1746-2201 |
2.51e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 44.24 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1746 AVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1825
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1826 QAVRQRElAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVR 1905
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1906 AEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAA 1985
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1986 ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRR 2065
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2066 QVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2145
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 2146 RQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2201
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2457-2619 |
2.55e-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: 43.79 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2457 KEKMQAVQEATRL-KAEAELLQ-QQKELAQEQARQLQEDKEQMAQQLAQEtqgfqrtLEAERQRQlemsaeAERLKLRVA 2534
Cdd:pfam15709 328 REQEKASRDRLRAeRAEMRRLEvERKRREQEEQRRLQQEQLERAEKMREE-------LELEQQRR------FEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2535 EMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvhtLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQ 2614
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL-----QELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLM 469
|
....*
gi 2044209144 2615 QKSEE 2619
Cdd:pfam15709 470 EMAEE 474
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2415-2509 |
2.55e-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: 43.43 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2415 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2488
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 2044209144 2489 QLQEDKEQMAQQLAQETQGFQ 2509
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| antiphage_ZorA_2 |
NF033915 |
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ... |
2410-2571 |
2.83e-03 |
|
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.
Pssm-ID: 411476 [Multi-domain] Cd Length: 383 Bit Score: 43.60 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2410 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRlkaeaellqQQKELAQEQARQ 2489
Cdd:NF033915 233 LQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVGNFMDGMTSAGR---------EQGLQMQQAAAD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2490 LQEDKEQMAQQLAQ--ETQGFQRTLEAERQRQL--EMSAEAERLklrvaeMSRAQARAEEDAQRFRKQAEEIGEKLHRTE 2565
Cdd:NF033915 304 VNAAVSGMSERLNQlfNSLSEQQGRQMERAQQQssTFETQLQRL------SGSANERQAQLEQRFEELMSGLTEQLQTQL 377
|
....*.
gi 2044209144 2566 LATQEK 2571
Cdd:NF033915 378 GAAQQR 383
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3904-3935 |
2.86e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.86e-03
10 20 30
....*....|....*....|....*....|..
gi 2044209144 3904 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLI 3935
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2301-2522 |
2.94e-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: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2301 LKQKQVADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEA-ARQRNQVEEELFSVRV 2379
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEkEREIARLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2380 QMEELSKLKARIEAENRALILRDKdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--- 2456
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKERQK---EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEdee 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 2457 KEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEM 2522
Cdd:pfam13868 276 IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1513-1719 |
3.00e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1513 LEKQRQLAEAHAQAKAQAEREAEELQRRMQEEvaRREEAAVDAQQQKRSIQEELQHLRQSSEaeiqakaRQVEAAERSRV 1592
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEE-------RLVQKEEQLDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1593 RIEEeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEAELALRVKAEAEaa 1672
Cdd:PRK12705 96 RAEK--------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2044209144 1673 REKQRALQALEdvrlqaEEAerrlrQAEADRARQVQVAlETAQRSAE 1719
Cdd:PRK12705 157 EEKAQRVKKIE------EEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1825-1968 |
3.05e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKV 1904
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 1905 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDA 1968
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
775-855 |
3.07e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.99 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 775 WLSEKEEEEVGFDWGEHNSNMAGKKESYSALMRELEVKEKKIKEIQSTGDRLLREGHPARPTVESFQAALQTQWSWMLQL 854
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 2044209144 855 C 855
Cdd:pfam00435 96 A 96
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
1470-1571 |
3.08e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 40.61 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1470 LTTLTSQYIKFIREtlrRMEEEERLAEQQraEERERLAEVEAALEKQRQLA-EAHAQAKAQAEREAEELQRRMQEEVARR 1548
Cdd:COG3599 29 LDEVAEDYERLIRE---NKELKEKLEELE--EELEEYRELEETLQKTLVVAqETAEEVKENAEKEAELIIKEAELEAEKI 103
|
90 100
....*....|....*....|...
gi 2044209144 1549 EEaavDAQQQKRSIQEELQHLRQ 1571
Cdd:COG3599 104 IE---EAQEKARKIVREIEELKR 123
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1502-1742 |
3.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1502 ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQeevarreeaavDAQQQKRSIQEELQHLRQSSEAEIQAka 1581
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLA-----------QAPAKLRQAQAELEALKDDNDEETRE-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1582 rqvEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEl 1661
Cdd:PRK11281 117 ---TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1662 aLRVKAEAE-AAREKQRALQALE---DVRLQA-EEAERRLRQAEADRARQVQVALETAqrsaeveLQSKRASFAEKTAQL 1736
Cdd:PRK11281 193 -QRVLLQAEqALLNAQNDLQRKSlegNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEA-------INSKRLTLSEKTVQE 264
|
....*.
gi 2044209144 1737 ERTLQE 1742
Cdd:PRK11281 265 AQSQDE 270
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1243-1725 |
3.11e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1243 QGAEEVLRAHEEQLKEAQAvpATLPELEATKAALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQHGERDV-EVERW 1321
Cdd:pfam12128 318 AKDRSELEALEDQHGAFLD--ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1322 RERVAPLLER--WQAALAQTDVRQREL---EQLGRQLRYYRESADPLGAWLQDAKQRQERIQAVP-----LANSQ----- 1386
Cdd:pfam12128 396 KDKLAKIREArdRQLAVAEDDLQALESelrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPelllqLENFDerier 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1387 ---------AVREQLQQEKELLEEI-ERYGEKVDECQQLAKQYINAIKDYELQLVT---------------YKAQLEPVA 1441
Cdd:pfam12128 476 areeqeaanAEVERLQSELRQARKRrDQASEALRQASRRLEERQSALDELELQLFPqagtllhflrkeapdWEQSIGKVI 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1442 SPAKKPKVQSGSESVIQEYVDLRTRYS---ELTTLTSQYIKFIRETLRR----MEEEERLAEQQRAEERERLAEVEAALE 1514
Cdd:pfam12128 556 SPELLHRTDLDPEVWDGSVGGELNLYGvklDLKRIDVPEWAASEEELRErldkAEEALQSAREKQAAAEEQLVQANGELE 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1515 KQRQLAEAHAQAKAQAER-------EAEELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAA 1587
Cdd:pfam12128 636 KASREETFARTALKNARLdlrrlfdEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1588 ERSRVRIEEEIRVVRLQL--EATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEaelalRV 1665
Cdd:pfam12128 716 KQAYWQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIA-----VR 790
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 1666 KAEAEAAREKQRALQALEDVRLQA--EEAERRLRQAEADRARQVQvalETAQRSAEVELQSK 1725
Cdd:pfam12128 791 RQEVLRYFDWYQETWLQRRPRLATqlSNIERAISELQQQLARLIA---DTKLRRAKLEMERK 849
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1481-1589 |
3.14e-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: 43.05 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 IRETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEahaqakaqAEREAEELQRRMQEEVARREeaavdA 1555
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIE--------AEKDAEVAKIQMQQKIMEKE-----A 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 2044209144 1556 QQQKRSIQEELQHLRQSS--EAEIQAKARQVEAAER 1589
Cdd:cd03406 224 EKKISEIEDEMHLAREKAraDAEYYRALREAEANKL 259
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2408-2608 |
3.37e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2408 RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2483
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2484 QEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARA----EEDAQRFRKQAEEIG 2558
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2044209144 2559 EKLHRTELATQEKVTLVHTLEIQRQQ------SDHDAERLRAAIAELErEKEKLQE 2608
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQ 337
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1627-1706 |
3.45e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1627 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL----RVKAE--AEAAREKQRALQA-LEDVRLQAEEAERRLRQA 1699
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAqqqeLVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 2044209144 1700 EADRARQ 1706
Cdd:PRK11448 218 RKEITDQ 224
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1161-1472 |
3.46e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1161 RECAQRIAEQQ----KAQAEVEGLGKGVARLSAEAEKVLALPEpspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTIS 1236
Cdd:TIGR02168 680 EELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELE------ELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1237 LVIRSTQGAEEVLRAHEEQLKEA-QAVPATLPELEATKA----ALKKLRVQAEAQQPVFDALRDELRGAQEVGERLQRQH 1311
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEElAEAEAEIEELEAQIEqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1312 GERDVEVERWRERVAPLLERwQAALAQtdvrqrELEQLGRQLryyRESADPLGAWLQDAKQRQERIQAVPLANSQAVREQ 1391
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSED-IESLAA------EIEELEELI---EELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1392 LQQEKELLEEIERYgekvDECQQLAKQYINAIKDYELQLVTYKAQL---------EPVASPAKKPKVQSGSE-------- 1454
Cdd:TIGR02168 904 RELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQERLseeysltleEAEALENKIEDDEEEARrrlkrlen 979
|
330 340
....*....|....*....|....*...
gi 2044209144 1455 ----------SVIQEYVDLRTRYSELTT 1472
Cdd:TIGR02168 980 kikelgpvnlAAIEEYEELKERYDFLTA 1007
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1838-2711 |
3.58e-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: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1838 LEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEaELAKVRAEMEVLLASKAR 1917
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD-PLKNRLKEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1918 AEEESRS--TSEKSKQRLEAEASRFRELAEEAA--RLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLk 1993
Cdd:TIGR00606 267 LDNEIKAlkSRKKQMEKDNSELELKMEKVFQGTdeQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1994 tEAEIALKEKEAENERLRRLAEDEAFQ--RRRLEEQAAQHKADIEErlaQLRKASENELERQkglvEDTLRQRRQVEEEi 2071
Cdd:TIGR00606 346 -LVEQGRLQLQADRHQEHIRARDSLIQslATRLELDGFERGPFSER---QIKNFHTLVIERQ----EDEAKTAAQLCAD- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2072 LALKASFEKAAAGKAELELE-LGRIRSNAEDTLrSKEQAELEATR-QRQLAAEEEQRRREAEERVQKSLAaeeeaarqRK 2149
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKgLGRTIELKKEIL-EKKQEELKFVIkELQQLEGSSDRILELDQELRKAER--------EL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2150 SALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEA 2229
Cdd:TIGR00606 488 SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2230 ARRAAEEAEEARERAEREAAQSRrqveeaERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQvaDA 2309
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTR------DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE--ES 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2310 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKA 2389
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2390 RIEAEnRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSvaaQEAARLRQLAEEdlaQQRALAEKMLKEKMqavqeatrl 2469
Cdd:TIGR00606 720 KKEKR-RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN---RDIQRLKNDIEE---QETLLGTIMPEEES--------- 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2470 kaeAELLQQQKELAQEQARQLQEDKEQMAQQLAQ-ETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQ 2548
Cdd:TIGR00606 784 ---AKVCLTDVTIMERFQMELKDVERKIAQQAAKlQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2549 RFRKQAEEIGEklHRTELATQEKvtlvhtleiQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQVVQQEQL 2628
Cdd:TIGR00606 861 HLKSKTNELKS--EKLQIGTNLQ---------RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2629 LQEtralqesflSEKDRLLQRERFIEQEKAKLEQLFRDEVAKaqKLREEQQRQQQQMEQEREQLVASMEEARQRQREAEE 2708
Cdd:TIGR00606 930 SSK---------ETSNKKAQDKVNDIKEKVKNIHGYMKDIEN--KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
...
gi 2044209144 2709 GVR 2711
Cdd:TIGR00606 999 DMR 1001
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1533-1671 |
3.61e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1533 EAEELQRRMqEEVARREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQR 1612
Cdd:COG0542 412 ELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 1613 GGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEAELALRVKAEAEA 1671
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1486-1736 |
3.63e-03 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 43.31 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEA---ALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARREEAAvdaqqQKRSI 1562
Cdd:pfam08017 49 RRQRDAENRSQGNVLERRQRDAENRSqgnVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDA-----ENKSQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1563 QEELQHLRQSSEAEIQAKA---RQVEAAERSRVRI-EEEIRVV--RLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1636
Cdd:pfam08017 124 GNVLERRQRDAENRSQGNVlerRQRDAENRSQGNVlERRQRDAenRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1637 QEEAERLRRQVQDESQ----RKRQAEAElalrVKAEAEAAREKQRALQAledvRLQAEEAERRLRQAEadrARQVQVALE 1712
Cdd:pfam08017 204 GNVLERRQRDAENRSQgnvlERRQRDAE----NRSQGNVLERRQRDAEN----KSQGNVLERRQRDAE---NRSQGNVLE 272
|
250 260
....*....|....*....|....*...
gi 2044209144 1713 TAQRSAEVELQ----SKRASFAEKTAQL 1736
Cdd:pfam08017 273 RRQRDAENRSQgnvlERRQRDAENKSQV 300
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2350-2570 |
3.75e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.43 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2350 DEELQRLKAEVTEAARQRnqVEEELfsVRVQMEELSKLKARIEAENRALILRDKDNTqrflqEEAEKMKQVAEEAARLSV 2429
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEE--ARKRL--VAKHGAEISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2430 AAQEAARLRQLAEEDLAQQRALAekmlkekmqavqeATRLKAEAELLQQQKELAQEQArqlqEDKEQMAQQLAQETQGFQ 2509
Cdd:PRK07735 75 AKQKREGTEEVTEEEKAKAKAKA-------------AAAAKAKAAALAKQKREGTEEV----TEEEKAAAKAKAAAAAKA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2510 RTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2570
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE 198
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1929-2091 |
3.81e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.59 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1929 SKQRLEAEASRFRELAEEAARLRALAEET-KRQRQLAEEDAARQRAEAERVLAEklaaISEATRLKTEAEIALKEKEAEn 2007
Cdd:pfam09731 304 AELKKREEKHIERALEKQKEELDKLAEELsARLEEVRAADEAQLRLEFEREREE----IRESYEEKLRTELERQAEAHE- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2008 ERLR-RLAEDEAFQRRR--------LEEQAAQHKADIEERLAQLrkaseNELERQKG---LVEDTLRQRRQVEEEILALK 2075
Cdd:pfam09731 379 EHLKdVLVEQEIELQREflqdikekVEEERAGRLLKLNELLANL-----KGLEKATSshsEVEDENRKAQQLWLAVEALR 453
|
170
....*....|....*.
gi 2044209144 2076 ASFEKAAAGKAELELE 2091
Cdd:pfam09731 454 STLEDGSADSRPRPLV 469
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2413-2548 |
3.83e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2413 EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2488
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044209144 2489 QLQEdkeqmaqqLAQETQgfQRTLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2548
Cdd:PTZ00491 761 QELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1542-1725 |
3.93e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.49 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1542 QEEVARREEAAVDAQQQKRsiqeelqhlrqsseaeiqaKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQA 1621
Cdd:PRK10811 589 QEQPAPKAEAKPERQQDRR-------------------KPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQ 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1622 LRARAEEAEAQKRQAQEEAERLRRQVQDESQR-----KRQAEAEL-ALRVKAEAEAA------------REKQRALQalE 1683
Cdd:PRK10811 650 TAETRESQQAEVTEKARTQDEQQQAPRRERQRrrndeKRQAQQEAkALNVEEQSVQEteqeervqqvqpRRKQRQLN--Q 727
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2044209144 1684 DVRLQ-AEEAERRLRQAEADRARQVQVALETAQRSAEVELQSK 1725
Cdd:PRK10811 728 KVRIEqSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLP 770
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1525-1701 |
3.96e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.95 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1525 QAKAQAEREA--EELQRRMQE------EVARREEAAVDAQQQKRSIQEELQ---HLRQSSEAEIQAKARQVEAAERsRVR 1593
Cdd:pfam15665 13 EAEIQALKEAheEEIQQILAEtrekilQYKSKIGEELDLKRRIQTLEESLEqheRMKRQALTEFEQYKRRVEEREL-KAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1594 IEEEIRVVRLQLEATERQRgGAEGELQALRARAEEAEAQKRQAQEEaerLRRQVQDESQRKRQAEAELALRVKAEAEAAR 1673
Cdd:pfam15665 92 AEHRQRVVELSREVEEAKR-AFEEKLESFEQLQAQFEQEKRKALEE---LRAKHRQEIQELLTTQRAQSASSLAEQEKLE 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 2044209144 1674 EKQRA-----LQALEDVRLQ----AEEAERRLRQAEA 1701
Cdd:pfam15665 168 ELHKAeleslRKEVEDLRKEkkklAEEYEQKLSKAQA 204
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1455-1648 |
4.00e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.95 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1455 SVIQEYVDLRTRYSELTTLTSQYIKFIRETLRRMEeeerlAEQQRAEERERLAEveaalekqrqlaEAHAQAKAQAEREA 1534
Cdd:pfam15665 43 SKIGEELDLKRRIQTLEESLEQHERMKRQALTEFE-----QYKRRVEERELKAE------------AEHRQRVVELSREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1535 EELQRRMQEEVARREEAAVDAQQQKRSIQEEL--QHLRQSSEAEIQAKARQVEAAErSRVRIEEEIRVvrlqleaterqr 1612
Cdd:pfam15665 106 EEAKRAFEEKLESFEQLQAQFEQEKRKALEELraKHRQEIQELLTTQRAQSASSLA-EQEKLEELHKA------------ 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2044209144 1613 ggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1648
Cdd:pfam15665 173 -----ELESLRKEVEDLRKEKKKLAEEYEQKLSKAQ 203
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1822-2260 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1822 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQgeQQRQLLEEELARLQREAAAATHKRQELEAEL 1901
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQ--RAAELAAEAAKKLAEAEKAAAEAEKKAAAEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1902 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAE 1981
Cdd:COG3064 98 AKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1982 KLAAISEATRL-KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDT 2060
Cdd:COG3064 178 AAAALVAAAAAaVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2061 LRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAA 2140
Cdd:COG3064 258 GVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2141 EEEAARQRKSALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSML 2220
Cdd:COG3064 338 EAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2044209144 2221 ERLRAEAEAARRAAEEAEEARERAEREAAQSRRQVEEAER 2260
Cdd:COG3064 418 VELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTG 457
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1604-2070 |
4.08e-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: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1604 QLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQaeaelalrvKAEAEAAREKQRALQALE 1683
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAA---------ELAAEAAKKLAEAEKAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1684 DVRLQAEEAERRLrQAEADRARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAE 1763
Cdd:COG3064 88 EAEKKAAAEKAKA-AKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1764 AERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1843
Cdd:COG3064 167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1844 LAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESR 1923
Cdd:COG3064 247 GAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1924 stsekSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 2003
Cdd:COG3064 327 -----LVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2004 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEE 2070
Cdd:COG3064 402 GLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKA 468
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2430-2610 |
4.11e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2430 AAQEAARLRQlaeedlaQQRALAEKMLKEKMQAVQEAtrlkaeAELLQQQkelAQEQARQLQEDKEQMAQQLAQETQGFQ 2509
Cdd:PRK09510 60 VVEQYNRQQQ-------QQKSAKRAEEQRKKKEQQQA------EELQQKQ---AAEQERLKQLEKERLAAQEQKKQAEEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2510 RTLEAERQRQLEMSAEAERlklrvaemSRAQARAEEDAQRFR---KQAEEIGEKLHRTELATQEKvtlvhtleiQRQQSD 2586
Cdd:PRK09510 124 AKQAALKQKQAEEAAAKAA--------AAAKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAKKAA---------AEAKKK 186
|
170 180
....*....|....*....|....
gi 2044209144 2587 HDAERLRAAIAELEREKEKLQEEA 2610
Cdd:PRK09510 187 AEAEAAAKAAAEAKKKAEAEAKKK 210
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1496-1599 |
4.18e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 42.47 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1496 EQQRAEERERLAEVEAALEKQRQLAEAHAqakaqAEREAEELQRRMQEEVARREEAAVDAQQQKRS-IQEELQHLRQSSE 1574
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARA-----AARAAASAAAAAAEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2044209144 1575 ----------------AEIQAkarQVEAAERSRVRIEEEIR 1599
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1625-1749 |
4.22e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1625 RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRalQALEdvrlQAEEAERRLRQAEADRA 1704
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEE----AAKQAALKQKQAEEAAA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2044209144 1705 RQVQVAletaqrSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQ 1749
Cdd:PRK09510 140 KAAAAA------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK 178
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2321-2611 |
4.31e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2321 TLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSKLKARIEAEnralIL 2400
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR----VA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2401 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQE-----------AARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEAT 2467
Cdd:pfam07888 84 ELKEELRQSREKHEELEEKYKELSASSEELSEEkdallaqraahEARIRELEEDikTLTQRVLERETELERMKERAKKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2468 RLKAE---------AELLQQQKELAQ-----EQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSA--------- 2524
Cdd:pfam07888 164 AQRKEeeaerkqlqAKLQQTEEELRSlskefQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAlleelrslq 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2525 --------EAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVHTLEIQRQQSDHDAERLRAA 2595
Cdd:pfam07888 244 erlnaserKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEADKDRIEKL 323
|
330
....*....|....*.
gi 2044209144 2596 IAELEREKEKLQEEAT 2611
Cdd:pfam07888 324 SAELQRLEERLQEERM 339
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1481-1723 |
4.36e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.36 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 IRETLRRMEEEERLAEQQrAEERERLAEvEAALEKQRQLAEAHaQAKAQAEREAEELQRRMQEEVARReeaavdaQQQKR 1560
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQ-VKQAVQMTE-EANFEKTKALIQCE-QLKSELERQKERLEKELASQQEKR-------AQEKE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1561 SIQEELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1640
Cdd:pfam15964 389 ALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1641 ERLRRQVQDESQrkrqaeaelalrvkaeaeaaREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEV 1720
Cdd:pfam15964 469 EKEHREYRTKTG--------------------RQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGES 528
|
...
gi 2044209144 1721 ELQ 1723
Cdd:pfam15964 529 EHQ 531
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2416-2572 |
4.36e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.32 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2416 KMKQvAEEAARLSV--AAQEAARLRQLAEEDLAQQRALAEKMLKEK-----MQAVQEAT--RLKAEAELLQQQKELAQEQ 2486
Cdd:PRK00106 25 KMKS-AKEAAELTLlnAEQEAVNLRGKAERDAEHIKKTAKRESKALkkellLEAKEEARkyREEIEQEFKSERQELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2487 ARQLQE------------DKEQMAQQLAQETQGFQRTLEaERQRQLEMSAEAERLKL-RVAEMSRAQARAEEDAQRFRKQ 2553
Cdd:PRK00106 104 SRLTERatsldrkdenlsSKEKTLESKEQSLTDKSKHID-EREEQVEKLEEQKKAELeRVAALSQAEAREIILAETENKL 182
|
170
....*....|....*....
gi 2044209144 2554 AEEIGEKLHRTELATQEKV 2572
Cdd:PRK00106 183 THEIATRIREAEREVKDRS 201
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1947-2091 |
4.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1947 AARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 2026
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044209144 2027 QAAQ------HKADIEERLAQLRKASENELERQKGLVEDTLRQR--RQVEEEILALKASFEKAAAGKAELELE 2091
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1488-1589 |
4.61e-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: 40.93 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1488 MEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHA-------QAKAQAEREAEELQRRMQEEVARREEAAvdaqqqK 1559
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEyEEKLAEARAeaaeiiaEARKEAEAIAEEAKAEAEAEAERIIAQA------E 102
|
90 100 110
....*....|....*....|....*....|
gi 2044209144 1560 RSIQEELQHLRQSSEAEIQAKArqVEAAER 1589
Cdd:COG0711 103 AEIEQERAKALAELRAEVADLA--VAIAEK 130
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1877-2118 |
4.69e-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: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1877 EEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQrleaeasrfreLAEEAARLRAlaEE 1956
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-----------LQAEIAEAEA--EI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1957 TKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA---FQRRRLEEQAAQHKA 2033
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAeleAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2034 DIEErLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEA 2113
Cdd:COG3883 162 LKAE-LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
....*
gi 2044209144 2114 TRQRQ 2118
Cdd:COG3883 241 AAAAS 245
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2407-2554 |
4.80e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2407 QRFLQEEAEKMKQVAEEAARLSVAAQEAAR---LRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2483
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 2484 QEQARQLQEDKEQMAQQLAQETQGFQR--TLEAERQRQL---EMSAEAER-LKLRVAEM-SRAQARAEEDAQRFRKQA 2554
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKLllkLLDAELEEeKAQRVKKIeEEADLEAERKAQNILAQA 185
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1481-1652 |
4.87e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 IRETLRRME-EEERLAEQQRAEERERLAEVEAALE-KQRQLAEAHAQAKAQAER------EAEELQRRMQEEVARREEAA 1552
Cdd:pfam05622 280 IREKLIRLQhENKMLRLGQEGSYRERLTELQQLLEdANRRKNELETQNRLANQRilelqqQVEELQKALQEQGSKAEDSS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1553 -----VDAQQQK-RSIQEELQHLRQSSE----AEIQAKARQVEAAERSRVRIEEEIRVV----RLQLEATE--------R 1610
Cdd:pfam05622 360 llkqkLEEHLEKlHEAQSELQKKKEQIEelepKQDSNLAQKIDELQEALRKKDEDMKAMeeryKKYVEKAKsviktldpK 439
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2044209144 1611 QRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ 1652
Cdd:pfam05622 440 QNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQEEK 481
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2376-2556 |
4.97e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2376 SVRVQMEELSKLKARIEAENRALI-----LRDKDNTQRFLQEEAEKMK------QVAEEAARLSVAAQEAARLRQ----- 2439
Cdd:PRK11637 62 SVRQQQQQRASLLAQLKKQEEAISqasrkLRETQNTLNQLNKQIDELNasiaklEQQQAAQERLLAAQLDAAFRQgehtg 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2440 -----LAEEDLAQQRALAekMLKEKMQAVQEA-TRLK-AEAELLQQQKELAQEQARQLQEDKEQMAQQ--LAQETQGFQR 2510
Cdd:PRK11637 142 lqlilSGEESQRGERILA--YFGYLNQARQETiAELKqTREELAAQKAELEEKQSQQKTLLYEQQAQQqkLEQARNERKK 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2511 TLEA------ERQRQL-EMSAEAERLKLRVAEMSR-AQARAEE---DAQRFRKQAEE 2556
Cdd:PRK11637 220 TLTGlesslqKDQQQLsELRANESRLRDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2028-2204 |
4.98e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2028 AAQHKADIEERLAQLRKasenELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE 2107
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2108 QAELE-ATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSA----------LEEVERLKAKVEEARRLRERAEQES 2176
Cdd:COG4942 94 ELRAElEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaparREQAEELRADLAELAALRAELEAER 173
|
170 180 190
....*....|....*....|....*....|
gi 2044209144 2177 ARQLQL--AQEAAQKRLQAEEKAHAFAVQQ 2204
Cdd:COG4942 174 AELEALlaELEEERAALEALKAERQKLLAR 203
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
1483-1583 |
5.02e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 41.46 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1483 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEevaRREEAAVD-------- 1554
Cdd:pfam06391 65 ETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKE---KAKQELIDelmtsnkd 141
|
90 100 110
....*....|....*....|....*....|....
gi 2044209144 1555 -----AQQQKRSIQEELQHLRQSSEAEIQAKARQ 1583
Cdd:pfam06391 142 aeeiiAQHKKTAKKRKSERRRKLEELNRVLEQKP 175
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1845-2341 |
5.08e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.31 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1845 AEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEEL-ARLQREAAAATHKRQELEAE---------LAKVRAEMEVLLAS 1914
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALaARALAALAALRHGNPPASARayanlglllLGDYEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1915 KARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKT 1994
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1995 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILAL 2074
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2075 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEE 2154
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2155 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAA 2234
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2235 EEAEEARERAEREAAQSRRQVEEAERLKQLAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQVADAEMEKH 2314
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 2044209144 2315 KKFAEQTLRQKAQVEQELTTLRLQLEE 2341
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2308-2674 |
5.34e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.97 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2308 DAEMEKHKkfaeqTLRQKAQVEQELTTLRLQLE-ETDHQKSILDEELQRLKAEVTeaaRQRNQVEEELFSVRVQMEELSK 2386
Cdd:pfam15964 346 EANFEKTK-----ALIQCEQLKSELERQKERLEkELASQQEKRAQEKEALRKEMK---KEREELGATMLALSQNVAQLEA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2387 LKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQLAEEDLAQQRALAEKMLKEKMQAVQea 2466
Cdd:pfam15964 418 QVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMK----KDEAEKEHREYRTKTGRQLEIKDQEIE-- 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2467 tRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRvaemsrAQARAEED 2546
Cdd:pfam15964 492 -KLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQ------AQQREQEL 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2547 AQRFRKQAEEIGEKLHRTELATQEKVTLVHTLE----IQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMqv 2622
Cdd:pfam15964 565 TQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKeeccTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEEL-- 642
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2623 vqqeqllqetralqesflseKDRLLQRERFIEQEKAKLEQLFRDEVAKAQKL 2674
Cdd:pfam15964 643 --------------------EEQCVQHGRMHERMKQRLRQLDKHCQATAQQL 674
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1503-1612 |
5.53e-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: 42.27 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1503 RERLAEVEAALEKQRQLAEAH-AQAKAQAEREAEELQRRMQEEVARREEAavDAQQQKRSIQEELQHLRQSSEAEIQAKA 1581
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEkAIEAERAKAEAAEAEQELLREKQKEEEQ--MMEAQERSYQEHVKQLIEKMEAEREQLL 260
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 1582 RQVEAAERSRVRIEEEIRVVRLQLEATERQR 1612
Cdd:pfam02841 261 AEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1553-1702 |
5.57e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1553 VDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrvrieeeirvvrlqleaterqrggAEGELQALRARAEEAEAQ 1632
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044209144 1633 KRQAQEEAERLRRQVQdesqrkrQAEAElalrvkaeaEAAREKQRALQALEdvRLQAEEAERR------LRQA--EAD 1702
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAK--RLELSEEETRilidqqLRKAgwEAD 252
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2329-2609 |
5.60e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2329 EQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRNQVEEELFSVRVQMEELSK----LKARIEAenralilrdkD 2404
Cdd:pfam15905 79 EKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRvnelLKAKFSE----------D 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2405 NTQRflqeeaekmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQAVQeaTRLKAEAELLQQQKELAQ 2484
Cdd:pfam15905 149 GTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQVTQ--KNLEHSKGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2485 EQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLhrt 2564
Cdd:pfam15905 209 STEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKC--- 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2044209144 2565 ELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEE 2609
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1860-2201 |
5.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1860 IRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASR 1939
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1940 FRELAEEAARLRALAEETKR-QRQLAEEDAARQRAEAERvlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA 2018
Cdd:COG4372 93 QAELAQAQEELESLQEEAEElQEELEELQKERQDLEQQR--KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2019 FQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 2098
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2099 AEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSALEEVERLKAKVEEARRLRERAEQESAR 2178
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
330 340
....*....|....*....|...
gi 2044209144 2179 QLQLAQEAAQKRLQAEEKAHAFA 2201
Cdd:COG4372 331 ALAILLAELADLLQLLLVGLLDN 353
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1481-1738 |
5.63e-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: 43.09 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1481 IRETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQR-RMQEEVARREEAAVDAQQQK 1559
Cdd:pfam05667 256 LRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAaTSSPPTKVETEEELQQQREE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1560 --RSIQEELQHLrqssEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEaterqrggaegELQALRARAEEAEAQKRQAQ 1637
Cdd:pfam05667 336 elEELQEQLEDL----ESSIQELEKEIKKLESSIKQVEEELEELKEQNE-----------ELEKQYKVKKKTLDLLPDAE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1638 EEAERLRRQVQDESQRKrqaeAELAlrvkAEAEAAR----EKQRALQalEDVRLQAEEAERRLRQAEADRaRQVQVALEt 1713
Cdd:pfam05667 401 ENIAKLQALVDASAQRL----VELA----GQWEKHRvpliEEYRALK--EAKSNKEDESQRKLEEIKELR-EKIKEVAE- 468
|
250 260
....*....|....*....|....*
gi 2044209144 1714 aqrsaevELQSKRASFAEKTAQLER 1738
Cdd:pfam05667 469 -------EAKQKEELYKQLVAEYER 486
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1486-1891 |
5.64e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1486 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAEELQRRMQEEVARREEAAVDAQQQKRSIQE 1564
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1565 ELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1644
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1645 RQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQS 1724
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1725 KRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQA 1804
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1805 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQ 1884
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*..
gi 2044209144 1885 REAAAAT 1891
Cdd:COG3064 424 LALAGAA 430
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1637-1961 |
5.67e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1637 QEEAERLRRQVQDESQRKRQAEAELA----LRVKAEAEAAREKQRALQALEDVRLQAEEA---------ERRLRQAEADR 1703
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSgqvtESVEPNEHNSYEEDSELKPSGQGGLDEEEAfldrtakreERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1704 ARQVQVALETAQRSAEVELQSKRASFAE-KTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKA 1782
Cdd:pfam02029 84 ERQKEFDPTIADEKESVAERKENNEEEEnSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1783 NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQEL-IR 1861
Cdd:pfam02029 164 EEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAeVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1862 LRAETEQGEQQRQLLEEElarlQREAAAATHKRQELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEASRfR 1941
Cdd:pfam02029 244 LEAEQKLEELRRRRQEKE----SEEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLREEEEK-R 316
|
330 340
....*....|....*....|
gi 2044209144 1942 ELAEEAARLRALAEEtKRQR 1961
Cdd:pfam02029 317 RMKEEIERRRAEAAE-KRQK 335
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1483-1610 |
5.69e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1483 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEEL-QRRMQEEVARREEAAVDAQQQKR 1560
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1561 SIQEELQHLRQSSEAeiqAKARQVEAAErsRVRIEEEIRVVRLQLEATER 1610
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAE--RQRQEREKIMQQEEQERLER 135
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4425-4455 |
5.70e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.31 E-value: 5.70e-03
10 20 30
....*....|....*....|....*....|.
gi 2044209144 4425 AGILDTETLEKVSITEAMRRNLVDNITGQRL 4455
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1832-2264 |
5.96e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1832 ELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVL 1911
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1912 LASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATR 1991
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1992 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASENELERQKGLVEDTLRQRRQVEEEI 2071
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2072 LALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEATRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKSA 2151
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2152 LEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAAR 2231
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|...
gi 2044209144 2232 RAAEEAEEARERAEREAAQSRRQVEEAERLKQL 2264
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAE 514
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1389-1630 |
6.12e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1389 REQLQQEKELLEEIERYGEKVDECQQLAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYS 1468
Cdd:COG1340 46 DELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1469 ELTTLTSQYIKFIRETLRRMEEEERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVARR 1548
Cdd:COG1340 126 QTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1549 EE---AAVDAQQQKRSIQEELQHLRQsseaeiqakarQVEAAERSRVRIEEEIRVVRLQLEATERQRggaegELQALRAR 1625
Cdd:COG1340 205 DElrkEADELHKEIVEAQEKADELHE-----------EIIELQKELRELRKELKKLRKKQRALKREK-----EKEELEEK 268
|
....*
gi 2044209144 1626 AEEAE 1630
Cdd:COG1340 269 AEEIF 273
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1489-2243 |
6.14e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1489 EEEERLAEQQRAEERErLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQEEVarreeaavdaqQQKRSIQEELQH 1568
Cdd:pfam05483 85 KEAEKIKKWKVSIEAE-LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEI-----------QENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1569 LRQSSEAEIQAKARQVEAAERSRVRiEEEIRVVRLQLEATERQRGGAegeLQALRARAEEAEAQKR-QAQEEAERLRRQV 1647
Cdd:pfam05483 153 TRHLCNLLKETCARSAEKTKKYEYE-REETRQVYMDLNNNIEKMILA---FEELRVQAENARLEMHfKLKEDHEKIQHLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1648 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVELQSKRA 1727
Cdd:pfam05483 229 EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1728 SFAEKTaqLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEQELERWRLKANEALRL---RLQAEEvAQQKSLAQA 1804
Cdd:pfam05483 309 MSTQKA--LEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNE-DQLKIITME 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1805 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQE--LEKQRQLaEGTAQQRLVAEQELIRLRaeteqgeqqrQLLEEELAR 1882
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEklLDEKKQF-EKIAEELKGKEQELIFLL----------QAREKEIHD 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1883 LQREAAAATHKRQELEAELAKVRAEMEvllaskARAEEESRSTSEKSKQRLEAeasrfRELAEEAARLralAEETKRQrq 1962
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTELE------KEKLKNIELTAHCDKLLLEN-----KELTQEASDM---TLELKKH-- 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1963 laEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEkeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 2042
Cdd:pfam05483 519 --QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE-------FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2043 rKASENELERQKGLVEDTLRQRRQVEEEILALKasfEKAAAGKAELelelgrirsNAEDTLRSKEQAELEATRQRqlaae 2122
Cdd:pfam05483 590 -KILENKCNNLKKQIENKNKNIEELHQENKALK---KKGSAENKQL---------NAYEIKVNKLELELASAKQK----- 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2123 eeqrRREAEERVQKSLaaeEEAARQRKSALEEVERLKAKVEEARRLRE----RAEQESARQLQLAQEAAQK--RLQAEEK 2196
Cdd:pfam05483 652 ----FEEIIDNYQKEI---EDKKISEEKLLEEVEKAKAIADEAVKLQKeidkRCQHKIAEMVALMEKHKHQydKIIEERD 724
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 2044209144 2197 AHAFAVQQKEQELQQTLQQEQSMLERLRAEAEAARRAAEEAEEARER 2243
Cdd:pfam05483 725 SELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1870-2061 |
6.20e-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: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1870 EQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAA- 1948
Cdd:cd00176 18 EKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1949 RLRALAEETKRQRQLAEEDAARQRAEAervlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED----EAFQRRRL 2024
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADDLEQWLEE----KEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRlkslNELAEELL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2044209144 2025 EEQAAQHKADIEERLAQLRKASEN---ELERQKGLVEDTL 2061
Cdd:cd00176 174 EEGHPDADEEIEEKLEELNERWEElleLAEERQKKLEEAL 213
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1500-1742 |
6.34e-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: 41.52 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1500 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAEELQRRMQeevarreeaavDAQQQKRSIQEELQHLRQSSEAEIQA 1579
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1580 KARqveaaersrvrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEA 1659
Cdd:pfam12795 74 ILA-------------------SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1660 EL---ALRVKAEAEAAREKQRALQALEDVRLQAEEAE-------RRLRQAEADRARQVQVALETAQRSAEVELQSKRASF 1729
Cdd:pfam12795 135 RLngpAPPGEPLSEAQRWALQAELAALKAQIDMLEQEllsnnnrQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQE 214
|
250
....*....|....
gi 2044209144 1730 AEKT-AQLERTLQE 1742
Cdd:pfam12795 215 AEQAvAQTEQLAEE 228
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
192-287 |
6.59e-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: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 192 KWVNKHLikhWRAEAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN- 266
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYf 91
|
90 100
....*....|....*....|.
gi 2044209144 267 IRNDDIADGNPKLTLGLIWTI 287
Cdd:cd21218 92 LTPEDIVSGNPRLNLAFVATL 112
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2333-2524 |
6.63e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2333 TTLRLQLEETDHQKSILDEELQRLKAEV----TEAARQRNQVEEELFSVRvqmEELSKLKARIEAENRAliLRDKDNTQR 2408
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIqqlrTELQELEAQQQEEAESSR---EQLQELEEQLATERSA--RREAEAELE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2409 FLQEEaekMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQraLAEKMLKEKMQAVQEAtRLKAEAELLQQQkelaQEQAR 2488
Cdd:pfam09787 118 RLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQ--LTSKSQSSSSQSELEN-RLHQLTETLIQK----QTMLE 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 2044209144 2489 QLQEDKEQMAQQLAQ-ETQGFQRTLEAERQRQLEMSA 2524
Cdd:pfam09787 188 ALSTEKNSLVLQLERmEQQIKELQGEGSNGTSINMEG 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2399-2839 |
6.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2399 ILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2472
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2473 AELLQQQKELAQ---EQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQR 2549
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2550 FRKQAEEIGEKLHRTELATQEKVTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKLQEEATLLQQKSEEMQvvqqeqll 2629
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-------- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2630 qetrALQESFLSEKDRLLQRERFIEqekAKLEQLfRDEVAKAQKLREE--------------QQRQQQQMEQEREQLVAS 2695
Cdd:PRK02224 412 ----DFLEELREERDELREREAELE---ATLRTA-RERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2696 MEEARQRQREAEEGVRRKQEELQLLEQQRQQQERLL------AEENQRLRERLQRLEEEHRAALAHSEEIAASQaaaska 2769
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREdleeliAERRETIEEKRERAEELRERAAELEAEAEEKR------ 557
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044209144 2770 lpngrdvldgpAAEAEPEHAFDGLRRKVPA--QRLQEVgilsAEELQRLAQGRTTVAELAQREDVRQYLQGR 2839
Cdd:PRK02224 558 -----------EAAAEAEEEAEEAREEVAElnSKLAEL----KERIESLERIRTLLAAIADAEDEIERLREK 614
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1960-2117 |
7.22e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1960 QRQLAE--EDAARQRAEAERvlaEKLAAISEATRLKTEAEIA-----LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 2032
Cdd:COG2268 191 RRKIAEiiRDARIAEAEAER---ETEIAIAQANREAEEAELEqereiETARIAEAEAELAKKKAEERREAETARAEAEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2033 ADIEErlAQLRKASENELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELElgrirsnaedtlrskEQAELE 2112
Cdd:COG2268 268 YEIAE--ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE---------------AEAEAE 330
|
....*
gi 2044209144 2113 ATRQR 2117
Cdd:COG2268 331 AIRAK 335
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2302-2487 |
7.52e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2302 KQKQVADAEMEKHKKFAEQT--LRQKAQVEQElttlRLQLEEtdhQKSILDEELQRLKAEVTEAARQRNQVEEElfsVRV 2379
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLE---KERLAAQEQKKQAEEAAKQAALKQKQAEE---AAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2380 QMEELSKLKAriEAENRALilrdkdntqrflqeeAEKMKQVAEEAARLSVAAQEAarlrQLAEEdlAQQRALAEkmlkEK 2459
Cdd:PRK09510 140 KAAAAAKAKA--EAEAKRA---------------AAAAKKAAAEAKKKAEAEAAK----KAAAE--AKKKAEAE----AA 192
|
170 180
....*....|....*....|....*...
gi 2044209144 2460 MQAVQEAtRLKAEAELLQQQKELAQEQA 2487
Cdd:PRK09510 193 AKAAAEA-KKKAEAEAKKKAAAEAKKKA 219
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1674-2071 |
7.75e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1674 EKQRALQALEDVRLQAEEAERRLRQAEA-------DRARQVQVALETAQRsaEVELQSKRASFAEKTAQLERTLQEEHVA 1746
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQRMRELQQQAAlaweelrRRDQKRQETLERERR--LLLQQSQEQWQAEKEQRKARLGREERRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1747 VAQLREEAERRAqqqaeaerareeaeqelERWRLKANEALRLRLQAEEVAQQkslaqaeaekqkeeaerearrrgkaeeq 1826
Cdd:pfam15558 82 ADRREKQVIEKE-----------------SRWREQAEDQENQRQEKLERARQ---------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1827 avrqrelaEQELEKQRQlaegtaQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRA 1906
Cdd:pfam15558 117 --------EAEQRKQCQ------EQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1907 eMEVLLASKARAEEESRSTS-EKSKQRLEAEASRFRELAEEAARLRALAEETKRQR-QLAEEDAARQRAEAERVLAEK-- 1982
Cdd:pfam15558 183 -RKVLVDCQAKAEELLRRLSlEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRaKWRAEEKEEERQEHKEALAELad 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1983 ---LAAISEATRLKTEAEIALKEKEAENERLRRL----AEDEAFQRRRLEEQAAQHKadiEERLAQLRKASENELERQKG 2055
Cdd:pfam15558 262 rkiQQARQVAHKTVQDKAQRARELNLEREKNHHIlklkVEKEEKCHREGIKEAIKKK---EQRSEQISREKEATLEEARK 338
|
410
....*....|....*.
gi 2044209144 2056 LVEDTLRQRRQVEEEI 2071
Cdd:pfam15558 339 TARASFHMREKVREET 354
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1521-1700 |
8.01e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1521 EAHAQAKAQAEREAEELQRRMQEEVARREEAAVDAQQQkrsiQEELQHLRQSSEAEIQAKARQVEAAERSrvrIEEEIRV 1600
Cdd:TIGR00927 633 GDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQE----GETETKGENESEGEIPAERKGEQEGEGE---IEAKEAD 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1601 VRLQLEATERQRGGA--------EGELQAlrarAEEAEAQKRQAQEEAERlRRQVQDESQRKrqaEAELALRVKAEAEAA 1672
Cdd:TIGR00927 706 HKGETEAEEVEHEGEteaegtedEGEIET----GEEGEEVEDEGEGEAEG-KHEVETEGDRK---ETEHEGETEAEGKED 777
|
170 180
....*....|....*....|....*...
gi 2044209144 1673 rEKQRALQALEDVRLQAEEAERRLRQAE 1700
Cdd:TIGR00927 778 -EDEGEIQAGEDGEMKGDEGAEGKVEHE 804
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1594-1933 |
8.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1594 IEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR 1673
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1674 EKQRALQALEDVRLQAEEAERRLRQAEADRARQVQVALETAQRSAEVE--LQSKRASFAEKTAQLERTLQEEHVAVAQLR 1751
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeqLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1752 EEAERRAQQQAEAERAREEAEQELERWRLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1831
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1832 ELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKVRAEMEVL 1911
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|..
gi 2044209144 1912 LASKARAEEESRSTSEKSKQRL 1933
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVADG 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1825-1990 |
8.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1825 EQAVRQRELAEQELEKQRQLAEGTAQQRLVAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATHKRQELEAELAKV 1904
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1905 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLA 1984
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 2044209144 1985 AISEAT 1990
Cdd:COG3883 275 GAAAAS 280
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1585-1701 |
8.11e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1585 EAAerSRVRIE-----EEIRVVRLQLEATERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDESQRKRQAEA 1659
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA 461
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2044209144 1660 elalRVKAEAEAAREKQRALQALEDVRLQAEEAERRLRQAEA 1701
Cdd:COG0542 462 ----RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEE 499
|
|
| 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 2044209144 185 VQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHR 260
Cdd:cd21306 16 VVKKSLITFVNKHLNK-----LNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDA 90
|
90 100 110
....*....|....*....|....*....|.
gi 2044209144 261 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 291
Cdd:cd21306 91 GLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2380-2677 |
8.43e-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: 41.83 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2380 QMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQ----EAARLRQLAEED--------LAQ 2447
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqieEREQKRQEEYEEklqereqmDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2448 QRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARQLQEDKEQMAQQLAQETQGFQRTLEAERQRQlEMSAEAE 2527
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI-EEEKERE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2528 RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK-VTLVHTLEIQRQQSDHDAERLRAAIAELEREKEKL 2606
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKkARQRQELQQAREEQIELKERRLAEEAEREEEEFER 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044209144 2607 QEEATLLQQKSEEMQVVQQEQLLQETRALQESFLSEKDRLLQRERfieqekakleqlfRDEVAKAQKLREE 2677
Cdd:pfam13868 266 MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER-------------EEELEEGERLREE 323
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1913-2199 |
8.83e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.44 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1913 ASKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEETKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRL 1992
Cdd:pfam09731 101 VAEEEKEATKDAAEAKAQLPKSEQE---KEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1993 KTEAEIALKEKEAENERLRRLAEDeafQRRRLEEQAAQHKADIEERLAQLRKASENELE-----RQKGLVEDTLRQRRQV 2067
Cdd:pfam09731 178 EKATDSALQKAEALAEKLKEVINL---AKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEkvekaQSLAKLVDQYKELVAS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2068 EEEILA--LKASFEKAAAGKAELELelgrIRSNAEDTLRSKEQAELEATrQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2145
Cdd:pfam09731 255 ERIVFQqeLVSIFPDIIPVLKEDNL----LSNDDLNSLIAHAHREIDQL-SKKLAELKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2146 RQRKSALEEV-----ERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2199
Cdd:pfam09731 330 EELSARLEEVraadeAQLRLEFEREReEIRESYEEKLRTELERQAEAHEEHLKDVLVEQE 389
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1454-1618 |
9.01e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1454 ESVIQEYVDLRTRYSELTTLTSQYIKFIRETLRRMEEEERLaeqQRAEERERLAEVEAALEKQRQLAEAHAQAKAQaere 1533
Cdd:pfam09787 64 QKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLAT---ERSARREAEAELERLQEELRYLEEELRRSKAT---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1534 aeeLQRRMQ--EEVARREEAAVDAQQQKRSIQEEL-QHLRQSSEAEIQaKARQVEAaersrvrIEEEIRVVRLQLEATER 1610
Cdd:pfam09787 137 ---LQSRIKdrEAEIEKLRNQLTSKSQSSSSQSELeNRLHQLTETLIQ-KQTMLEA-------LSTEKNSLVLQLERMEQ 205
|
....*...
gi 2044209144 1611 QRGGAEGE 1618
Cdd:pfam09787 206 QIKELQGE 213
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1504-1675 |
9.28e-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: 40.32 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1504 ERLAEVEAALEK-QRQLAEAHAQAKAQAEREAEELQRRMQ---EEVARREEAAVDAQQQKrsIQEELQHLRQsseaeiQA 1579
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQkdlEEVRAKLEPYLEELQAK--LGQNVEELRQ------RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1580 KARQVEAAERSRVRIEEEIRVVRlqlEATERQRGGAEGELQALRARAEEAEAQKRQ-----AQEEAERLRRQVQDESQRK 1654
Cdd:pfam01442 76 EPYTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPYAEELRQklaerLEELKESLAPYAEEVQAQL 152
|
170 180
....*....|....*....|.
gi 2044209144 1655 RQAEAELALRVKAEAEAAREK 1675
Cdd:pfam01442 153 SQRLQELREKLEPQAEDLREK 173
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1489-1676 |
9.48e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.29 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1489 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAE-----ELQRR--------MQEEVARREEAAVDA 1555
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERKGEqegegEIEAKeadhkgetEAEEVEHEGETEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 1556 QQQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAERSRVRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1630
Cdd:TIGR00927 726 TEDEGEIEtgEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2044209144 1631 AQKRQAQEEAERlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ 1676
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2349-2615 |
9.88e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2349 LDEELQRLKAEVTEAarqRNQVEE-ELFSVRVQMEELSK--------LKARIEAENRalILRDKDNTQRFLQEEAEKMKQ 2419
Cdd:PRK04778 254 IEKEIQDLKEQIDEN---LALLEElDLDEAEEKNEEIQEridqlydiLEREVKARKY--VEKNSDTLPDFLEHAKEQNKE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2420 VAEEAARLSvaaqeaaRLRQLAEEDLAQQRALaEKMLKEkmqavqeatrlkAEAELLQQQKELAQEQAR--QLQEDKEQM 2497
Cdd:PRK04778 329 LKEEIDRVK-------QSYTLNESELESVRQL-EKQLES------------LEKQYDEITERIAEQEIAysELQEELEEI 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044209144 2498 AQQLAqetqgfqrtleaerqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL----------- 2566
Cdd:PRK04778 389 LKQLE------------------EIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNLpglpedylemf 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2044209144 2567 -ATQEKV-TLVHTLEIQR------QQSDHDAErlrAAIAELEREKEKLQEEATLLQQ 2615
Cdd:PRK04778 451 fEVSDEIeALAEELEEKPinmeavNRLLEEAT---EDVETLEEETEELVENATLTEQ 504
|
|
| |
