|
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 ... |
178-282 |
1.96e-76 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 249.24 E-value: 1.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 178 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 257
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1820553714 258 RNDDIADGNPKLTLGLIWTIILHFQ 282
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
175-293 |
1.63e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 241.47 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 254
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1820553714 255 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 293
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
173-291 |
6.06e-72 |
|
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: 237.19 E-value: 6.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 173 ATDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQV 252
Cdd:cd21236 10 YKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQV 89
|
90 100 110
....*....|....*....|....*....|....*....
gi 1820553714 253 KLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 291
Cdd:cd21236 90 KLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
295-400 |
6.50e-72 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 236.46 E-value: 6.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 295 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 374
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1820553714 375 PEDVDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
296-400 |
5.47e-66 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 219.19 E-value: 5.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 375
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1820553714 376 EDVDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
175-292 |
1.86e-63 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 212.59 E-value: 1.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 254
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1820553714 255 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 292
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
296-400 |
2.55e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.43 E-value: 2.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 375
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1820553714 376 EDVDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
294-400 |
1.18e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 178.31 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 294 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 373
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1820553714 374 DPEDVDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
180-283 |
1.23e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 175.65 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 180 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 258
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1820553714 259 NDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
175-279 |
1.14e-47 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 167.54 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 253
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1820553714 254 LVNIRNDDIADGNPKLTLGLIWTIIL 279
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
296-396 |
7.53e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 161.81 E-value: 7.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 375
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1820553714 376 EDVDVPQPDEKSIITYVSSLY 396
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
1.92e-45 |
|
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: 159.99 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 7 MPRDQLRAIYEVLFREGVMVAKKDRRPrSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWCHFYWYLTNEGIAHLRQYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKDFNL-PKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 1820553714 87 HLPPEIVPASLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
179-396 |
2.81e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 176.28 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 179 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 255
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLFNAII 334
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 335 HRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 396
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
176-283 |
2.55e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.54 E-value: 2.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 251
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1820553714 252 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
296-396 |
5.18e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 375
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1820553714 376 EDVDVPQPDEKSIITYVSSLY 396
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
175-279 |
6.52e-44 |
|
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: 156.69 E-value: 6.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLrHRQVK 253
Cdd:cd21193 11 EERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKVR 89
|
90 100
....*....|....*....|....*.
gi 1820553714 254 LVNIRNDDIADGNPKLTLGLIWTIIL 279
Cdd:cd21193 90 LENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
176-283 |
9.65e-44 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 156.19 E-value: 9.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 248
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1820553714 249 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1818-2386 |
1.90e-41 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 168.58 E-value: 1.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1897
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1898 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEE---DAARQRAEAERVLAE 1974
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1975 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKgLVEDTL 2054
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2055 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAE 2134
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2135 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2209
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2210 QSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQA 2289
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2290 EQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFS 2369
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 1820553714 2370 VRVQMEELSKLKARIEA 2386
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
295-400 |
3.12e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 148.62 E-value: 3.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 295 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 374
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1820553714 375 PEDVDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
283-398 |
5.90e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 148.28 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 283 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 362
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 363 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
165-279 |
3.19e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 147.09 E-value: 3.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 165 RPGPEPAPA------------TDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGR 231
Cdd:cd21318 11 RPWDEPAATaklfecsrikalADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGR 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1820553714 232 MRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 279
Cdd:cd21318 91 MRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
175-279 |
4.67e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 143.27 E-value: 4.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 253
Cdd:cd21317 26 DEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKVH 105
|
90 100
....*....|....*....|....*.
gi 1820553714 254 LVNIRNDDIADGNPKLTLGLIWTIIL 279
Cdd:cd21317 106 LENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
178-279 |
8.49e-39 |
|
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: 141.76 E-value: 8.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 178 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 256
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1820553714 257 IRNDDIADGNPKLTLGLIWTIIL 279
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1455-2030 |
1.25e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 159.72 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1455 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEErERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRM 1534
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-AELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1535 QEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQA 1614
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1615 LRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1694
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1695 ERArqvqvALETAQRSAEAELQSKRASFAEKTAQLERSLQeehvavAQLREEAERRAQQQAEAERAREEAERELERWQLK 1774
Cdd:COG1196 464 LLA-----ELLEEAALLEAALAELLEELAEAAARLLLLLE------AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1775 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1854
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1855 LRAETEQGEqqrqLLEEELARLQHEAAAATQKRqeLEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1934
Cdd:COG1196 613 ARYYVLGDT----LLGRTLVAARLEAALRRAVT--LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1935 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 2014
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|....*.
gi 1820553714 2015 RRLEEQAAQHKADIEE 2030
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
292-396 |
1.52e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 141.30 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 292 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 371
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1820553714 372 LLDPEDVDVPQPDEKSIITYVSSLY 396
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
176-283 |
1.63e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 141.12 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 253
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1820553714 254 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
180-281 |
1.95e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 180 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 257
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1820553714 258 RNDDIADGNPKLTLGLIWTIILHF 281
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
292-396 |
5.70e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.81 E-value: 5.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 292 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 371
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1820553714 372 LLDPEDVDVPQPDEKSIITYVSSLY 396
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1488-2110 |
8.48e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 157.02 E-value: 8.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1488 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAKELQQRMQEevvRREEAAVdaqQQKRSIQEELQQLrqss 1566
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELKEELKE---LEAELLL---LKLRELEAELEEL---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1567 EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAterqrggAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQR 1646
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1647 KRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALEtaQRSAEAELQSKRASFAEKT 1726
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1727 AQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEA 1806
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1807 EREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQHEAAAA 1883
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1884 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA-----LAEEAKRQRQLAE 1958
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtlLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1959 EDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 2038
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 2039 SDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRsnaedtlrsKEQAELEAARQR 2110
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE---------RELERLEREIEA 778
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
295-396 |
3.12e-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: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 295 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 374
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1820553714 375 PEDVDVPQPDEKSIITYVSSLY 396
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
175-283 |
6.22e-37 |
|
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: 136.59 E-value: 6.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 253
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1820553714 254 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1578-2186 |
2.53e-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: 2.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1578 EAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR 1657
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1658 VKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEH 1737
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1738 VAVAQLreeaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE 1817
Cdd:COG1196 341 ELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1897
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1898 RAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1974
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1975 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasDSELERQKGLVEDtL 2054
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL--EAALRRAVTLAGR-L 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2055 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAE 2134
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 2135 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2186
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1482-2188 |
4.91e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 152.60 E-value: 4.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1482 EEEERLAEQQRAEERERLAEVEAALEkqrqlaeahAQAKAQAEREAKELqqRMQEEVVRREEAAVDAQQQKRSIQEELQQ 1561
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEE---------AKKKAEDARKAEEA--RKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1562 LRQSSEAEIQAKARQAEAAERS-RLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQK-------RQAQEEA 1633
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAeEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeaKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1634 ERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqalEELRlQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1713
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1714 ELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRlqAEEVAQQKS 1793
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--AEEKKKADE 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1794 LAQaeaekqkeeaerearrrgKAEEQAVRHRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQLLE-- 1870
Cdd:PTZ00121 1396 AKK------------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEea 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1871 ---EELARLQHEAAAATQKRQELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARL 1943
Cdd:PTZ00121 1457 kkaEEAKKKAEEAKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEA 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1944 RAlAEEAKRQRQLAEEDAARQRAEAERvlAEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ 2023
Cdd:PTZ00121 1528 KK-AEEAKKADEAKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2024 HKADIEERLAQLRKASDSELERQKGLVEDTLRQRrqveEEILALKASFEKAAAGKAELELELGRIRS-----NAEDTLRS 2098
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEEDKKK 1676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2099 KEQA--ELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQ 2172
Cdd:PTZ00121 1677 AEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
730
....*....|....*.
gi 1820553714 2173 LQLAQEAAQKRLQAEE 2188
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEE 1772
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
299-400 |
9.11e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 132.94 E-value: 9.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 299 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 377
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1820553714 378 VDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
280-396 |
4.02e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.10 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 280 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 359
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 360 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 396
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1620-2215 |
1.43e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 146.62 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAEAQKRQAQEEAERL---RRQVqdESQRKRqaeaelalrVKAEAEAAREKQRALQALEE-------LRLQAEEAERRL 1689
Cdd:COG1196 175 EEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKEleaelllLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1690 RQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELE 1769
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1770 RWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAE 1849
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1850 QELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAE 1929
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1930 AGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA----AISEATRLKTEAEIALKEKEAENERLRR 2005
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2006 LAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELEL 2085
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2086 GRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERA 2165
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2166 EQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDR 2215
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1920-2603 |
4.91e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 144.69 E-value: 4.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1920 EKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLaaisEATRLKTEAEIALKEKEAE 1999
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2000 NERLRRLAEDEAFQRRRLEEQAAqhkadiEERLAQLRKASDSELERQkglvEDTLRQRRQVEEEILALKASFEKAAAGKA 2079
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYEL------LAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2080 ELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAkvEEAR 2159
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE--RLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2160 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAER 2239
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2240 EAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAAdaemekhkkfAEQTLRQKA 2319
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA----------AAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2320 QVEQELTTLRLqleETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNT 2399
Cdd:COG1196 569 AKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2400 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2479
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2480 ARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQL----EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgeklh 2555
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL----- 800
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1820553714 2556 rtelaTQEKVTLVQTLEiqrqqsdhdaeRLREAIAELEREKEKLQQEA 2603
Cdd:COG1196 801 -----SEQREDLEEARE-----------TLEEAIEEIDRETRERFLET 832
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
179-284 |
7.78e-34 |
|
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: 128.34 E-value: 7.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 179 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 255
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHFQIS 284
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-143 |
2.84e-33 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 126.68 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 5 MLMPRDQLRAIYEVLFREGVMVAKKDRrPRSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWCHFYWYLTNEGIAHLRQ 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKDP-KGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 85 YLHLPPEIVPASLQRVRRPVAMVMPARraphvqavqgplGSPPKRGPLPveEQRVYRRK 143
Cdd:PTZ00034 80 YLHLPPDVFPATHKKKSVNFERKTEEE------------GSRGGRGGRG--RGRGYGRG 124
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1842-2490 |
5.99e-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: 5.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1842 AQQRL-AAEQELIRLRAETEQgeqqrqlLEEELARLQHEAAAAtQKRQELEAELAKVRAEMEVLLASKARAEEEsrstse 1920
Cdd:COG1196 177 AERKLeATEENLERLEDILGE-------LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELE------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1921 kskqRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAEN 2000
Cdd:COG1196 243 ----ELEAEL---EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2001 ERLRRLAEdeafQRRRLEEQAAQHKADIEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAE 2080
Cdd:COG1196 316 ERLEELEE----ELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2081 LELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARR 2160
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2161 LRERAEQESARQLQLAQEAAQKR---LQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAeeaeearvqa 2237
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLlllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL---------- 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2238 eREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQ 2317
Cdd:COG1196 541 -EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2318 KAQVEQELTTLRLqleetDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKD 2397
Cdd:COG1196 620 DTLLGRTLVAARL-----EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2398 NTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELlqqqkelaQ 2477
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL--------E 766
|
650
....*....|...
gi 1820553714 2478 EQARRLQEDKEQM 2490
Cdd:COG1196 767 RELERLEREIEAL 779
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
180-283 |
6.10e-33 |
|
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: 125.09 E-value: 6.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 180 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 257
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1820553714 258 RNDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
295-393 |
1.34e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 124.07 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 295 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 374
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1820553714 375 PEDVDVPQPDEKSIITYVS 393
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
296-396 |
1.61e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 123.67 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 375
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1820553714 376 EDVDVPQPDEKSIITYVSSLY 396
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
180-283 |
1.77e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 123.58 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 180 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 258
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1820553714 259 NDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
175-279 |
3.45e-32 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 124.77 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 253
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 1820553714 254 LVNIRNDDIADGNPKLTLGLIWTIIL 279
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1858-2597 |
9.27e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 138.35 E-value: 9.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1858 ETEQGEQQRQLLEE----ELARLQHEAAAATQKRQELEAELAK-VRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGR 1932
Cdd:PTZ00121 1089 ADEATEEAFGKAEEakktETGKAEEARKAEEAKKKAEDARKAEeARKAEDARKAEEARKAEDAKRV-EIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1933 FRELAEEAARLRAL--AEEAKRQRQLAEEDAARQ-----RAEAERVLAE--------KLAAISEATRLKTEAEIALK-EK 1996
Cdd:PTZ00121 1168 EARKAEDAKKAEAArkAEEVRKAEELRKAEDARKaeaarKAEEERKAEEarkaedakKAEAVKKAEEAKKDAEEAKKaEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1997 EAENERLRRLAEDEAFQRRRleeQAAQHKADIEERLAQLRKASdselERQKGLVEDTLRQRRQVEEeilalkasfekaAA 2076
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFAR---RQAAIKAEEARKADELKKAE----EKKKADEAKKAEEKKKADE------------AK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2077 GKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVE 2156
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2157 EARR---LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSvlDRLRSEAEVArraaeeaeea 2233
Cdd:PTZ00121 1389 EKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEA---------- 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2234 rvqaeREAAQSRRQVEEAERLKQLAEEQAQARAQAqaaaeKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQ 2313
Cdd:PTZ00121 1457 -----KKAEEAKKKAEEAKKADEAKKKAEEAKKAD-----EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2314 TlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQrlKAEATEAARQRSQVEEELFSVRVQMEELSKL-KARIEAENRALI 2392
Cdd:PTZ00121 1527 A--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeEARIEEVMKLYE 1602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2393 LRDKDNTQRFLQEEAEKMKqvAEEAARlsvaAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEllqQQ 2472
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE---ED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2473 KELAQEqARRLQEDKEQMAQQLAEETQgfqrtlEAERQRQLEMSAEAERLKLRmaEMSRAQARAEEDAQRFRKQAEEIGE 2552
Cdd:PTZ00121 1674 KKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKKAE--ELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1820553714 2553 KLHRTELATQEKvTLVQTLEIQRQQSDHDAERLREAIAELEREKE 2597
Cdd:PTZ00121 1745 KAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
283-398 |
2.82e-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: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 283 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 362
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 363 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 398
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
299-400 |
4.12e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 119.68 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 299 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 377
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1820553714 378 VDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
295-393 |
1.24e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.40 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 295 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 374
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1820553714 375 PEDVDVPQPDEKSIITYVS 393
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1451-2164 |
1.39e-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: 134.03 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1451 QEYVDLRTRYSELT-TLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqAKAQAEREAKE 1529
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1530 LQQRMQEEVVRREeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1609
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1610 GELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1689
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1690 RQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL- 1768
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1769 ---------------ERWQLKANEALRLRLQA---EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQE 1830
Cdd:TIGR02168 518 lsgilgvlselisvdEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1831 -------------------------------------LEKQRQL-----------------------AEGTAQQRLAAEQ 1850
Cdd:TIGR02168 598 egflgvakdlvkfdpklrkalsyllggvlvvddldnaLELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1851 ELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRL 1926
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1927 EAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAeialKEKEAENERLRRL 2006
Cdd:TIGR02168 758 ELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2007 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAGKAELELELG 2086
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2087 RIRSNAE--DTLRSKEQAELEAARQR------QLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLK----AK 2154
Cdd:TIGR02168 912 ELRRELEelREKLAQLELRLEGLEVRidnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAA 991
|
810
....*....|
gi 1820553714 2155 VEEARRLRER 2164
Cdd:TIGR02168 992 IEEYEELKER 1001
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
299-401 |
1.41e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.49 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 299 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 376
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1820553714 377 DVDVPQPDEKSIITYVSSLYDAMPR 401
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
176-285 |
2.15e-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: 118.07 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 251
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1820553714 252 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 285
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
301-396 |
3.49e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.06 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 301 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 379
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1820553714 380 VPQPDEKSIITYVSSLY 396
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
179-281 |
5.19e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 116.81 E-value: 5.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 179 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 255
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHF 281
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1031-1108 |
1.19e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 114.62 E-value: 1.19e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 1031 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 1108
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1488-2706 |
3.80e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 129.18 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1488 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAE--REAKELQQRMQEEVVRRE---EAAVD-----AQQQKRSIQ 1556
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAElhTEAVQRRQQLDQELAERRqtvESHVNenvawAEQLRARTE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1557 EELQQLRQSSEAEiqakARQAEAAERSRL-RIEEEIRVvRLQLEAtERQRGGAEGELQALRAQAEE----AEAQKRQAQE 1631
Cdd:NF041483 163 SQARRLLDESRAE----AEQALAAARAEAeRLAEEARQ-RLGSEA-ESARAEAEAILRRARKDAERllnaASTQAQEATD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1632 EAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAreKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALET-AQRS 1710
Cdd:NF041483 237 HAEQLRSSTAAESDQARRQAAELS-------RAA--EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAnEQRT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1711 AEAELQSKR-ASFAEKTAQLERSLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVA 1789
Cdd:NF041483 308 RTAKEEIARlVGEATKEAEALKAEAEQALADARAEA-----------------------EKLVAEAAEKARTVAAEDTAA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1790 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrql 1868
Cdd:NF041483 365 QLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1869 LEEELARLQHEAAaatQKRQELEAELAKVRAEmevllaskARAEeesrstsekSKQRLEAEAGRFRELAEEAarlRALAE 1948
Cdd:NF041483 438 LQEEARRLRGEAE---QLRAEAVAEGERIRGE--------ARRE---------AVQQIEEAARTAEELLTKA---KADAD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1949 EAKrqrqlaeedaARQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 2028
Cdd:NF041483 495 ELR----------STATAESERVRTE---AIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREE 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2029 EERLAQLRKA-SDSELERQKGLVEdtlrQRRQVEEEilALKASFEKAAAGKAELELELGRIRSNAEDTLRS-KEQAELEA 2106
Cdd:NF041483 562 TERAIAARQAeAAEELTRLHTEAE----ERLTAAEE--ALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2107 ARQRqlaaeeeqrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLR-------ERAEQESARQLQLAQ- 2177
Cdd:NF041483 636 ERLR---------TEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQEsADRVRaeaaaaaERVGTEAAEALAAAQe 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2178 EAAQKRLQAEE---KAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEE--AE 2252
Cdd:NF041483 707 EAARRRREAEEtlgSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvAG 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2253 RLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVR--------RAQAEQAALRQKQAADAEMEKHKKFAEQTLRQkAQVEQE 2324
Cdd:NF041483 787 LQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRvrsdayaeRERASEDANRLRREAQEETEAAKALAERTVSE-AIAEAE 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2325 lttlRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR----VQMEELSKLKARIEAENRALILRDKDNTQ 2400
Cdd:NF041483 866 ----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLR 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2401 RFLQEEAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavqEATRLKAEAELLQQQKELAQE 2478
Cdd:NF041483 942 DEARAEAERVRADAAAQAEqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEA-----ERVKAEAAAEAERLRTEAREE 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2479 QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRfrKQAEEIgeklhrTE 2558
Cdd:NF041483 1017 ADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAAR--KEAERI------VA 1088
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2559 LATQEKVTLVqtlEIQRQQSDH-------DAERLREAIAEL----EREKEKLQQEAKllQLKSEEMQTVQQEQLLQETQA 2627
Cdd:NF041483 1089 EATVEGNSLV---EKARTDADEllvgarrDATAIRERAEELrdriTGEIEELHERAR--RESAEQMKSAGERCDALVKAA 1163
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2628 LQQ---------SFLSEKDSLLQRERFIEQEKAklEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVAsmeearQRQHE 2698
Cdd:NF041483 1164 EEQlaeaeakakELVSDANSEASKVRIAAVKKA--EGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVE------EGKRE 1235
|
....*...
gi 1820553714 2699 AEEGVRRK 2706
Cdd:NF041483 1236 LDVLVRRR 1243
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
281-398 |
4.61e-29 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 114.80 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 281 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 360
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1820553714 361 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1240-2483 |
7.98e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 128.40 E-value: 7.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1240 EVLRAheeQLKEAQAVPATLPELEATKASLKK---LR-AQAEAQQPMFDALRdELRGAQEVGERLQQRHGERDVeverwr 1315
Cdd:NF041483 46 EVLRA---KLHEARRSLASRPAYDGADIGYQAeqlLRnAQIQADQLRADAER-ELRDARAQTQRILQEHAEHQA------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1316 ervaqlleRWQAVLAQTDV--RQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVREQ----LRQEK 1389
Cdd:NF041483 116 --------RLQAELHTEAVqrRQQLDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQalaaARAEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1390 ALLEEIERH--GEKVEECQRFAKQYI-NAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTRYSELTTL 1466
Cdd:NF041483 188 ERLAEEARQrlGSEAESARAEAEAILrRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESD-----QARRQAAELSRA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1467 TSQyikfisetlrRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqAKAQAEREAKELQQRMQEEVVRREEAav 1546
Cdd:NF041483 263 AEQ----------RMQEAEEALREARAEAEKVVAEAKEAAAKQLASAES---ANEQRTRTAKEEIARLVGEATKEAEA-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1547 daqqqkrsIQEELQQLRQSSEAEiqAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRAQAEEAEAQK 1626
Cdd:NF041483 328 --------LKAEAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1627 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqalEELRLQaEEAERRLRQAEVERARQV---QVA 1703
Cdd:NF041483 389 RAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEARRLRGEAEQLRAEAVaegERI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1704 LETAQRSAEAELQsKRASFAEKTAQLERSLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLKANE-ALRLR 1782
Cdd:NF041483 464 RGEARREAVQQIE-EAARTAEELLTKAKADADELRSTATAES-----------------------ERVRTEAIErATTLR 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1783 LQAEEVAQqkslaqaeaekqkeeaerearrrgKAEEQAVRHRELAEQELEKQRQlaegtaqqrlAAEQELIRLRAETEQG 1862
Cdd:NF041483 520 RQAEETLE------------------------RTRAEAERLRAEAEEQAEEVRA----------AAERAARELREETERA 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1863 EQQRQL-LEEELARLQHEAaaaTQKRQELEAELAKVRAEMEVLlaSKARAEEESRSTSEKS------KQRLEAEAGRFR- 1934
Cdd:NF041483 566 IAARQAeAAEELTRLHTEA---EERLTAAEEALADARAEAERI--RREAAEETERLRTEAAerirtlQAQAEQEAERLRt 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1935 ELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEA----ERVLAEKLAAiseATRLKTEAEIALKEKEAENERLRRLAED 2009
Cdd:NF041483 641 EAAADASAARAEGENvAVRLRSEAAAEAERLKSEAqesaDRVRAEAAAA---AERVGTEAAEALAAAQEEAARRRREAEE 717
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2010 -------EAFQRRRL-----EEQAAQHKADIEERLAQLRKASDSELERQKGLV---EDTLRQRR--------QVEEEILA 2066
Cdd:NF041483 718 tlgsaraEADQERERareqsEELLASARKRVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAG 797
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2067 LKASFEKAAA-GKAELELELGRIRSnaeDTLRSKEQAELEAARQRQlaaeeeqrrreaeERVQKSLAAEEEAARQRKAAL 2145
Cdd:NF041483 798 LRSAAEHAAErTRTEAQEEADRVRS---DAYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAI 861
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2146 EEVERLKAKVEE-ARRLRERAeqeSARQLQLAQEAAQKRLQAEEKAHAF---AVQQKEQELQQTLQQEQSVLDRLRSEAE 2221
Cdd:NF041483 862 AEAERLRSDASEyAQRVRTEA---SDTLASAEQDAARTRADAREDANRIrsdAAAQADRLIGEATSEAERLTAEARAEAE 938
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2222 VARRAAEEAEEARVQAEREAAQS--RRQVEEAERLK----QLAEEQAQARAQAQAAAEKLRKDAEQEAVR-RAQAEQAAL 2294
Cdd:NF041483 939 RLRDEARAEAERVRADAAAQAEQliAEATGEAERLRaeaaETVGSAQQHAERIRTEAERVKAEAAAEAERlRTEAREEAD 1018
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2295 RQKQAADAEMEKHK-KFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDE------------ELQRLKAEAT-----EA 2356
Cdd:NF041483 1019 RTLDEARKDANKRRsEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEaqadtmvgaarkEAERIVAEATvegnsLV 1098
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2357 ARQRSQVEEELFSVRVQM----EELSKLKARIEAENRALilrdkdnTQRFLQEEAEKMKQVAEEAARLSVAAQE------ 2426
Cdd:NF041483 1099 EKARTDADELLVGARRDAtairERAEELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEEqlaeae 1171
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2427 --AARLRQLAEEDLAQQRALA----EKMLKE----KMQAVQEATRLKAEAEllQQQKELAQEQARRL 2483
Cdd:NF041483 1172 akAKELVSDANSEASKVRIAAvkkaEGLLKEaeqkKAELVREAEKIKAEAE--AEAKRTVEEGKREL 1236
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
299-398 |
2.46e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.61 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 299 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 377
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1820553714 378 VDVPQPDEKSIITYVSSLYDA 398
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1243-1953 |
4.05e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1243 RAHEEQLKEAQAVpATLPELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLl 1322
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1323 erwqavlaqtdvrQRELEQLGRQLRYYRESadplgawLQDARQRQEQIQAmpladsqavreqlrQEKALLEEIERHGEKV 1402
Cdd:COG1196 294 -------------LAELARLEQDIARLEER-------RRELEERLEELEE--------------ELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1403 EECQrfakqyinaikdyelqlvtykaqlepvaspakkpkvqsgsesviqeyvdlrtryselttltsqyikfisETLRRME 1482
Cdd:COG1196 340 EELE---------------------------------------------------------------------EELEEAE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1483 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRREEAAVDAQQQKRSIQEELQQL 1562
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1563 RQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRrqvQD 1642
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE---GF 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1643 ESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1722
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1723 AEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA----NEALRLRLQAEEVAQQKSLAQAE 1798
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGS 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1799 AEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1878
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1879 EAAAATQ-------KRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLralaEEAK 1951
Cdd:COG1196 747 LLEEEALeelpeppDLEELERELERLEREIEALGPVNLLAIEE-----------YEELEERYDFLSEQREDL----EEAR 811
|
..
gi 1820553714 1952 RQ 1953
Cdd:COG1196 812 ET 813
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
179-281 |
1.95e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 109.11 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 179 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 255
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHF 281
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
283-398 |
2.12e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 109.79 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 283 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 362
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 363 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1536-2409 |
2.24e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.71 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1536 EEVVrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL 1615
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1616 RAQAEEaEAQKRQAQEEAERLRRqvqdeSQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQ-AEEAERRLRQAEV 1694
Cdd:PTZ00121 1108 TGKAEE-ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1695 ERARQVQVALETaqRSAEaelQSKRASFAEKtAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaerELERWQLK 1774
Cdd:PTZ00121 1182 RKAEEVRKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVK-----------------KAEEAKKD 1238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1775 ANEALRlrlqAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEqAVRHRELAEQELEKQRQLAEGTAQQRLAaeQELIR 1854
Cdd:PTZ00121 1239 AEEAKK----AEEERNNEEIRKFEEARMAHFARRQAAI--KAEE-ARKADELKKAEEKKKADEAKKAEEKKKA--DEAKK 1309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1855 LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAeagrfR 1934
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-----K 1384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1935 ELAEEAARlralAEEAKRQrqlAEEDAAR----QRAEAERVLAEKLAAISEATRLKTEAeialkEKEAENERLRRLAEDE 2010
Cdd:PTZ00121 1385 KKAEEKKK----ADEAKKK---AEEDKKKadelKKAAAAKKKADEAKKKAEEKKKADEA-----KKKAEEAKKADEAKKK 1452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2011 AFQRRRLEEqaAQHKADiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEeilALKASFEKAaagKAElELELGRIRS 2090
Cdd:PTZ00121 1453 AEEAKKAEE--AKKKAE-EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKK---KAD-EAKKAEEAK 1522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2091 NAEDTLRSKEQAELEAARQRQlaaeeeqrrreaeervQKSLAAEEEAARQRKAALEeverlKAKVEEARRLRERaEQESA 2170
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAE----------------EKKKADELKKAEELKKAEE-----KKKAEEAKKAEED-KNMAL 1580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2171 RQLQLAQEAAQKRLQAEEKAHAFAVQQKeqelqqtlqqeqsvldrlrseaevarraaeeaeEARVQAEREAAQSRRQVEE 2250
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMK---------------------------------AEEAKKAEEAKIKAEELKK 1627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2251 AERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADA--EMEKHKKFAEQTLRQKAQVEQELTTL 2328
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2329 RLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLkARIEAENRALILRDKDNTQRFLQEEAE 2408
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI-AHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
.
gi 1820553714 2409 K 2409
Cdd:PTZ00121 1787 E 1787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1859-2760 |
3.04e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1859 TEQGEQQRQLLEEELARLQHEAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1936
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1937 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 2014
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2015 RRLEEQaaqHKADIEERLAQLRKASDSelerqkglvedtlrqrRQVEEeilalkasfekaaAGKAELELELGRIRsNAED 2094
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2095 TLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2174
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2175 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEqsvldrlrseaevarraaeeaeearvqaeREAAQSRRQVEEAERL 2254
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA-----------------------------KKKAEEAKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2255 KQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2334
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2335 TDHQknlldEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARiEAENRALILRDKDNtqrfLQEEAEKMKQVA 2414
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADE----AKKKAEEAKKKA 1499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2415 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeQM 2490
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NM 1578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2491 AQQLAEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtlvqt 2570
Cdd:PTZ00121 1579 ALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK----- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2571 leiqrqqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSflSEKDSLLQRERFIEQEK 2650
Cdd:PTZ00121 1647 ---------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKAEELKKKEAEEK 1715
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2651 AKLEQLFQDEVAKAQqlreeqqrqqqqmeqerqrlvasmeEARQRQHEAEEGvRRKQEELQQLEQQRRQQEELLAEENQR 2730
Cdd:PTZ00121 1716 KKAEELKKAEEENKI-------------------------KAEEAKKEAEED-KKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
890 900 910
....*....|....*....|....*....|
gi 1820553714 2731 LREQLQRLEEQHRAALAHSEEVTALQVAAT 2760
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1818-2656 |
7.16e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.70 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1897
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1898 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK-- 1975
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELes 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1976 -LAAISEATRLKTEAEIALKEKEAENERLRRLaedeafqRRRLEEQAAQHKADIEERLAQLrkaSDSELERQKGLVEDTL 2054
Cdd:TIGR02168 356 lEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2055 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdtlrsKEQAELEAARQRQLaaeeeqrrreaeervqkSLAAE 2134
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2135 EEAARQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFA 2194
Cdd:TIGR02168 484 LAQLQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2195 VQQKEQELQQTLQQEQSVLDR-LRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEE-------AERLKQ---LAEEQAQ 2263
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNaleLAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2264 ARAQAQAAAEKLRKDAeqeAVRRAQAEQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLD 2343
Cdd:TIGR02168 644 GYRIVTLDGDLVRPGG---VITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2344 EELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEnralilrdkdntqrfLQEEAEKMKQVAEEAARLSVA 2423
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2424 AQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLAEETQgfq 2502
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2503 rtleaerqrqlEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDA 2582
Cdd:TIGR02168 849 -----------ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2583 ERLREAIAELEREKEKLQQEAKLLQlkseemQTVQQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2656
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
158-284 |
1.20e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.81 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 158 TTQRTLARPGPepapatdeRDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRF 234
Cdd:cd21310 2 ATEKDLAEDAP--------WKKIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQ 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 235 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 284
Cdd:cd21310 74 MKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1992-2656 |
1.21e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 120.81 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1992 ALKEKEAENERLRRLaEDEAF----QRRRLEEQAAQ------HKADIEERLAQLRKASDSELERQKGLVEdtlRQRRQVE 2061
Cdd:COG1196 177 AERKLEATEENLERL-EDILGelerQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELE---AELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2062 EEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQR 2141
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2142 KAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAvqqkeqelqqtlqqeqsvldrlrseae 2221
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--------------------------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2222 varraaeeaeearvqaEREAAQSRRQVEEAERLKQLAeeqaqaraqaqaaaeKLRKDAEQEAVRRAQAEQAALRQKQAAD 2301
Cdd:COG1196 386 ----------------EELLEALRAAAELAAQLEELE---------------EAEEALLERLERLEEELEELEEALAELE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2302 AEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAArqrsQVEEELFSVRVQMEELSKLK 2381
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA----ARLLLLLEAEADYEGFLEGV 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2382 ARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR 2461
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2462 LKAEAELLQQQKELAQEQARRlqedkEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQ 2541
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREA-----DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2542 RFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQL 2621
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
650 660 670
....*....|....*....|....*....|....*
gi 1820553714 2622 LQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2656
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERE-LERLEREIEAL 779
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
283-398 |
1.29e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.50 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 283 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 362
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 363 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1232-1991 |
5.50e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.09 E-value: 5.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1232 IRSTQGAEEVLRAHE-EQLKEAQAVPATLPELEATKASLKKlRAQ----AEAQQPMFDALR-DELRGAQEVGERLQQRHG 1305
Cdd:PTZ00121 1130 AEEARKAEDARKAEEaRKAEDAKRVEIARKAEDARKAEEAR-KAEdakkAEAARKAEEVRKaEELRKAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1306 ERDVEVERWR----ERVAQLLERWQAVLAQTD-VRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQA 1380
Cdd:PTZ00121 1209 EEERKAEEARkaedAKKAEAVKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1381 VR--EQLR--QEKALLEEIERHGEKVEECQRFAKQYINAIKDYELqlVTYKAQLEPVASPAKKPKVQSGSESViqeyvDL 1456
Cdd:PTZ00121 1289 KKkaDEAKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEA-----EA 1361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1457 RTRYSELTTLTSQYIKFISETLRRMEEEERLAEQ--QRAEERERLAEveaalekqrqlaeaHAQAKAQAEREAKELQQRm 1534
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKAD--------------ELKKAAAAKKKADEAKKK- 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1535 QEEVVRREEAAVDAQQQKRSiqeelqqlrqsseAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelqa 1614
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKA-------------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK--------- 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1615 lraqAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRAlqalEELRlqaeEAERRLRQAEV 1694
Cdd:PTZ00121 1485 ----ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKA----DEAK----KAEEKKKADEL 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1695 ERARQVQVAlETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAerareeaerelerwqlK 1774
Cdd:PTZ00121 1552 KKAEELKKA-EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK----------------K 1614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1775 ANEAlrlRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRHRElaeqELEKQRQLAEGTAQQRLAAEQELIR 1854
Cdd:PTZ00121 1615 AEEA---KIKAEELKKAEEEKKKVEQLK------------KKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKK 1675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1855 LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAElakVRAEMEVllaskARAEEESRSTSEKSKQRLEAEAGRFR 1934
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE---KKKAEEL-----KKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1935 ELAEEAARLRALAEEAKRQRQLAEEdaarQRAEAERVLAEKLAAISEATRLKTEAEI 1991
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1827-2704 |
6.60e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 118.77 E-value: 6.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1827 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQHEA-AAATQKRQELEAELAKVRAEMEV 1903
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1904 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLaekLAAISE 1981
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1982 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR----LEEQAAQHKADIEERLAQLRKASDSELE-------RQKGLV 2050
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRqaaeLSRAAEQRMQEAEEALREARAEAEKVVAeakeaaaKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2051 EDTLRQR-RQVEEEILALKASFEK-AAAGKAELELELGRIRSNAEDTLRSKEqaelEAARQRQLAAEEEQRRREAEERVQ 2128
Cdd:NF041483 300 ESANEQRtRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEAA----EKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2129 KSLAAEEEAARQRKAALEEVERLKAKVE-EARRLRERAEQES---------------ARQLQLAQEAAQKRLQAE----- 2187
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEaEADRLRGEAADQAeqlkgaakddtkeyrAKTVELQEEARRLRGEAEqlrae 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2188 -----EKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQS-RRQVEEAerLKQLAEEQ 2261
Cdd:NF041483 456 avaegERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTlRRQAEET--LERTRAEA 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2262 AQARAQAQAAAEKLRKDAEQEAV-RRAQAEQAALRQKQAADAEMEKHKKFAEQTLrqkAQVEQELTTLRlqlEETDHQKN 2340
Cdd:NF041483 534 ERLRAEAEEQAEEVRAAAERAAReLREETERAIAARQAEAAEELTRLHTEAEERL---TAAEEALADAR---AEAERIRR 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2341 LLDEELQRLKAEATEAARQ-RSQVEEELFSVRVQMEELSKlKARIEAENRALILRD-------------KDNTQRFLQEE 2406
Cdd:NF041483 608 EAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAADAS-AARAEGENVAVRLRSeaaaeaerlkseaQESADRVRAEA 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2407 AEKMKQVAEEAAR-LSVAAQEAARLRQLAEEDLAQQRALAEKmlkEKMQAVQEATRLKAEAellQQQKELAQEQARRLQE 2485
Cdd:NF041483 687 AAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEADQ---ERERAREQSEELLASA---RKRVEEAQAEAQRLVE 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2486 DK-----------EQMAQQLAEETQGFQRTLE-------------AERQRQlEMSAEAERLKlrmAEMSRAQARAEEDAQ 2541
Cdd:NF041483 761 EAdrratelvsaaEQTAQQVRDSVAGLQEQAEeeiaglrsaaehaAERTRT-EAQEEADRVR---SDAYAERERASEDAN 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2542 RFRKQAEEIGEKLHrtELATQEKVTLVQTLEIQRQQSDHDAERLR----EAIAELEREKEKLQQEAKllQLKSEEMQTVQ 2617
Cdd:NF041483 837 RLRREAQEETEAAK--ALAERTVSEAIAEAERLRSDASEYAQRVRteasDTLASAEQDAARTRADAR--EDANRIRSDAA 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2618 QEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQH 2697
Cdd:NF041483 913 AQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIR 992
|
....*..
gi 1820553714 2698 EAEEGVR 2704
Cdd:NF041483 993 TEAERVK 999
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1540-2461 |
8.38e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 118.24 E-value: 8.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1540 RREEAavdaQQQKRSIQEELQQL---RQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEAterqrggaeGELQALR 1616
Cdd:TIGR02168 173 RRKET----ERKLERTRENLDRLediLNELERQLKSLERQAEKAERYK-ELKAELRELELALLV---------LRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1617 AQAEEAEAQKRQAQEEAERLRRQVQdesqrkrQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLR--QAEV 1694
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1695 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLErSLQEEHVAVAQlreeaerraqqqaeaerareeaerELERWQLK 1774
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEA------------------------ELEELEAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1775 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQlaEGTAQQRLAAEQELIR 1854
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1855 LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGR 1932
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1933 FRELAEEAARLRALAEEAKRQRQLA----EEDAARQRAEAERVLAEKLAAISEATRLKteaeialkEKEAENERLRRLAE 2008
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGRLQAvvveNLNAAKKAIAFLKQNELGRVTFLPLDSIK--------GTEIQGNDREILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2009 DEAFQR--RRLEEQAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILALKASFEKAAAG----KAELE 2082
Cdd:TIGR02168 597 IEGFLGvaKDLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAK 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2083 LELGRI-RSNAEDTLRSK-EQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARR 2160
Cdd:TIGR02168 668 TNSSILeRRREIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2161 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAERE 2240
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2241 AAQSRRQVEEAERLkqlaeeqaqaraqaqaaaekLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFaEQTLRQKAQ 2320
Cdd:TIGR02168 826 LESLERRIAATERR--------------------LEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERAS 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2321 VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL-SKL--KARIEAENRALILRDKD 2397
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqERLseEYSLTLEEAEALENKIE 964
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2398 NTQRFLQEEAEKMKQVAEEAARLSVAAQEAarLRQLAE--EDLAQQRALAEKMLKEKMQAVQEATR 2461
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEE--YEELKEryDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
175-283 |
1.36e-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: 104.84 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHR- 250
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTKv 94
|
90 100 110
....*....|....*....|....*....|...
gi 1820553714 251 QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21247 95 PVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1262-2101 |
2.05e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.08 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1262 LEATKASLKKLRAQAEAQQpMFDALRDELRGAQE--VGERLQQRHGERDvEVERWRERVAQLLERWQAVLAQTDVrqrEL 1339
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAE-RYKELKAELRELELalLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEE---KL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1340 EQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDY 1419
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1420 ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTtltsQYIKFISETLRRMEEEerlaEQQRAEERERL 1499
Cdd:TIGR02168 350 KEELESLEAELE--ELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNNEIERLEAR----LERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1500 AEVEAALEKQRQLAEAHAQAKAQAEREAKELQQrmQEEVVRREEAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEA 1579
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEEL--QEELERLEEALEELREELEEAEQALDAAER----ELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1580 AERSRLRIEEEIRVVRlQLEATERQRGGAEGELqalrAQAEEAEAQKRQAQEEAERLRRQ---VQDESQRKR--QAEAEL 1654
Cdd:TIGR02168 494 LERLQENLEGFSEGVK-ALLKNQSGLSGILGVL----SELISVDEGYEAAIEAALGGRLQavvVENLNAAKKaiAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1655 ALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALET-------AQRSAEAELQSKRASFAEKTA 1727
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1728 QLERSLQEEHVAVAQlreeaerraqqqaeaeRAREEAERELERwqlkANEALRLRLQAEEVAQQkslaqaeaekqkeeae 1807
Cdd:TIGR02168 649 TLDGDLVRPGGVITG----------------GSAKTNSSILER----RREIEELEEKIEELEEK---------------- 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1808 reaRRRGKAEEQAVRH-RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1886
Cdd:TIGR02168 693 ---IAELEKALAELRKeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1887 RQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR 1963
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEElkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1964 QRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRL-------------AEDEAFQRRRLEEQAAQHKADIEE 2030
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLrseleelseelreLESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2031 RLAQLRKASDSELERQKGLVEDTLrqrRQVEEEILALKASFEKAAAGKAELEL---ELGRIRSNAEDTLRSKEQ 2101
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTL---EEAEALENKIEDDEEEARRRLKRLENkikELGPVNLAAIEEYEELKE 1000
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
183-280 |
2.26e-25 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 103.16 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 183 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 258
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1820553714 259 NDDIADGnPKLTLGLIWTIILH 280
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
301-396 |
2.36e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.39 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 301 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 379
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1820553714 380 VPQPDEKSIITYVSSLY 396
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
283-398 |
4.08e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 103.23 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 283 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 362
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 363 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
295-401 |
6.71e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.98 E-value: 6.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 295 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 371
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1820553714 372 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 401
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
180-283 |
2.30e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 180 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 255
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
299-399 |
3.80e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 99.85 E-value: 3.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 299 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 378
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1820553714 379 DVPQPDEKSIITYVSSLYDAM 399
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
297-396 |
4.46e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.56 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 297 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 376
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1820553714 377 D-VDVPQPDEKSIITYVSSLY 396
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
296-400 |
2.81e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.17 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 375
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1820553714 376 EDVDVPQPDEKSIITYVSSLYDAMP 400
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
296-396 |
2.98e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 97.11 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 375
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1820553714 376 EDVDVPQ-PDEKSIITYVSSLY 396
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1238-2038 |
4.76e-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: 108.99 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1238 AEEVLRAHE--EQLKEAQAVPATLpELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERD------- 1308
Cdd:TIGR02168 209 AEKAERYKElkAELRELELALLVL-RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEeeieelq 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1309 -------VEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQA--------- 1372
Cdd:TIGR02168 288 kelyalaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAeleeleael 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1373 -MPLADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQ 1451
Cdd:TIGR02168 368 eELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1452 EYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER------ 1525
Cdd:TIGR02168 448 ELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilg 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1526 -------------EAKE--LQQRMQEEVVRREEAAVDAQQ---QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRI 1587
Cdd:TIGR02168 524 vlselisvdegyeAAIEaaLGGRLQAVVVENLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1588 EEEIRvvrlqlEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAelalRVKAEAEAARE 1667
Cdd:TIGR02168 604 AKDLV------KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVIT----GGSAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1668 KQRalQALEELRLQAEEAERRLR--QAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEehvaVAQLRE 1745
Cdd:TIGR02168 674 ERR--REIEELEEKIEELEEKIAelEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1746 EAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRE 1825
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1826 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL 1905
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1906 --ASKARAE-EESRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAISE 1981
Cdd:TIGR02168 908 skRSELRRElEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGP 986
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1982 ATRLkteaeiALKEKEAENERLRRLaedeafqrrrleeqaAQHKADIEERLAQLRKA 2038
Cdd:TIGR02168 987 VNLA------AIEEYEELKERYDFL---------------TAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1153-1717 |
6.79e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1153 ARECAQRITEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1232
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1233 RSTQGAEEVLRAHEEQLKEAQAvpATLPELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVE 1312
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1313 RWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAmpladsqAVREQLRQEKALL 1392
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1393 EEIERHGEKVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyik 1472
Cdd:COG1196 470 EEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1473 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA----HAQAKAQAEREAKELQQRMQEEVVRREEAAVDA 1548
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQ 1628
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1629 AQEEAERLRRQvqdESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVA-LETA 1707
Cdd:COG1196 692 ELELEEALLAE---EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEeLERE 768
|
570
....*....|
gi 1820553714 1708 QRSAEAELQS 1717
Cdd:COG1196 769 LERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2129-2742 |
8.04e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2129 KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQ 2208
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2209 EQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQ 2288
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2289 AEQAALRQKQAADAEMEKhkkfAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELF 2368
Cdd:COG1196 363 AEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2369 SVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2448
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2449 LKEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRM 2526
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2527 AEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLL 2606
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2607 QLKSEEMQTVQQEQLLQETQALQQSFLSEKDS-LLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRL 2685
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAeAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2686 VASMEEARQRQHEAEEGVRRkqeelqqleqqrrqqeellAEENQRLREQLQRLEEQH 2742
Cdd:COG1196 759 PPDLEELERELERLEREIEAlgpv-----------nllaIEEYEELEERYDFLSEQR 804
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-112 |
3.11e-22 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 94.22 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 5 MLMPRDQLRAIYEVLFREGVMVAKKDRRpRSLHPHVpGVTNLQVMRAMASLRARGLVRETFAWCHFYWYLTNEGIAHLRQ 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|....*...
gi 1820553714 85 YLHLPPEIVPASLQRVRRPVAmvMPARR 112
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ--RPQRR 104
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
296-394 |
3.14e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 94.23 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 374
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1820553714 375 PEDVDVPQPDEKSIITYVSS 394
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
158-284 |
4.64e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.77 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 158 TTQRTLARPGPepapatdeRDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRF 234
Cdd:cd21308 6 ATEKDLAEDAP--------WKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQ 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 235 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 284
Cdd:cd21308 78 MQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
179-284 |
5.09e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.76 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 179 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 255
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHFQIS 284
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
930-996 |
7.31e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.94 E-value: 7.31e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 930 QLKPRhpAHPMRGHLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 996
Cdd:pfam17902 1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2025-2824 |
4.26e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 103.30 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2025 KADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAEL 2104
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA--KKTETGKAEEARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2105 EAARQrqlaaeeeqrrreaeervqkslaaEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQEAAQKRl 2184
Cdd:PTZ00121 1137 EDARK------------------------AEEARKAEDAKRVEIAR---KAEDARKAEEARKAEDAKKAEAARKAEEVR- 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2185 QAEEKAHAFAVQQKEQElqqtlqqeqsvldRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQA 2264
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAA-------------RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2265 RAQAQAAAEKLRKDA--EQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEETDHQKnll 2342
Cdd:PTZ00121 1256 KFEEARMAHFARRQAaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKA--- 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2343 dEELQRlKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAenralilrDKDNTQRfLQEEAEKMKQVAEEAARLSV 2422
Cdd:PTZ00121 1332 -DAAKK-KAEEAKKAAEAAKAEAE-----AAADEAEAAEEKAEA--------AEKKKEE-AKKKADAAKKKAEEKKKADE 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2423 AAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAEllqqQKELAQEQARRLQEDKEqmaqqlAEETQgfQ 2502
Cdd:PTZ00121 1396 AKKKAEEDKKKADE------------LKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKK------ADEAK--K 1451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2503 RTLEAERQRQLEMSAEAERlklrMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvQTLEIQRQQSDHDA 2582
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAK----KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKA 1524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2583 ERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQALQQSFLSEKD---SLLQRERFIEQEKAKLEQLF-- 2657
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMkl 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2658 --QDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL 2735
Cdd:PTZ00121 1601 yeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2736 QRLEEQHRAAlahsEEvtalqvAATKTLPNGRDALDGPATEAEPEHSFDGLRQKvpaqrlQEAGILSAEELQRLAQGHTT 2815
Cdd:PTZ00121 1681 KKAEEDEKKA----AE------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKA------EEENKIKAEEAKKEAEEDKK 1744
|
....*....
gi 1820553714 2816 VDELARRED 2824
Cdd:PTZ00121 1745 KAEEAKKDE 1753
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1468-2322 |
4.91e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 102.36 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1468 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVD 1547
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1548 AQQQKRSIQEELQQLRQSSEAEIQA-----KARQAEAAERSRLRIEEE----------------IRVVRLQLEATERQRG 1606
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESskqeiEKEEEKLAQVLKENKEEEkekklqeeelkllakeEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1607 GAEGELQalRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElalrvKAEAEAAREKQRALQALEELRLQAEEAE 1686
Cdd:pfam02463 311 DDEEKLK--ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEE-----EEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1687 RRLRQAEVERARQVQVALETAQrsaEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAER 1766
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEK---EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1767 ELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRE---LAEQELEKQRQLAEGTAQ 1843
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1844 QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK 1923
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1924 QRLEAEAG-RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENER 2002
Cdd:pfam02463 621 RAKVVEGIlKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2003 LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELE 2082
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2083 LELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2162
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2163 ERAEQESARQLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAER 2239
Cdd:pfam02463 861 EEITKEELLQELLLKEeelEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2240 EAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAvRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKA 2319
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE-EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
...
gi 1820553714 2320 QVE 2322
Cdd:pfam02463 1020 KEF 1022
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1476-2166 |
2.47e-20 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 99.99 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDA 1548
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKRSIQEELQQLRQ-----------SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1606
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1607 GAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELrLQAEEAE 1686
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1687 RRLRQAeVERarqvqvALETAQRS--AEAELQSKRASFAEKTaQLERSLQEEHVavaqlreeaerrAQQQAEAERAREEA 1764
Cdd:COG4913 474 ERWRGA-IER------VLGGFALTllVPPEHYAAALRWVNRL-HLRGRLVYERV------------RTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1765 ERELERWQLKANEAlRLRLQAeEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQ 1844
Cdd:COG4913 534 DSLAGKLDFKPHPF-RAWLEA-ELGRRFDYVCVDSPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1845 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQ---------ELEAELAKVRAEMEVLLASKA--RAEE 1913
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELERLDASSDdlAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1914 ESRSTSEKSKQRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIA 1992
Cdd:COG4913 692 EQLEELEAELEELEEELDELkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1993 LKEKEAENERLRRLaedeafqRRRLEEQAAQHK--------------ADIEERLAQLRKASDSELERQKGLVEDTLrqRR 2058
Cdd:COG4913 772 EERIDALRARLNRA-------EEELERAMRAFNrewpaetadldadlESLPEYLALLDRLEEDGLPEYEERFKELL--NE 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2059 QVEEEILALKASFEKAAA-GKAELEL---ELGRIRSNAEDTLR-SKEQAELEAAR--QRQLAAEEEqrrreaeervqKSL 2131
Cdd:COG4913 843 NSIEFVADLLSKLRRAIReIKERIDPlndSLKRIPFGPGRYLRlEARPRPDPEVRefRQELRAVTS-----------GAS 911
|
730 740 750
....*....|....*....|....*....|....*.
gi 1820553714 2132 AAEEEAARQRKAALEE-VERLkAKVEEARRLRERAE 2166
Cdd:COG4913 912 LFDEELSEARFAALKRlIERL-RSEEEESDRRWRAR 946
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
300-397 |
2.69e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.94 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 300 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 378
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1820553714 379 DVPQPDEKSIITYVSSLYD 397
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
296-396 |
4.24e-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: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 375
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1820553714 376 EDVDV--PQPDEKSIITYVSSLY 396
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1926-2740 |
5.81e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.98 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1926 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLAEKLAAISEATRlKTEAE 1990
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1991 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAsdselerqkglvedtlrqRRQVEEEILALKAS 2070
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLE------------------VSELEEEIEELQKE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2071 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQlaaeeeqrrreaeervqKSLAAEEEAARQRKA---ALEE 2147
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-----------------KLDELAEELAELEEKleeLKEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2148 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQqtlqqeqsvLDRLRSEAEVARRAA 2227
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR---------LERLEDRRERLQQEI 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2228 EEAEEARVQAEREAAQsRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKdaEQEAVRRAQAEQAALRQKQAADAEMEKH 2307
Cdd:TIGR02168 424 EELLKKLEEAELKELQ-AELEELEEELEELQEELERLEEALEELREELEE--AEQALDAAERELAQLQARLDSLERLQEN 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2308 KKFAEQTLRQKAQVEQELTTLR---LQLEETDHQ-----KNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSK 2379
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGILgvlSELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDS 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2380 LKARIEAENRALILRDKDNTQRFLqeeaekmKQVAEEAARLSVAAQeaARLRQLA-EEDLAQQRALAEKMLKEKMQAVQE 2458
Cdd:TIGR02168 581 IKGTEIQGNDREILKNIEGFLGVA-------KDLVKFDPKLRKALS--YLLGGVLvVDDLDNALELAKKLRPGYRIVTLD 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2459 ATRL--------------------KAEAELLQQQKELAQEQARRLQ---EDKEQMAQQLAEETQGFQRTLEAERQRQLEM 2515
Cdd:TIGR02168 652 GDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISAL 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2516 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELERE 2595
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2596 KEKLQQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQ 2675
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEAL 889
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2676 QQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQRLEE 2740
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1469-2105 |
1.41e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 97.42 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1469 QYIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAEREAKELQQRMQEEV 1538
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1539 VRREEaavdaqqqkrsIQEELQQLRQSSE---AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAterqrggAEGELQAL 1615
Cdd:PRK02224 286 ERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQA-------HNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1616 RAQAEEAEAQKRQAQEEAERLrrqvqdesqrkrqaEAELalrvkAEAEAAREKQRAlqALEELRLQAEEAERRLRQAEVE 1695
Cdd:PRK02224 348 REDADDLEERAEELREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1696 RArqvqvalETAQRSaeAELQSKRASFAEKTAQLERSLQEEHVAVAQlreeaerraqqqaeaerareeaerelerwqlka 1775
Cdd:PRK02224 407 LG-------NAEDFL--EELREERDELREREAELEATLRTARERVEE--------------------------------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1776 NEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRHRELAEqELEKQRqLAEGTAQQRLAAEQELIRL 1855
Cdd:PRK02224 445 AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA-ELEDLE-EEVEEVEERLERAEDLVEA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1856 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLEAEAGRFRE 1935
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1936 LAEEAARLRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAISEatrLKTEAEIALKEKeaeNERLRRLAEDeaFQRR 2015
Cdd:PRK02224 584 LKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDERRERLAEK---RERKRELEAE--FDEA 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2016 RLEE------QAAQHKADIEERLAQLRKASDsELERQKGLVE------DTLRQRR-QVEEEILALKASFEKAaagkAELE 2082
Cdd:PRK02224 647 RIEEaredkeRAEEYLEQVEEKLDELREERD-DLQAEIGAVEneleelEELRERReALENRVEALEALYDEA----EELE 721
|
650 660
....*....|....*....|...
gi 1820553714 2083 LELGRIRSNaedtLRSKEQAELE 2105
Cdd:PRK02224 722 SMYGDLRAE----LRQRNVETLE 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2313-2858 |
1.84e-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: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2313 QTLRQKAQVEQELTTLRLQLEETDHQKNLLdeELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEaENRALI 2392
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAEL---EELEAELAELEAELE-ELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2393 LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEkmlkekmqavQEATRLKAEAELLQQQ 2472
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE----------ELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2473 KELAQE--QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEI 2550
Cdd:COG1196 347 EEAEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2551 GEKLhrTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQ 2630
Cdd:COG1196 427 EEAL--AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2631 SFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEG-----VRR 2705
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2706 KQEELQQLEQQRRQQEELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQVAATKTLPNGRDALDGPATEAEPEHSFDG 2785
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2786 LRQKVPAQRLQEAGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLLLKPTSEKLSVYAALQRQLL 2858
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
292-397 |
2.63e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 86.15 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 292 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 371
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1820553714 372 LLDPEDV-DVPQPDEKSIITYVSSLYD 397
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
296-395 |
2.82e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 85.99 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 375
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1820553714 376 ED-VDVPQPDEKSIITYVSSL 395
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
299-395 |
3.84e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.45 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 299 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 374
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1820553714 375 PEDVDVPQPDEKSIITYVSSL 395
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1863-2754 |
6.67e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 95.42 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1863 EQQRQLLEEELARLQH------EAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRF-RE 1935
Cdd:pfam02463 152 PERRLEIEEEAAGSRLkrkkkeALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYlDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1936 LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAErVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 2015
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2016 RLEEQAAQHKADIEERLAQLRKASDSELERQKglvedtlrqrrqVEEEILALKASFEKAAAGKAELELELGRIRSNAEDT 2095
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEK------------ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2096 LRSKEQAELEAARQRQLaaeeeqrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQL 2175
Cdd:pfam02463 379 KKLESERLSSAAKLKEE---------------ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2176 AQEAAQKrlqaeekahAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLK 2255
Cdd:pfam02463 444 GKLTEEK---------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2256 QLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEet 2335
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK-- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2336 DHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK----------------ARIEAENRALILRDKDNT 2399
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesakakesglrkgvslEEGLAEKSEVKASLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2400 QRFLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKELAQE 2478
Cdd:pfam02463 673 KELLEIQELQEKAESELAkEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD--KINEELKLLKQKIDEEEE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2479 QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAE--EDAQRFRKQAEEIGEKLHR 2556
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEElkEEAELLEEEQLLIEQEEKI 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2557 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQ--SFLS 2634
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEesQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2635 EKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRkqeelqqle 2714
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE--------- 981
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1820553714 2715 qqrrqQEELLAEENQRLREQLQRLEEQHRAALAHSEEVTA 2754
Cdd:pfam02463 982 -----EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
181-281 |
1.04e-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: 84.17 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 181 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 256
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1820553714 257 IRNDDIADGNPKLTLGLIWTIILHF 281
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1608-2520 |
3.10e-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: 93.50 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1608 AEGELQALRAQAEEAEAQKRQAQEE----AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAE 1683
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAEliidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1684 EAERRLRQAEVERARQVQVAletaqrsAEAELQSKRASFAEKTAQLErsLQEEHVAVAQLREEAERRAQQQAEAERAREE 1763
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEK-------EEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1764 AERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQ 1843
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKEL---------KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1844 QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSK 1923
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1924 QRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERL 2003
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKL--EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2004 RRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSeLERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELEL 2083
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2084 ELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2163
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2164 RAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQ 2243
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2244 SRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2323
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2324 ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFL 2403
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2404 QEEAEKMKQVAEEAarlsvaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2483
Cdd:pfam02463 941 LLEEADEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1820553714 2484 QEDKEQMAQQLAEETQGF---QRTLEAERQRqLEMSAEAE 2520
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFvsiNKGWNKVFFY-LELGGSAE 1047
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
182-279 |
3.40e-18 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 82.77 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 182 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 257
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1820553714 258 RNDDI-ADGNPKLTLGLIWTIIL 279
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1456-2188 |
5.04e-18 |
|
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: 92.72 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1456 LRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQrqlaeahaQAKAQAEREAKELQQRMQ 1535
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ--------EEQLKKQQLLKQLRARIE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1536 EevVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQakarqaeaaersrlrIEEEIRVVRLQLEATERQRGGAEGELQAL 1615
Cdd:TIGR00618 271 E--LRAQEAVLEETQERINRARKAAPLAAHIKAVTQ---------------IEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1616 RAQAEEAEAQKR---QAQEEAERLRRQVQDESQRKRQAEAELALRvkaeaeaarEKQRALQALEELRLQAEEAERRLRqa 1692
Cdd:TIGR00618 334 VKQQSSIEEQRRllqTLHSQEIHIRDAHEVATSIREISCQQHTLT---------QHIHTLQQQKTTLTQKLQSLCKEL-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1693 EVERARQVQVALETAQRSAEAelQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQ 1772
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQ--GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE-------------------KIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1773 LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQ---ELEKQRQLAEGTAQQRLAAE 1849
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQdidNPGPLTRRMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1850 QELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS------- 1922
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQhallrkl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1923 -----KQRLEAEAGRF-RELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 1996
Cdd:TIGR00618 622 qpeqdLQDVRLHLQQCsQELALKLTALHALQLTLTQERV--REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1997 EAENERLRRLAEDEAFQRRRLEEQAaqhkadieerlaQLRKASDSELERQKGLVEDTLRQRRQVEEEilALKASFEKAAA 2076
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIE------------NASSSLGSDLAAREDALNQSLKELMHQART--VLKARTEAHFN 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2077 GKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVE 2156
Cdd:TIGR00618 766 NNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG 845
|
730 740 750
....*....|....*....|....*....|..
gi 1820553714 2157 EARRLRERAEQESARQLQLAQEAAQKRLQAEE 2188
Cdd:TIGR00618 846 EITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1476-2244 |
1.76e-17 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 91.04 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAqAEREAKELQQRMQEEVVR-REEAAVDAQQQK 1552
Cdd:NF041483 470 EAVQQIEEAARTAEELLTKAKADADELRstATAESERVRTEAIERATT-LRRQAEETLERTRAEAERlRAEAEEQAEEVR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1553 RSIQEELQQLRQssEAEIQAKARQAEAA-ERSRLRIEEEIRVV--------------RLQLEA---TERQRGGAEGELQA 1614
Cdd:NF041483 549 AAAERAARELRE--ETERAIAARQAEAAeELTRLHTEAEERLTaaeealadaraeaeRIRREAaeeTERLRTEAAERIRT 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1615 LRAQAE--------EAEAQKRQAQEEAE----RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQrALQALEELRLQA 1682
Cdd:NF041483 627 LQAQAEqeaerlrtEAAADASAARAEGEnvavRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERV-GTEAAEALAAAQ 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1683 EEAERRLRQAE--VERARQ-VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAER 1759
Cdd:NF041483 706 EEAARRRREAEetLGSARAeADQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVA 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1760 AREEAERElerwqlkanEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAE 1839
Cdd:NF041483 786 GLQEQAEE---------EIAGLRSAAEHAAER--TRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAE 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1840 GTAQQrlaAEQELIRLRAETEQGEQQ-------------------RQLLEEELARLQHEAAA-----ATQKRQELEAELA 1895
Cdd:NF041483 855 RTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAqadrlIGEATSEAERLTA 931
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1896 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAERVLAEk 1975
Cdd:NF041483 932 EARAEAERLRDEARAEAERVRADAAAQAEQLIAEA------TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE- 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1976 laAISEATRLKTEAEialkekeAENERLRRLAEDEAFQRRRleEQAAQHKADIEERLAQLRK-ASDSELERQKGLVE--- 2051
Cdd:NF041483 1002 --AAAEAERLRTEAR-------EEADRTLDEARKDANKRRS--EAAEQADTLITEAAAEADQlTAKAQEEALRTTTEaea 1070
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2052 --DTLRQRRQVEEEILALKASFE------KAAAGKAELELELGR----IRSNAEDtLRSKEQAELEAARQRQLAAEEEQR 2119
Cdd:NF041483 1071 qaDTMVGAARKEAERIVAEATVEgnslveKARTDADELLVGARRdataIRERAEE-LRDRITGEIEELHERARRESAEQM 1149
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2120 RREAEERVQKSLAAEEEAARQRKAALEEVERLK--------AKVEEARRLRERAEQESArqlQLAQEAAQKRLQAEEKAH 2191
Cdd:NF041483 1150 KSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvriAAVKKAEGLLKEAEQKKA---ELVREAEKIKAEAEAEAK 1226
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2192 AFAVQQKEQElqqtlqqeqSVLDRLRSEAEVARRAAEEAEearvqaerEAAQS 2244
Cdd:NF041483 1227 RTVEEGKREL---------DVLVRRREDINAEISRVQDVL--------EALES 1262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1494-2038 |
2.33e-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: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1494 EERERLAEVEAALEKQRQLAEAHAQAkaqaeREAKElqqrmQEEVVRREEAAVDAQQQKRSIQEELQQLRqsSEAEIQAK 1573
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEAL-----EDARE-----QIELLEPIRELAERYAAARERLAELEYLR--AALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1574 ARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQA--------EEAEAQKRQAQEEAERLRRQVQDESQ 1645
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1646 RKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQV------ALETAQRSAEAELQSKR 1719
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleaeiaSLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1720 ASFAEKTAQLERSLQ--EEHVAVAQLReeaerraqqqaeaerareeaerelERWQLKANEAL---RLRL--------QAE 1786
Cdd:COG4913 447 DALAEALGLDEAELPfvGELIEVRPEE------------------------ERWRGAIERVLggfALTLlvppehyaAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1787 EVAQQKSLAQAEAEKQKEEAEREARRRgKAEEQAVRHR-ELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG 1862
Cdd:COG4913 503 RWVNRLHLRGRLVYERVRTGLPDPERP-RLDPDSLAGKlDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAG 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1863 ---------------------------EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1915
Cdd:COG4913 582 qvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1916 RSTS--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAISEATR 1984
Cdd:COG4913 662 DVASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLEAAED 741
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1985 LKTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 2038
Cdd:COG4913 742 LARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1822-2615 |
2.57e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 90.51 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1822 RHRELAE--QELEKQRQLAEGT--AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAK- 1896
Cdd:TIGR02169 205 REREKAEryQALLKEKREYEGYelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDl 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1897 -------VRAEMEVLLASKARAEeesRSTSEKsKQRLEAEAGRFRELAEEAARL--------RALAEEAKRQRQLAEEDA 1961
Cdd:TIGR02169 285 geeeqlrVKEKIGELEAEIASLE---RSIAEK-ERELEDAEERLAKLEAEIDKLlaeieeleREIEEERKRRDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1962 ARQ------RAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeafQRRRLEEQAAQHKADI---EERL 2032
Cdd:TIGR02169 361 ELKeeledlRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE----ELQRLSEELADLNAAIagiEAKI 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2033 AQL---RKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRirsnAEDTLRSKEQAELEAARQ 2109
Cdd:TIGR02169 437 NELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2110 RQLAAEEEQRrreaeerVQKSLAAEEEAARQRKAALEEV--ERLKAKVEE----ARRLRERAEQESARQL------QLAQ 2177
Cdd:TIGR02169 513 EEVLKASIQG-------VHGTVAQLGSVGERYATAIEVAagNRLNNVVVEddavAKEAIELLKRRKAGRAtflplnKMRD 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2178 EAAQKRLQAEEKAHAFAV-----QQKEQELQQTLQQEQSVLDRLRSEAEVA----------------------RRAAEEA 2230
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDIEAARRLMgkyrmvtlegelfeksgamtggSRAPRGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2231 EEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEaVRRAQAEQAALRQKQAADAE-MEKHKK 2309
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-IGEIEKEIEQLEQEEEKLKErLEELEE 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2310 FAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLkaEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENR 2389
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQ 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2390 ALilrdkdNTQRFLQEEAEKMKQVAEEAaRLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELL 2469
Cdd:TIGR02169 820 KL------NRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDL 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2470 QQQKELAQEQARRLQEDKEQMAQQLaEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEE 2549
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2550 IgeklhrtelatqEKVTLVQTLEIQrqqsdhDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2615
Cdd:TIGR02169 967 I------------RALEPVNMLAIQ------EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1367-2357 |
3.71e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 89.85 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1367 QEQIQAMP--LADSQAVREQLRQEKALLEEI--------ERHGEKVEECQRFAKQYINAIKDYELQL-----VTYKAQLE 1431
Cdd:pfam01576 46 QEQLQAETelCAEAEEMRARLAARKQELEEIlhelesrlEEEEERSQQLQNEKKKMQQHIQDLEEQLdeeeaARQKLQLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1432 PVASPAKKPKVQS-------GSESVIQEYVDLRTRYSELTT--------------LTSQYIKFISETLRRMEEEERLaeQ 1490
Cdd:pfam01576 126 KVTTEAKIKKLEEdillledQNSKLSKERKLLEERISEFTSnlaeeeekakslskLKNKHEAMISDLEERLKKEEKG--R 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1491 QRAEERERLAEVEAAlEKQRQLAEAHAQA---KAQAEREAKELQQ---RMQEEVVRREEAavdaQQQKRSIQEELQQLRQ 1564
Cdd:pfam01576 204 QELEKAKRKLEGEST-DLQEQIAELQAQIaelRAQLAKKEEELQAalaRLEEETAQKNNA----LKKIRELEAQISELQE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1565 SSEAEIQAKARqaeaAERSRLRIEEEIRVVRLQLEATeRQRGGAEGELQALRAQaeEAEAQKRQAQEEAERLRRQVQDES 1644
Cdd:pfam01576 279 DLESERAARNK----AEKQRRDLGEELEALKTELEDT-LDTTAAQQELRSKREQ--EVTELKKALEEETRSHEAQLQEMR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1645 QRKRQAEAELAlrvkaeaEAAREKQRALQALEELRlQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAE 1724
Cdd:pfam01576 352 QKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1725 ktAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAQAEAEKqke 1804
Cdd:pfam01576 424 --SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL--- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1805 eaerearrrgkaEEQAVRHRELAEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAT 1884
Cdd:pfam01576 495 ------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1885 QKRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEAGRFRELaeeaarlraLAEEAKRQRQLAE 1958
Cdd:pfam01576 559 QQLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQKKFDQM---------LAEEKAISARYAE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1959 EdaaRQRAEAERVLAEKLA-----AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ-------RRRLEEQAAQHKA 2026
Cdd:pfam01576 623 E---RDRAEAEAREKETRAlslarALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNvhelersKRALEQQVEEMKT 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2027 DIEERLAQLRKASDSEL-------------------------ERQKGLVedtlRQRRQVEEEILALKASFEKAAAGKAEL 2081
Cdd:pfam01576 700 QLEELEDELQATEDAKLrlevnmqalkaqferdlqardeqgeEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKL 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2082 ELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL 2161
Cdd:pfam01576 776 ELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERA 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2162 RERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSVLDRLR-SEAEVARRAAEEAEEARVQAE 2238
Cdd:pfam01576 856 RRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRkSTLQVEQLTTELAAERSTSQK 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2239 REAA--QSRRQVEE-----AERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAaLRQKQAADAE----MEKH 2307
Cdd:pfam01576 936 SESArqQLERQNKElkaklQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKL-VRRTEKKLKEvllqVEDE 1014
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2308 KKFAEQTLRQKAQVEQELTTLRLQLEETDHQK---NLLDEELQRLKAEATEAA 2357
Cdd:pfam01576 1015 RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAsraNAARRKLQRELDDATESN 1067
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
296-395 |
4.40e-17 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 79.90 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 375
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1820553714 376 ED-VDVPQPDEKSIITYVSSL 395
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
300-397 |
5.61e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.54 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 300 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 378
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1820553714 379 DVPQPDEKSIITYVSSLYD 397
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1103-2012 |
9.59e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.59 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1103 QQLLQSLEQGAQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQKAQAEVEGLGKGVARLSA 1182
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1183 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEEVLRAHEEQLKEAQ 1253
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1254 AVPATL-PELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1332
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1333 dvRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAmpladsqavreqlrqekalleEIERHGEKVEECQRFAKQY 1412
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1413 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQR 1492
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1493 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKelqQRMQEEVVRREEAAVDAQQQKRS-------------IQEEL 1559
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1560 QQLRQSSEA----------EIQAKARQA-----------EAAERSRlRIEEEIRVVRLQLEATERQ---RGGAEGELQAL 1615
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvEFDPKYEPAfkyvfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1616 RAQAEEaEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeAEAAREKQRALQALEELRLQAEEAERRlRQAEVE 1695
Cdd:TIGR02169 667 LFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKLKE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1696 RARQVQVALETAQRSAEAElQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKA 1775
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENV-KSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------SRIPEIQ 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1776 NEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRlAAEQELIRL 1855
Cdd:TIGR02169 798 AE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEEL 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1856 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAEAGRFRE 1935
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDEE 945
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1936 LAEEAARLRALAEEAKR-QRQLAEEDAARQRA--EAERVLAEKLAAISEATRLKTEAEiALKEKEAENERLRRLAEDEAF 2012
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKREVFMEAF 1024
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1473-1960 |
1.09e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 87.52 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1473 FISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQ-RMQEEVVRREEAAVDAQQQ 1551
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1552 KRSIQEELQQLRQSSEA------EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG-GAEGELQALRAQAEEAEA 1624
Cdd:COG4717 127 LLPLYQELEALEAELAElperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1625 QKRQAQEEAERLRRQVQDESQRKRQAEAELaLRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVAL 1704
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1705 ETAqrsAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQ 1784
Cdd:COG4717 286 LAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1785 AEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRHRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQ 1864
Cdd:COG4717 363 LQLEELEQEIAALLAEAGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1865 qrqlLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlaskaraeEESRSTSEKSKQRLEAEAgRFRELAEEAARLR 1944
Cdd:COG4717 430 ----LEEELEELEEELEELEEELEELREELAELEAELEQL--------EEDGELAELLQELEELKA-ELRELAEEWAALK 496
|
490
....*....|....*.
gi 1820553714 1945 ALAEEAKRQRQLAEED 1960
Cdd:COG4717 497 LALELLEEAREEYREE 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1148-1735 |
1.12e-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: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1148 LDKEPARECAQRITEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKL-EQVRSLSAIYLEKLK 1226
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeEQLETLRSKVAQLEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1227 TISLvIRSTQgaeEVLRAHEEQLKEAQAVPATlpelEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGE 1306
Cdd:TIGR02168 394 QIAS-LNNEI---ERLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1307 RDVEVERWRERVAQL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQR---------------QE 1368
Cdd:TIGR02168 466 LREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieaalGG 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1369 QIQAMPLADSQAVR---EQLRQEK----ALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP----- 1436
Cdd:TIGR02168 546 RLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggv 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1437 ----------AKKPKVQSGSESVIQEYVDLRTRYS--------ELTTL-TSQYIKFISETLRRMEEEERLAEQQRAEERE 1497
Cdd:TIGR02168 626 lvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1498 RLAEVEAALEKQRQLAE----AHAQAKAQAEREAKElQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQsseaeiqak 1573
Cdd:TIGR02168 706 ELEELEEELEQLRKELEelsrQISALRKDLARLEAE-VEQLEERIAQLSKELTELEAEIEELEERLEEAEE--------- 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1574 arQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE 1653
Cdd:TIGR02168 776 --ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1654 LAlrvkaeaeaarekqRALQALEELRLQAEEAERRLRQAEVERArQVQVALETAqRSAEAELQSKRASFAEKTAQLERSL 1733
Cdd:TIGR02168 854 IE--------------SLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELSEELRELESKRSELRREL 917
|
..
gi 1820553714 1734 QE 1735
Cdd:TIGR02168 918 EE 919
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1233-2186 |
1.34e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.82 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1233 RSTQGAEEVLRAHEEQLKEAQAVpatLPELEATKASLKKLRAQAEAqqpmFDALRDELRGAqEVGERLQQrhgerdveve 1312
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAER----YQALLKEKREY-EGYELLKE---------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1313 rWRERVAQLlerwQAVLAQTDVRQRELEQLGRQLRyyrESADPLGAWLQDARQRQEQIQAMPLADSQAVREQLRQEKALL 1392
Cdd:TIGR02169 232 -KEALERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1393 EEIERhgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltsqyik 1472
Cdd:TIGR02169 304 ASLER---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL--------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1473 fisetlrrmeeeerlaeqqraeeRERLAEVEAALEKQRQlaeahaqaKAQAEREAKELQQRMQEEVVRREEAAVDAQQQK 1552
Cdd:TIGR02169 370 -----------------------RAELEEVDKEFAETRD--------ELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1553 RsiqEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqrggAEGELQALRAQAEEAEAQKRQAQEE 1632
Cdd:TIGR02169 419 S---EELADLNAAIAGIEAKINELEEEKEDKALEIKK------------------QEWKLEQLAADLSKYEQELYDLKEE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1633 AERLRRqvqdesqRKRQAEAELAlRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAE 1712
Cdd:TIGR02169 478 YDRVEK-------ELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRL 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1713 AELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQk 1792
Cdd:TIGR02169 550 NNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVED- 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1793 slaqaeaekqkeeaereaRRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAA------EQELIRLRAETEQGEQQR 1866
Cdd:TIGR02169 629 ------------------IEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGIlfsrsePAELQRLRERLEGLKREL 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1867 QLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAAR 1942
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEIENVKS----ELKELEAR 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1943 LRALaEEAKRQRQLAEEDAARQRAEAE--------RVLAEKLAAISEATRlktEAEIALKEKEAENERLRRLAEDEAFQR 2014
Cdd:TIGR02169 767 IEEL-EEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2015 RRLEEQAAQHKADIEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAED 2094
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2095 TLRSKE--QAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQE 2168
Cdd:TIGR02169 922 LKAKLEalEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
970
....*....|....*...
gi 1820553714 2169 SARQLQLAQEAAQKRLQA 2186
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREV 1019
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
298-409 |
1.57e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 78.49 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 298 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 377
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1820553714 378 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 409
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1550-2493 |
1.60e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.82 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1550 QQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRAQAEEAEA----- 1624
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1625 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR------EKQRALQALEELRLQAEEAERrlrQAEVERAR 1698
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEL---EAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1699 QVQVALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwqlka 1775
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL--------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1776 nEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHR-ELAEQELEKQRQLAEGTAQQRLAAEQELIR 1854
Cdd:TIGR02169 367 -EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1855 LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAG 1931
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHG 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1932 RFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAiseatrlktEAEIALKEKEAENER---LRRLAE 2008
Cdd:TIGR02169 526 TVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2009 DEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELeRQKGLVEDTLRQRRQVEEEILALKAS--FEKAAA--GKAElele 2084
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGAmtGGSR---- 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2085 lgRIRSNAEDTLRSKEQAELEAARqrqlaaeeeqrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRER 2164
Cdd:TIGR02169 661 --APRGGILFSRSEPAELQRLRER-------------------------LEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2165 AEQE----SARQLQLAQE-AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRseaevarraaeeaeearvqaeR 2239
Cdd:TIGR02169 714 ASRKigeiEKEIEQLEQEeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---------------------E 772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2240 EAAQSRRQVEEAERlkQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKA 2319
Cdd:TIGR02169 773 DLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2320 QVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENraliLRDKDNT 2399
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSELK 923
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2400 QRfLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2479
Cdd:TIGR02169 924 AK-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
970
....*....|....
gi 1820553714 2480 ARRLQEDKEQMAQQ 2493
Cdd:TIGR02169 1002 RKAILERIEEYEKK 1015
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
301-396 |
4.76e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 77.02 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 301 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 379
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1820553714 380 VPQPDEKSIITYVSSLY 396
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
298-397 |
6.89e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 76.16 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 298 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 377
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1820553714 378 VDV--PQPDEKSIITYVSSLYD 397
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
298-401 |
1.12e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 75.86 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 298 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 377
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1820553714 378 VDV--PQPDEKSIITYVSSLYDAMPR 401
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1238-1736 |
1.31e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1238 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRaqaeaqqpmfDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1317
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1318 VAQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLGAWLQDARQRQEQIQamplADSQAVREQLRQEKA 1390
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1391 LLEEIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqy 1470
Cdd:PRK02224 385 EIEELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT---- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1471 ikfISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAK--AQAEREA 1527
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEdlVEAEDRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1528 KELQQRMQ--EEVVRREEAAVDAQQQKR-SIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvRLQLEATERQ 1604
Cdd:PRK02224 512 ERLEERREdlEELIAERRETIEEKRERAeELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1605 RGGAEGELQALRAQAE---EAEAQKRQAQEEAERLRR-QVQDESQRKRQAEAELAlrvKAEAEAARE-KQRALQALEEL- 1678
Cdd:PRK02224 590 SLERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYLEQVe 666
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1679 -RLQAEEAERRLRQAEVERARQVQVALEtaqrsaeaELQSKRASFAEKTAQLErSLQEE 1736
Cdd:PRK02224 667 eKLDELREERDDLQAEIGAVENELEELE--------ELRERREALENRVEALE-ALYDE 716
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
178-277 |
2.25e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.87 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 178 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 252
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1820553714 253 KLVNIRNDDIADGNPKLTLGLIWTI 277
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1151-1725 |
2.36e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.81 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1151 EPARECAQRITEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1230
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1231 VIRSTQGAEEvlraheEQLKEaqavpatlpELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVE 1310
Cdd:COG4913 331 QIRGNGGDRL------EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1311 VERWRERVAQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLGAWLQDARQRQEqiQAMPLADSQA--------VR 1382
Cdd:COG4913 396 LEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALRDALA--EALGLDEAELpfvgelieVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1383 -EQLRQEKAlleeIER--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqey 1453
Cdd:COG4913 471 pEEERWRGA----IERvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG------ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1454 vdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQ 1518
Cdd:COG4913 539 --------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1519 AKAQAEREAKELQQRMQeEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAErsrlrIEEEIRvvrlQL 1598
Cdd:COG4913 611 KLAALEAELAELEEELA-EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE-----LEAELE----RL 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1599 EAterqrggAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL-ALRVKAEAEAAREKQRALQALEE 1677
Cdd:COG4913 681 DA-------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEE 753
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1820553714 1678 LRlqAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEK 1725
Cdd:COG4913 754 RF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1450-2429 |
2.95e-15 |
|
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: 83.85 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1450 IQEYVDLRTRYSELTTLTSQYikFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKE 1529
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARE-SD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1530 LQQRMQ--EEVVRREEAAVDAQQQKRSIQEELQQLrqSSEAEIQAKARqAEAAERsrlRIEEEIRVVRLQLEATERQRGG 1607
Cdd:COG3096 325 LEQDYQaaSDHLNLVQTALRQQEKIERYQEDLEEL--TERLEEQEEVV-EEAAEQ---LAEAEARLEAAEEEVDSLKSQL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1608 AEGElQALRAQAEEAeAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALqaleELRLQ-AEEAE 1686
Cdd:COG3096 399 ADYQ-QALDVQQTRA-IQYQQAVQALEKARALCGLPDLTPENAEDYLA-AFRAKEQQATEEVLEL----EQKLSvADAAR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1687 RRLRQA---------EVERARQVQVALETAQRSAEAELQSKRASfaektaQLERSLQEehvavaqlreeaerraqqqaea 1757
Cdd:COG3096 472 RQFEKAyelvckiagEVERSQAWQTARELLRRYRSQQALAQRLQ------QLRAQLAE---------------------- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1758 erareeaereLERwqlkanealRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrGKAEEQAVRHRELAEQELEKQRQL 1837
Cdd:COG3096 524 ----------LEQ---------RLRQQQNAERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1838 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEElARLQHEAAAATQKRQELEAE----LAKVRAEMEVLLaSKARAEE 1913
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREAT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1914 ESRSTSEKSKQRLEAEAgrfRELA----EEAARLRALAEE------AKRQRQLAEEDA---------ARQR---AEAERV 1971
Cdd:COG3096 644 VERDELAARKQALESQI---ERLSqpggAEDPRLLALAERlggvllSEIYDDVTLEDApyfsalygpARHAivvPDLSAV 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1972 lAEKLA-----------------AISEATRLKTEAEIALKEKEAENE-RLRRLAEDEAFQRRRLEEQAAQHKADIEERLA 2033
Cdd:COG3096 721 -KEQLAgledcpedlyliegdpdSFDDSVFDAEELEDAVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2034 QLRKAS--DSELERQKGLVEDTLRQRRQV------EEEILALKASFEKAAAGKAELELELGRIRSNAEDtlrSKEQAELE 2105
Cdd:COG3096 800 QYAKASfdVQKLQRLHQAFSQFVGGHLAVafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQ---LKEQLQLL 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2106 AARQRQLAAEEEQRRREAEERVQKSLAAEEEAAR---QRKAALEEVERLkakveeARRLRERAEQESARQLQLAQ-EAAQ 2181
Cdd:COG3096 877 NKLLPQANLLADETLADRLEELREELDAAQEAQAfiqQHGKALAQLEPL------VAVLQSDPEQFEQLQADYLQaKEQQ 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2182 KRLQAEEKAHAFAVQQKE----QELQQTLQQEQSVLDRLRseaevarraaeeaeearvQAEREAAQSRRQVEEAERLKQl 2257
Cdd:COG3096 951 RRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLR------------------ARLEQAEEARREAREQLRQAQ- 1011
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2258 aeeQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALrqKQAADAEMEkhkkfaEQTLRQKAQVEQELTTLRLqleetdh 2337
Cdd:COG3096 1012 ---AQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL--GVQADAEAE------ERARIRRDELHEELSQNRS------- 1073
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2338 QKNLLDEELQRLKAEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENRalILRDKD-----NTQRFLQEEAEKMKQ 2412
Cdd:COG3096 1074 RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER---EQVVQAKAGWCAVLR--LARDNDverrlHRRELAYLSADELRS 1148
|
1050 1060
....*....|....*....|
gi 1820553714 2413 VAEE---AARLSVAAQEAAR 2429
Cdd:COG3096 1149 MSDKalgALRLAVADNEHLR 1168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1259-1718 |
3.04e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.89 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1259 LPELEATKASLKKLRAQAEAqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWR--ERVAQLLERWQAVLAQTDVRQ 1336
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1337 RELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVREQLRQekaLLEEIERHGEKVEECQRFAKQYINAI 1416
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1417 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EE 1485
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1486 RLAEQQRAEERERL--AEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKrsIQEELQQLR 1563
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1564 QSSEAEIQAKARQAEAAErsrlRIEEEIRVVRLQLEATERqrggaEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDE 1643
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEELLG-----ELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1644 SQRKRQAEAELalrvkAEAEAAREKQRALQALEELRLQAEEAERRLRqaeveRARQVQVALETAQRSAEAELQSK 1718
Cdd:COG4717 452 REELAELEAEL-----EQLEEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYREERLPP 516
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4179-4217 |
3.59e-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: 3.59e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 4179 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4217
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1511-1881 |
3.63e-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: 82.86 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1511 QLAEAHAQAKAQAEREAKELQQRMQEEVVRreeaavdaqQQKRSIQEELQQLRQSSEAEiqaKARQAEA-------AERS 1583
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1584 RLRIEEEIRVVRLQLEatERQRggaegELQALRAQAEEAEAQKRQaqeEAERLRRQVQDESQRKRQaEAELALRVK-AEA 1662
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1663 EAAREKQRALQALEELRLQAEEA-ERRLRQAEVERARqvqvaletaqrsaeaELQSKRASFAEKTAQLERSLQEEhvava 1741
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1742 qlreeaerraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQa 1820
Cdd:pfam17380 470 ---------------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE- 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1821 vrHRELAEQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAA 1881
Cdd:pfam17380 534 --RRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1305-2067 |
4.88e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1305 GERDVEVERWRE---RVAQLLERWQAVLAQTdvrqreLEQLGRqLRYYRESADPLgawlQDARQRQEQIQAMPLADS-QA 1380
Cdd:TIGR02169 166 AEFDRKKEKALEeleEVEENIERLDLIIDEK------RQQLER-LRREREKAERY----QALLKEKREYEGYELLKEkEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1381 VREQLRQEKALLEEIERHGEKVEEcqrfakqyinAIKDYELQLVTYKAQLEPVASPAKKpkvqSGSESVIQEYVDLRTRY 1460
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1461 SELTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVR 1540
Cdd:TIGR02169 301 AEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1541 REEAaVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAE 1620
Cdd:TIGR02169 380 FAET-RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1621 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1700
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1701 QVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALR 1780
Cdd:TIGR02169 538 ATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1781 LRLQAEEVAQQKSLAQAEAEK---------------------QKEEAEREARRRGKAEEQAVRHR--------ELAEQEL 1831
Cdd:TIGR02169 618 YVFGDTLVVEDIEAARRLMGKyrmvtlegelfeksgamtggsRAPRGGILFSRSEPAELQRLRERleglkrelSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1832 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKR--------------QELEAELAKV 1897
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvkselkeleariEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1898 RAEMEVLLAS-----------KARAEEESRSTSEKSKQRLEAEAGR-------FRELAEEAARLRALAEEAKRQRQLAEE 1959
Cdd:TIGR02169 778 EEALNDLEARlshsripeiqaELSKLEEEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1960 DAARQRAEAERVLAEKLAAI----SEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQL 2035
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEI 936
|
810 820 830
....*....|....*....|....*....|....
gi 1820553714 2036 --RKASDSELERQKGLVEDTLRQRRQVEEEILAL 2067
Cdd:TIGR02169 937 edPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3601-3639 |
6.14e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 6.14e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 3601 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRIL 3639
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
174-280 |
9.27e-15 |
|
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: 73.08 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 174 TDERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIA 243
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYA 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 244 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 280
Cdd:cd21219 71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1106-1735 |
1.06e-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: 81.64 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1106 LQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLD---KEPARECAQRITEQQKAQAEVEGLGKGVARLSA 1182
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQeelKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1183 EAEKVLALPEpspAAPTLRSELELTLGKL-EQVRSLSAIYLEKLKTISLVIRSTQGAEEVLRAHEEQLKEAQAVPATLP- 1260
Cdd:TIGR02168 282 EIEELQKELY---ALANEISRLEQQKQILrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEa 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1261 ELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVL-----AQTDVR 1335
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1336 QRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVrEQLRQEKALLEEIERHGEKVEECQRFAKQ---Y 1412
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-AQLQARLDSLERLQENLEGFSEGVKALLKnqsG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1413 INAIKDYELQLVT----YKAQLEPVASPAKKPKVQSGSESVIQEYVDL------RTRYSELTTLTSQYIKFiSETLRRME 1482
Cdd:TIGR02168 518 LSGILGVLSELISvdegYEAAIEAALGGRLQAVVVENLNAAKKAIAFLkqnelgRVTFLPLDSIKGTEIQG-NDREILKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1483 EEERLAEQQRAEERERLAE---------------VEAALEKQRQL--------------------------AEAHAQAKA 1521
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRkalsyllggvlvvddLDNALELAKKLrpgyrivtldgdlvrpggvitggsakTNSSILERR 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1522 QAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR---QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQL 1598
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1599 EATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEAAREKQRALQALE-E 1677
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLErR 832
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1678 LRLQAEEAERRLRQAEVERARQVQVALE-TAQRSAEAELQSKRASFAEKTAQLERSLQE 1735
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEiEELEELIEELESELEALLNERASLEEALAL 891
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3860-3898 |
1.37e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.37e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 3860 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3898
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
755-935 |
1.41e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.95 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 755 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 834
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 835 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 914
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180
....*....|....*....|.
gi 1820553714 915 KGHLSGLAKRAKAIVQLKPRH 935
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPD 179
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
298-399 |
1.98e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 72.42 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 298 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 377
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1820553714 378 -VDVPQPDEKSIITYVSSLYDAM 399
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
296-396 |
2.77e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.03 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 375
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1820553714 376 ED-VDVPQPDEKSIITYVSSLY 396
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
181-281 |
2.96e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.56 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 181 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 252
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1820553714 253 KLVNIRNDDIADGNPKLTLGLIWTIILHF 281
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1476-2372 |
4.35e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 79.63 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1555
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVH-RTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1556 QEELQQLrQSSEAEIQAKARQAEAAeRSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAER 1635
Cdd:TIGR00618 132 IHDLLKL-DYKTFTRVVLLPQGEFA-QFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1636 LRRQVQDESQRKRQAEAELalrvKAEAEAAREKQRALQALEELRLQAEEAERRLRQAeveraRQVQVALETAQ-RSAEAE 1714
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKEL----KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLL-----KQLRARIEELRaQEAVLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1715 LQSKRASFAEKTAQLerslQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKSL 1794
Cdd:TIGR00618 281 ETQERINRARKAAPL----AAHIKAVTQIEQQAQRI-----------------HTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1795 AQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQgeqqrqlleeeLA 1874
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL--QQQKTTLTQKLQSLCKELDI-----------LQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1875 RLQHEAAAATQKRQELEAELAKVRAEMEVLL--ASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAK 1951
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQryAELCAAAITCTAQCEKLEKIHLQESAQsLKEREQQLQTKEQIHLQET 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1952 RQRQLAEEDAARQRAE------AERVLAEKLAAISEA---TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAa 2022
Cdd:TIGR00618 487 RKKAVVLARLLELQEEpcplcgSCIHPNPARQDIDNPgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2023 QHKADIEERLAQLRKASDSELERQKGLVED-------TLRQRRQVEEEILALKASFEKAAAgKAELELELGRIRSNAEDT 2095
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRlqdltekLSEAEDMLACEQHALLRKLQPEQD-LQDVRLHLQQCSQELALK 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2096 LRSKEQAELEAA--RQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVER-------LKAKVEEARRLRErae 2166
Cdd:TIGR00618 645 LTALHALQLTLTqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtllreLETHIEEYDREFN--- 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2167 qesarQLQLAQEAAQKRLQAEEKAHAfavqqkeqelqqtlqqeqSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRR 2246
Cdd:TIGR00618 722 -----EIENASSSLGSDLAAREDALN------------------QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2247 QVEEAERLKQLAEEQaqaraqaqaaaekLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELT 2326
Cdd:TIGR00618 779 ELSHLAAEIQFFNRL-------------REEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG 845
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 1820553714 2327 TLRLQLEEtdhqknllDEELQRLKAEATEAARQRSQVEEELFSVRV 2372
Cdd:TIGR00618 846 EITHQLLK--------YEECSKQLAQLTQEQAKIIQLSDKLNGINQ 883
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1451-2034 |
4.96e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1451 QEYVDLRTRYSELTTLTSQY-IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAER 1525
Cdd:COG4913 262 ERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1526 EAKELQQRMQEEVVRREEAAVDAQQQKRSI--------------QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEI 1591
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1592 RVVRLQLEATERQRGGAEGELQALRAQAEEAeaqkrqAQEEAERLR-----RQVQDESQRKRQAeAELALR-------VK 1659
Cdd:COG4913 422 RELEAEIASLERRKSNIPARLLALRDALAEA------LGLDEAELPfvgelIEVRPEEERWRGA-IERVLGgfaltllVP 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1660 AEAEAArekqrALQALEEL----RLQAEEAERRLRQAEVER------ARQVQVALETAQRSAEAELQsKRASFA--EKTA 1727
Cdd:COG4913 495 PEHYAA-----ALRWVNRLhlrgRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELG-RRFDYVcvDSPE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1728 QLERslqeEHVAVAQlreeaeRRAQQQAEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKSLAQAEAEKQKEea 1806
Cdd:COG4913 569 ELRR----HPRAITR------AGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL-- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1807 erearrrgKAEEQAVRHRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEAAAA 1883
Cdd:COG4913 637 --------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1884 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR 1963
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNR 784
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1964 QRAEAERVLAE-KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRRLEEQAAQHKADIEERLAQ 2034
Cdd:COG4913 785 AEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRR 857
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2942-2980 |
6.51e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.12 E-value: 6.51e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 2942 LLEAQIATGGVIDPVHSHRVPVDVAYQRGYFNEEMNRVL 2980
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1196-1956 |
6.98e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.86 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1196 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKtislvirSTQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRA 1274
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKK-------SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1275 QAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERwqavlaqtdvrQRELEQLGRQLRYYRESAd 1354
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEET-----------QERINRARKAAPLAAHIK- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1355 plgAWLQDARQRQEQIQAmpLADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVA 1434
Cdd:TIGR00618 301 ---AVTQIEQQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1435 SPAKKPKVQSGSESVIQEyvDLRTRYSELTTLTSQYIKFISETLRRMEEEERL--AEQQRAEERERLAEVEAALEKQRQ- 1511
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQc 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1512 --LAEAHAQAKAQAEREAKELQQRMqEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQA----------EA 1579
Cdd:TIGR00618 454 ekLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1580 AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRaQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVK 1659
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1660 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVA 1739
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1740 VAQLREEAERRAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrGKAEEQ 1819
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSL-------------------KELMHQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1820 avRHRELAEQELEKQRQ-LAEGTAQQRLAAEQELIR-LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1897
Cdd:TIGR00618 752 --ARTVLKARTEAHFNNnEEVTAALQTGAELSHLAAeIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1898 RAEMEVLLASKARAEEESRSTSEKSKQRLEaeagRFRELAEEAARLRALAEEAKRQRQL 1956
Cdd:TIGR00618 830 EEQFLSRLEEKSATLGEITHQLLKYEECSK----QLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1846-2614 |
7.08e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.06 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1846 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1925
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1926 LEAEAGRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLAE-KLAAISEATRLKTEAEIAL-KEKEAENERL 2003
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2004 RRL---AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKglvedtlrQRRQVEEEILALKASFEKAAAGKAE 2080
Cdd:pfam01576 162 SEFtsnLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK--------AKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2081 LELELgrirsnaedtlrSKEQAELEAARQRqlaaeeeqrrreaeervqkslaAEEEAArQRKAALEEVERLKAKVEEarr 2160
Cdd:pfam01576 234 LRAQL------------AKKEEELQAALAR----------------------LEEETA-QKNNALKKIRELEAQISE--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2161 LRERAEQESArqlQLAQEAAQKRLQAEEkahafavqqkeqelqqtlqqeqsvLDRLRSEAEVARRAAEEAEEARVQAERE 2240
Cdd:pfam01576 276 LQEDLESERA---ARNKAEKQRRDLGEE------------------------LEALKTELEDTLDTTAAQQELRSKREQE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2241 AAQSRRQVEEAERLKQlaeeqaqaraqaqAAAEKLRKDAEQEAVRRAQAEQAALRQKQAadaeMEKHKKFAEQtlrQKAQ 2320
Cdd:pfam01576 329 VTELKKALEEETRSHE-------------AQLQEMRQKHTQALEELTEQLEQAKRNKAN----LEKAKQALES---ENAE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2321 VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALilrDKD--- 2397
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDvss 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2398 ------NTQRFLQEEAekmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLqq 2471
Cdd:pfam01576 466 lesqlqDTQELLQEET---RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL-- 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2472 qkELAQEQARRLQEDKEQMAQQLAEETQGFQR---------------TLEAERQRQLEMSAEAERLKLR--MAEMSRAQA 2534
Cdd:pfam01576 541 --EALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrlqqelddlLVDLDHQRQLVSNLEKKQKKFDqmLAEEKAISA 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2535 RAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA-------IAELEREKEKLQQEAKLLQ 2607
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKRALEQQVEEMK 698
|
....*..
gi 1820553714 2608 LKSEEMQ 2614
Cdd:pfam01576 699 TQLEELE 705
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
296-393 |
1.26e-13 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 69.72 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 371
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1820553714 372 LLDPEDVDVPQPDEKSIITYVS 393
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2279-2497 |
1.38e-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: 75.96 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2279 AEQEAVRRAQAEQAALRQK-QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAA 2357
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2358 RQRSQVEEEL---FSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLA 2434
Cdd:COG4942 97 AELEAQKEELaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2435 EEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEE 2497
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1854-2408 |
1.45e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1854 RLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1933
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1934 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE---AENERLRRLA 2007
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2008 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAEL 2081
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2082 ELELGRIRSNAEDtLRSKE---QAELEAARQR-----------------QLAAEEEQRRREAEERVQKS-LAAEEEAARQ 2140
Cdd:PRK02224 411 EDFLEELREERDE-LREREaelEATLRTARERveeaealleagkcpecgQPVEGSPHVETIEEDRERVEeLEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2141 RKAALEE-VERLKAKVEEARRLRERAEQESArqlqLAQEAAQKRLQAEEKAHAfavqqkeqelqqtlqqeqsvLDRLRse 2219
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRER--------------------AEELR-- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2220 aevarrAAEEAEEARVQAEREAAQSRR-QVEEA-ERLKQLAEEQAQARAQAQAaaekLRKDAE-QEAVRRAQAEQAALRQ 2296
Cdd:PRK02224 544 ------ERAAELEAEAEEKREAAAEAEeEAEEArEEVAELNSKLAELKERIES----LERIRTlLAAIADAEDEIERLRE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2297 KQAADAEMEKHKKFAEQTLRQ-KAQVEQELTTLRlqLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQME 2375
Cdd:PRK02224 614 KREALAELNDERRERLAEKRErKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
570 580 590
....*....|....*....|....*....|....
gi 1820553714 2376 ELSKLKARIEA-ENRALILRDkdntqrfLQEEAE 2408
Cdd:PRK02224 692 ELEELRERREAlENRVEALEA-------LYDEAE 718
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
296-396 |
2.24e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 69.29 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 375
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1820553714 376 ED-VDVPQPDEKSIITYVSSLY 396
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2469-2891 |
2.65e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2469 LQQQKELAqEQARRLQEDKEQM-AQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQA 2547
Cdd:COG1196 205 LERQAEKA-ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2548 EEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEmqtvqqeqLLQETQA 2627
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE--------AEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2628 LQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQmeqerqrlvASMEEARQRQHEAEEGVRRKQ 2707
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL---------EEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2708 EELQQLEQQRRQQEELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQVAAtktlpngRDALDGPATEAEPEHSFDGLR 2787
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA-------LAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2788 QKVPAQRLQeaGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLLLKPTSEKLSVYAALQRQLLSPGTALILL 2867
Cdd:COG1196 500 EADYEGFLE--GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420
....*....|....*....|....
gi 1820553714 2868 EAQAASGFLLDPVRNRRLTVNEAV 2891
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAV 601
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2312-2607 |
2.91e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.70 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2312 EQTLRQKAQVEQELTTLRLQLEETDHQKNLlDEELQRLKAEATEAARQRSQVEEELFSV--RVQMEELSKLK-------A 2382
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2383 RIEAENRALILRDKDNTQRFLQEEaekmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR-----------ALAEKMLKE 2451
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMRELERLQMERQQknervrqeleaARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2452 KMQAVQEATRLKAEaELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQlemsAEAERLKLRMAEMSR 2531
Cdd:pfam17380 410 ERQRKIQQQKVEME-QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE----EERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2532 AQARAEEDAqrfRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREaiAELEREKEKLQQEAKLLQ 2607
Cdd:pfam17380 485 DRKRAEEQR---RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEERRRIQ 555
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3194-3232 |
4.82e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 4.82e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 3194 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 3232
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
199-278 |
6.31e-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: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 199 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 270
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1820553714 271 LGLIWTII 278
Cdd:cd21223 105 LALLWRII 112
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1493-2446 |
6.42e-13 |
|
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: 76.14 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1493 AEERERLaeVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVvrreeaavdAQQQKRsiQEELQQLRQSSE---AE 1569
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQL-----AEEQYRLVEMAREL---------EELSAR--ESDLEQDYQAASdhlNL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1570 IQAKARQAEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraqaEEAEAQKRQAQEEAERLRRQVQDesqrkrq 1649
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD------- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1650 aeaelalrvkaeaeaareKQRALQALEELRLQAEEAERRLrqaevERARQVQVALETAQRSAEAELQSKRASFAEKTAQ- 1728
Cdd:COG3096 401 ------------------YQQALDVQQTRAIQYQQAVQAL-----EKARALCGLPDLTPENAEDYLAAFRAKEQQATEEv 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1729 --LERSLQEEHVAVAQLReeaerraqqqaeaerareeaerelerwqlKANEALRL------RLQAEEVAQQkslaqaeae 1800
Cdd:COG3096 458 leLEQKLSVADAARRQFE-----------------------------KAYELVCKiageveRSQAWQTARE--------- 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1801 kqkeeaerearrrgkAEEQAVRHRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQhea 1880
Cdd:COG3096 500 ---------------LLRRYRSQQALAQRLQQLRAQLAE--LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELL--- 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1881 AAATQKRQELEAELAKVRAEmevllASKARAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEED 1960
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQ-----RSELRQQLEQ---LRARIKELAARAPAWLAAQDALERLREQSGEALADSQ--EVT 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1961 AARQR-AEAERVL-AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAE-------DEAFQRRRLEEQAAqhkadIEER 2031
Cdd:COG3096 630 AAMQQlLEREREAtVERDELAARKQALESQIERLSQPGGAEDPRLLALAErlggvllSEIYDDVTLEDAPY-----FSAL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2032 LAQLRKA---SDSELERQK--GLvEDTLRQRRQVEEEILALKASFEKAAagkaelELELGRIRSNAEDTLRSKEQAEL-- 2104
Cdd:COG3096 705 YGPARHAivvPDLSAVKEQlaGL-EDCPEDLYLIEGDPDSFDDSVFDAE------ELEDAVVVKLSDRQWRYSRFPEVpl 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2105 --EAARQRQLaaeeeqrrreaeervqkslaaeEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLA------ 2176
Cdd:COG3096 778 fgRAAREKRL----------------------EELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpe 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2177 ---QEAAQKRLQAEEKAHAFAVQ-QKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQV--EE 2250
Cdd:COG3096 836 aelAALRQRRSELERELAQHRAQeQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQAFiqQH 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2251 AERLKQLAEEQAQaraqaqaaaekLRKDAEQE-----AVRRAQAEQAALRQKQAADAE-MEKHKKFAEQ----------- 2313
Cdd:COG3096 916 GKALAQLEPLVAV-----------LQSDPEQFeqlqaDYLQAKEQQRRLKQQIFALSEvVQRRPHFSYEdavgllgensd 984
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2314 ---TLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEElfsvrvqMEELSkLKARIEAENR 2389
Cdd:COG3096 985 lneKLRARlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE-------LEELG-VQADAEAEER 1056
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2390 ALILRDKDNTQ----RFLQEEAEKMKQVAEEAARlsvaaQEAARLRQlAEEDLAQQRALAE 2446
Cdd:COG3096 1057 ARIRRDELHEElsqnRSRRSQLEKQLTRCEAEMD-----SLQKRLRK-AERDYKQEREQVV 1111
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2130-2826 |
9.79e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2130 SLAAEEEAARQRKAALEEVERLKAKVEEARRlRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2209
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2210 QSVLDRLRSEaevarraaeeaeearvqaeREAAQSRRqVEEAERLKQLAEEQAQARAQAQAAAEKLRKdaeQEAVRRAQA 2289
Cdd:PTZ00121 1154 VEIARKAEDA-------------------RKAEEARK-AEDAKKAEAARKAEEVRKAEELRKAEDARK---AEAARKAEE 1210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2290 EQAALRQKQAADAEMEKHKKFAEQTlRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEElfS 2369
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA--E 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2370 VRVQMEELSKLKARIEAENRALILRDKDNTQRfLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2449
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2450 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmaqqlAEETqgfqRTLEAERQRQLEMSAEAErlKLRMAEM 2529
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-----ADEL----KKAAAAKKKADEAKKKAE--EKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2530 SRAQARAEEDAQRFRKQAEEiGEKLHRTELATQEKvtlvqtleiqrqqsdHDAERLREAiAELEREKEKLQQEAKLLQLK 2609
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEE-AKKAEEAKKKAEEA---------------KKADEAKKK-AEEAKKADEAKKKAEEAKKK 1498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2610 SEEMqtvqqeqllqetqalqqsflsekdsllqreRFIEQEKAKLEQLFQDEVAKAQqlreeqqrqqqqmeqerqrlvasm 2689
Cdd:PTZ00121 1499 ADEA------------------------------KKAAEAKKKADEAKKAEEAKKA------------------------ 1524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2690 EEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLrEQLQRLEEQHRAALAHSEEVTALQVAatktlpngrda 2769
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA-EEAKKAEEDKNMALRKAEEAKKAEEA----------- 1592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2770 ldgpateaepehsfdglRQKVPAQRLQEAGILSAEELQRLAQGHTTVDELARREDVR 2826
Cdd:PTZ00121 1593 -----------------RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1824-2488 |
1.59e-12 |
|
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: 74.62 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1824 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRaEMEV 1903
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1904 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE-EDAARQRAEAERVLAEKLAAISEA 1982
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKrAAHVKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1983 TRLKTEAEIALKEKE------AENERLRRLAEDEAFQRRRLeeQAAQHKADIEERLAQLRKASDSE--LERQKGLVEDTL 2054
Cdd:TIGR00618 355 IHIRDAHEVATSIREiscqqhTLTQHIHTLQQQKTTLTQKL--QSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2055 RQRRQVEEEILALKASFEKAAAGKAELEL-ELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAA 2133
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2134 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSV 2212
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFsILTQCDNRSKEDIPNLQNI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2213 LDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQA 2292
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2293 ALRQKQAADAEMEKHKKfaEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRV 2372
Cdd:TIGR00618 673 ELLASRQLALQKMQSEK--EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2373 QMEElsKLKARIEAENRA------LILRD------KDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQ 2440
Cdd:TIGR00618 751 QART--VLKARTEAHFNNneevtaALQTGaelshlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ 828
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1820553714 2441 QRALAEKMLKEKMQAVQEATR-LKAEAELLQQQKELAQEQARRLQEDKE 2488
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHqLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
183-284 |
1.99e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 66.88 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 183 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 255
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHFQIS 284
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
298-397 |
2.03e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 66.21 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 298 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 373
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1820553714 374 DPEDVdVPQPDEKSIITYVSSLYD 397
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1825-2706 |
2.25e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.06 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1825 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAeME 1902
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1903 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEA 1982
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1983 TRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQ---------------AAQH--KADIEERLAQLRKASDSELER 2045
Cdd:pfam01576 267 REL--EAQISELQEDLESERAARNKAEK--QRRDLGEElealkteledtldttAAQQelRSKREQEVTELKKALEEETRS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2046 QKGLVEDTLRQRRQVEEEilaLKASFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEAARQRQlaaeeeqrrrE 2122
Cdd:pfam01576 343 HEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK----------K 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2123 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARqlqLAQEAAQKRLQaeekahafaVQQKEQEL 2202
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSSLESQ---------LQDTQELL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2203 QQTLQQEQSVLDRLRSEAEvarraaeeaeearvqaerEAAQSRRQVEEAERLKQ-LAEEQAQARAQAQAAAEKLRKDAE- 2280
Cdd:pfam01576 478 QEETRQKLNLSTRLRQLED------------------ERNSLQEQLEEEEEAKRnVERQLSTLQAQLSDMKKKLEEDAGt 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2281 ----QEAVRRAQAEQAALRQKqaadaeMEKHKKFAEQTLRQKAQVEQELTTLRLQLeetDHQKNLL----------DEEL 2346
Cdd:pfam01576 540 lealEEGKKRLQRELEALTQQ------LEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVsnlekkqkkfDQML 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2347 QRLKAEATEAARQRSQVEEE-------LFSVRVQMEELSKLKARIEAENRAL------ILRDKDNTQRFLQEeAEKMKQV 2413
Cdd:pfam01576 611 AEEKAISARYAEERDRAEAEareketrALSLARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHE-LERSKRA 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2414 AEeaarlsvaaQEAARLR-QLAE-EDLAQQRALAEKMLKEKMQAvqeatrLKAEAEL-LQQQKELAQEQARRLQEDKEQM 2490
Cdd:pfam01576 690 LE---------QQVEEMKtQLEElEDELQATEDAKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLVKQVREL 754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2491 AQQLAEETQgfQRTLEAERQRQLEMsaEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQT 2570
Cdd:pfam01576 755 EAELEDERK--QRAQAVAAKKKLEL--DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2571 LEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQlksEEMQtvqqeqllqetqalqqSFLSEKDSLLQRERFIEQEK 2650
Cdd:pfam01576 831 SEKKLKNLEAELLQLQEDLAASERARRQAQQERDELA---DEIA----------------SGASGKSALQDEKRRLEARI 891
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2651 AKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvASMEEARQRQHEAEEGVRRK 2706
Cdd:pfam01576 892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL-AAERSTSQKSESARQQLERQ 946
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1830-2611 |
2.34e-12 |
|
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: 73.85 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1830 ELEKQRQLAEGTAQQRLAAEQELIrlrAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKA 1909
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAE---LLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1910 RAEEESRSTSEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLAEKLAAISEATRLKTEA 1989
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIE-----ELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1990 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR-RQVEEEILALK 2068
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2069 ASFEKAAAGKAELELELGRIrsNAEDTLRSKEQAELEAAR-QRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE 2147
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2148 VERLKAKVEEARRLRERAEQESARQLQLAQEaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAA 2227
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2228 EEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAvrRAQAEQAALRQKQAADAEMEKH 2307
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS--EAEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2308 KKFAEQTLRQKAQveqelttlRLQLEETdhqknlldeelqRLKAEATEAARQRsqVEEELFSVRVQMEELSKLKarieae 2387
Cdd:TIGR00618 627 LQDVRLHLQQCSQ--------ELALKLT------------ALHALQLTLTQER--VREHALSIRVLPKELLASR------ 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2388 nralilrdkdntQRFLQEEAEKMKQVAEEAARLsvaAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE 2467
Cdd:TIGR00618 679 ------------QLALQKMQSEKEQLTYWKEML---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2468 LLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQA 2547
Cdd:TIGR00618 744 SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2548 EEIGEKLHRTELATQEKVTLVQTLeiqRQQSDHDAERLReaiaeleREKEKLQQEAKLLQLKSE 2611
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEI---THQLLKYEECSK-------QLAQLTQEQAKIIQLSDK 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1543-1743 |
2.75e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.10 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1543 EAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEA 1622
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1623 EAQKRQAQEEAERLRRQVQdesQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEVERA 1697
Cdd:COG4942 96 RAELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1820553714 1698 RQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1743
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1563-2189 |
4.15e-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: 73.33 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1563 RQSSEAEIQAKARQAEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR-----AQAEEAEAQKRQAQEEAER 1635
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHfgyksDETLIASRQEERQETSAEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1636 LRRQVQDESQRKrQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAeL 1715
Cdd:pfam12128 289 NQLLRTLDDQWK-EKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-L 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1716 QSKRASFAEKTAQLERSLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1794
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1795 AQAEAEKQKEEAEREARRRGKAEEQAVRH-RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEel 1873
Cdd:pfam12128 447 GELKLRLNQATATPELLLQLENFDERIERaREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1874 ARLQHEAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALA 1947
Cdd:pfam12128 525 LELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASE 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1948 EEAKRQRQLAEEDAARQR---AEAERVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQH 2024
Cdd:pfam12128 600 EELRERLDKAEEALQSARekqAAAEEQLVQANGELEKASREETFARTALKNAR---LDLRRLFDEKQSEKDKKNKALAER 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2025 KADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEkaaagkAELELELGRIRSN--AEDTLRSKEQA 2102
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSGAKAELK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2103 ELEAARQRQLAAEEEQRRREAEERVQ-KSLAAEEEAARQRKAA------------LEEVERLKAKVEEARRLRERAEQES 2169
Cdd:pfam12128 751 ALETWYKRDLASLGVDPDVIAKLKREiRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAISELQQQL 830
|
650 660
....*....|....*....|
gi 1820553714 2170 ARQlqlaQEAAQKRLQAEEK 2189
Cdd:pfam12128 831 ARL----IADTKLRRAKLEM 846
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4448-4486 |
4.17e-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: 4.17e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 4448 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4486
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
298-398 |
4.46e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 65.45 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 298 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 377
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1820553714 378 VdVPQPDEKSIITYVSSLYDA 398
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3936-3974 |
5.37e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 5.37e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 3936 LLDAQLATGGIVDPHLGFHLPLEVAYQRGYLNKDTHDQL 3974
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1820-2601 |
5.57e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.06 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1820 AVRHRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEAAAATQK----RQ 1888
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1889 ELEAELAKVRAEMEVLLA---SKARAEEESRSTSEKSK----------QRLEAE---AGRFR------ELAEEAARLRAL 1946
Cdd:COG3096 355 DLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEVDslksqladyqQALDVQqtrAIQYQqavqalEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1947 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlrrlaeDEAFQR-RRLEEQAAQHK 2025
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER------SQAWQTaRELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2026 AdIEERLAQLRkASDSELERQkglvedtLRQRRQVEEeilaLKASFEKAAAGKAELELELGRIRSNAEDTL-RSKEQAEL 2104
Cdd:COG3096 509 A-LAQRLQQLR-AQLAELEQR-------LRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLeELEEQAAE 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2105 EAARQRQLAAEEEQRRREAEERVQKS---LAAEEEAAR---QRKAALEE-----------VERLKAKVEEARRLRERAEQ 2167
Cdd:COG3096 576 AVEQRSELRQQLEQLRARIKELAARApawLAAQDALERlreQSGEALADsqevtaamqqlLEREREATVERDELAARKQA 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2168 --ESARQLQLAQEAAQKRLQA-------------------EEKA----------HAFAVQQKEQELQQTLQQEQSVLDRL 2216
Cdd:COG3096 656 leSQIERLSQPGGAEDPRLLAlaerlggvllseiyddvtlEDAPyfsalygparHAIVVPDLSAVKEQLAGLEDCPEDLY 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2217 RSEAEVARRAAEEAEEARVQAEREAAQSRRQVE-----------EAERLKQLaeeqaqaraqaqaaaEKLRKDAEQEAVR 2285
Cdd:COG3096 736 LIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRysrfpevplfgRAAREKRL---------------EELRAERDELAEQ 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2286 RAQAeqAALRQK-----QAADAEMEKHKKFAEQtlrqkAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQR 2360
Cdd:COG3096 801 YAKA--SFDVQKlqrlhQAFSQFVGGHLAVAFA-----PDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2361 SQVEEELFSVRVQMEElsKLKARIEAENRAliLRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQ 2440
Cdd:COG3096 874 QLLNKLLPQANLLADE--TLADRLEELREE--LDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2441 QRALAEKM--LKEKMQ-----AVQEATRLKAEA----ELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQrTLEAER 2509
Cdd:COG3096 950 QRRLKQQIfaLSEVVQrrphfSYEDAVGLLGENsdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSR 1028
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2510 QRQLEMSAEAERlklRMAEMS-RAQARAEEDAQRFRKqaeEIGEKLHRTElatQEKVTLVQTLEIQRQQSDHDAERLREA 2588
Cdd:COG3096 1029 DAKQQTLQELEQ---ELEELGvQADAEAEERARIRRD---ELHEELSQNR---SRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
890
....*....|...
gi 1820553714 2589 IAELEREKEKLQQ 2601
Cdd:COG3096 1100 ERDYKQEREQVVQ 1112
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
298-393 |
5.76e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.10 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 298 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 376
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1820553714 377 DVDVPQPDEKSIITYVS 393
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2866-2904 |
7.34e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.34e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 2866 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2904
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1247-2018 |
7.87e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.29 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1247 EQLKEAQAVPATlpELEATKASLKKLRAQAEAQ------QPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERV-- 1318
Cdd:COG3096 316 EELSARESDLEQ--DYQAASDHLNLVQTALRQQekieryQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVds 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1319 --AQLLERWQAVlaqtDVRQRE----------LEQLGRQLRYYRESADPLGAWLQDARQRQEQI------QAMPLADSQA 1380
Cdd:COG3096 394 lkSQLADYQQAL----DVQQTRaiqyqqavqaLEKARALCGLPDLTPENAEDYLAAFRAKEQQAteevleLEQKLSVADA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1381 VREQLRQEKALLEEIERHGEKVEECQRfAKQYINAIKDYELQLvtykAQLEPVAspakkpkvqsgsesviQEYVDLRTRY 1460
Cdd:COG3096 470 ARRQFEKAYELVCKIAGEVERSQAWQT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1461 S---ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaeahaqakaqaEREAKELQQRMQEe 1537
Cdd:COG3096 529 RqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSEL-----------RQQLEQLRARIKE- 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1538 VVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaERSRLRIEEEIRVVRLQLEATER---QRGGAE-GELQ 1613
Cdd:COG3096 597 LAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQALESQIErlsQPGGAEdPRLL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1614 ALRAQ-----------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQRKRQaEA 1652
Cdd:COG3096 676 ALAERlggvllseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVFDAE-EL 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1653 ELALRVKAE---------------AEAAREKQralqaLEELRLQAEE-----AERRLRQAEVER---------ARQVQVA 1703
Cdd:COG3096 755 EDAVVVKLSdrqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvGGHLAVA 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1704 LETaqrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRA-------QQQAEAERAREEAERELERWQLKAN 1776
Cdd:COG3096 830 FAP---DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELREELDAAQ 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1777 EALR-LRLQAEEVAQ-QKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQ-LAEGTAQQRLAAEQELI 1853
Cdd:COG3096 907 EAQAfIQQHGKALAQlEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLN 986
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1854 -RLRAETEQGEQQRQLLEEELARLQHEAAAATQKR--------------QELEAELAK--VRAEMEVLLASKARAEE--- 1913
Cdd:COG3096 987 eKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQELEElgVQADAEAEERARIRRDElhe 1066
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1914 ------ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKR-----QRQLAEEDAARQ--RAEAERVLAEKL 1976
Cdd:COG3096 1067 elsqnrSRRSQLEKQLTRCEAEmdslQKRLRKAERDYKQEREQVVQAKAgwcavLRLARDNDVERRlhRRELAYLSADEL 1146
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1820553714 1977 AAISEatrlktEAEIALKEKEAENERLR---RLAEDEAFQRRRLE 2018
Cdd:COG3096 1147 RSMSD------KALGALRLAVADNEHLRdalRLSEDPRRPERKVQ 1185
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1652-2188 |
9.50e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 72.20 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1652 AELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSAEAELQSKRAS--------- 1721
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1722 -FAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAE 1800
Cdd:COG3899 792 aRAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1801 KQKEEAEREARRrgkAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEA 1880
Cdd:COG3899 872 ALAAAAAAAAAA---AALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1881 AAATQKRQELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1960
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1961 AARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASD 2040
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2041 SELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRR 2120
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 2121 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2188
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4103-4141 |
9.75e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 9.75e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 4103 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4141
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1919-2656 |
9.86e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.02 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1919 SEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIsEATRLKTEAEIALKEK-- 1996
Cdd:TIGR02169 170 RKKEKALEELE-----EVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKea 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1997 -EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAA 2075
Cdd:TIGR02169 242 iERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2076 AGKAELELELGRIRSNAEDtlrSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQR---KAALEEVERLK 2152
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2153 AKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRseaeva 2223
Cdd:TIGR02169 399 REINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY------ 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2224 rraaeEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKD-----AEQEAVRRAQA---EQAALR 2295
Cdd:TIGR02169 473 -----DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvAQLGSVGERYAtaiEVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2296 QKQAADAEMEKHKKFAEQTLRQKA----------QVEQELTTLRLQLEE--TDHQKNLLDEELQRlkAEATEAARQRSQV 2363
Cdd:TIGR02169 548 RLNNVVVEDDAVAKEAIELLKRRKagratflplnKMRDERRDLSILSEDgvIGFAVDLVEFDPKY--EPAFKYVFGDTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2364 EEELFSVRVQMeelskLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRA 2443
Cdd:TIGR02169 626 VEDIEAARRLM-----GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL--SSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2444 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLK 2523
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2524 LRMAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEA 2603
Cdd:TIGR02169 779 EALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2604 KLLQLKSEEMQTVQQEQLLQETQalqqsfLSEKDSLLQRERfiEQEKAKLEQL 2656
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRD------LESRLGDLKKER--DELEAQLREL 901
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1815-2031 |
1.29e-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: 69.79 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1894
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1895 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1970
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 1971 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 2031
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1462-1679 |
1.57e-11 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 70.29 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1462 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAEREA 1527
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1528 KELQQRMQEEVVRRE-EAAVDAQQQKRsiQEELQQlrqssEAEIQAKARQAEAAERSRLRIEEEirvvrlqLEATERQRg 1606
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANA--EREVQR-----QLEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1607 gAEGELQALRAQAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELR 1679
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1450-2446 |
2.05e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1450 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKE 1529
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1530 LQQRMQeevvrreeAAVDAQQqkrSIQEELQQlrqsSEAEIQAKARQAEAAErsrlRIEEeirvvrlQLEATERQRGgae 1609
Cdd:PRK04863 326 LEQDYQ--------AASDHLN---LVQTALRQ----QEKIERYQADLEELEE----RLEE-------QNEVVEEADE--- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1610 gelqalraQAEEAEAQKRQAQEEAERLRRQVQDesqrkrqaeaelalrvkaeaeaareKQRALQALEELRLQAEEAERRL 1689
Cdd:PRK04863 377 --------QQEENEARAEAAEEEVDELKSQLAD-------------------------YQQALDVQQTRAIQYQQAVQAL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1690 rqaevERARQVQVALETAQRSAE---AELQSKRASFAEKTAQLERSLQEEHVAVAQLReeaerraqqqaeaerareeaer 1766
Cdd:PRK04863 424 -----ERAKQLCGLPDLTADNAEdwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE---------------------- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1767 elerwqlKANEALRL------RLQAEEVAQQkslaqaeaekqkeeaerearrrgkAEEQAVRHRELAEQELEKQRQLAEg 1840
Cdd:PRK04863 477 -------QAYQLVRKiagevsRSEAWDVARE------------------------LLRRLREQRHLAEQLQQLRMRLSE- 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1841 tAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAtqkRQELEAELAKVRAEMEVLlaskaRAEEESrstSE 1920
Cdd:PRK04863 525 -LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR---LESLSESVSEARERRMAL-----RQQLEQ---LQ 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1921 KSKQRLEAEAGRFRELAEEAARLRALAEEA---------KRQRQLAEEDAARQraEAERVLAEKLAAISEATRLkteaei 1991
Cdd:PRK04863 593 ARIQRLAARAPAWLAAQDALARLREQSGEEfedsqdvteYMQQLLERERELTV--ERDELAARKQALDEEIERL------ 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1992 aLKEKEAENERLRRLAED-------EAFQRRRLEEQAAqhkadIEERLAQLRKA---SD-SELERQKGLVEDTLRQRRQV 2060
Cdd:PRK04863 665 -SQPGGSEDPRLNALAERfggvllsEIYDDVSLEDAPY-----FSALYGPARHAivvPDlSDAAEQLAGLEDCPEDLYLI 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2061 EEEILALKAS------FEKAAAGK-AELELELGRIRSnaedtlrskEQAELEAARQRQLaaeeeqrrreaeervqkslaa 2133
Cdd:PRK04863 739 EGDPDSFDDSvfsveeLEKAVVVKiADRQWRYSRFPE---------VPLFGRAAREKRI--------------------- 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2134 eEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLA---------QEAAQKRLQAEEKAHAFAVQ-QKEQELQ 2203
Cdd:PRK04863 789 -EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeaelRQLNRRRVELERALADHESQeQQQRSQL 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2204 QTLQQEQSVLDRLRSEAEVARRAAEEAeearvqaerEAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEA 2283
Cdd:PRK04863 868 EQAKEGLSALNRLLPRLNLLADETLAD---------RVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFE 938
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2284 VRRAQAEQAALRQKQAadaemeKHKKFAEQTLRQKAQ------------VEQELT-TLRLQLEETDHQKNLLDEELQRLK 2350
Cdd:PRK04863 939 QLKQDYQQAQQTQRDA------KQQAFALTEVVQRRAhfsyedaaemlaKNSDLNeKLRQRLEQAEQERTRAREQLRQAQ 1012
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2351 AEATEAarqrSQVEEEL---FSVRVQM-----EELSKL--KARIEAENRALILRDKDNTQrfLQEEAEKMKQVAEEAARL 2420
Cdd:PRK04863 1013 AQLAQY----NQVLASLkssYDAKRQMlqelkQELQDLgvPADSGAEERARARRDELHAR--LSANRSRRNQLEKQLTFC 1086
|
1050 1060
....*....|....*....|....*.
gi 1820553714 2421 SVAAQEAARLRQLAEEDLAQQRALAE 2446
Cdd:PRK04863 1087 EAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2128-2823 |
3.94e-11 |
|
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: 70.09 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2128 QKSLAAEEEAARQRKAALEEVER----LKAKVEEARRLRERAEQESARQLQLA----QEAAQKRLQAEEKAHAfaVQQKE 2199
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERqlksLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKE--AEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2200 QELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEA-ERLKQLAEEQAQARAQAQAAAEKLRKD 2278
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILrERLANLERQLEELEAQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2279 AEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAAR 2358
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL-EEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2359 QRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEED 2437
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAeQALDAAERELAQLQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2438 LAQQRALA-------------------------------------EKMLKEKMQA--VQEATRLKAEAELLQQQK----- 2473
Cdd:TIGR02168 495 ERLQENLEgfsegvkallknqsglsgilgvlselisvdegyeaaiEAALGGRLQAvvVENLNAAKKAIAFLKQNElgrvt 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2474 --ELAQEQARRLQEDKEQM----------------------------------------AQQLAEETQGFQR--TLEAER 2509
Cdd:TIGR02168 575 flPLDSIKGTEIQGNDREIlkniegflgvakdlvkfdpklrkalsyllggvlvvddldnALELAKKLRPGYRivTLDGDL 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2510 QR---------------QLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQ 2574
Cdd:TIGR02168 655 VRpggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2575 RQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLE 2654
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2655 QLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQ 2734
Cdd:TIGR02168 814 LL-NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2735 LQRLEEQHRAALAHSEEVTALQvaatktlpNGRDALDGPATEAEPEhsFDGLRQKVP--AQRLQEAGILSAEELQRLAQG 2812
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELR--------RELEELREKLAQLELR--LEGLEVRIDnlQERLSEEYSLTLEEAEALENK 962
|
810
....*....|.
gi 1820553714 2813 HTTVDELARRE 2823
Cdd:TIGR02168 963 IEDDEEEARRR 973
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3270-3308 |
4.98e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 4.98e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 3270 LLDAQLSTGGVVDPSKSHHVPLDVAYARGCLDEETSRAL 3308
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1988-2437 |
5.05e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1988 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILAL 2067
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2068 KASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAARQRQLaaeeeqrrrEAEERVQKSLAAEEEAARQRKAALEE 2147
Cdd:COG4717 145 PERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSL---------ATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2148 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAA 2227
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2228 EEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAE--QEAVRRAQAEQAALRQKQAADAEME 2305
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEelQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2306 KHKKF---AEQTLRQKAQVEQELTTLRLQLEETDHQ-KNLLDEELQRLKAEATEAARQR-SQVEEELFSVRVQMEELSKL 2380
Cdd:COG4717 375 LLAEAgveDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREE 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 2381 KARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEED 2437
Cdd:COG4717 455 LAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1488-1686 |
5.47e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.91 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1488 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREeaavdAQQQKrsiQEELQQLRQSS 1566
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1567 EAEIQAKARQAEAAERSRlRIEEEIRVvRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERlrrqVQDESQR 1646
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAKK-KAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1820553714 1647 KRQAEAELAL-RVKAEAEAAREKQRALQALEELRLQAEEAE 1686
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1815-2192 |
5.64e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAE-GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1893
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1894 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED-----------AA 1962
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleqleneleaaAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1963 RQRAEAERVLAEKLAAI--------SEATRLKTEAEIAL-----------------KEKEAENERLRRLAEDEAFQRRRL 2017
Cdd:COG4717 242 EERLKEARLLLLIAAALlallglggSLLSLILTIAGVLFlvlgllallflllarekASLGKEAEELQALPALEELEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2018 EEQAAQHKADIEERLAQLRKASDSELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTL 2096
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2097 RSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQ 2174
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELL 475
|
410
....*....|....*...
gi 1820553714 2175 LAQEAAQKRLQAEEKAHA 2192
Cdd:COG4717 476 QELEELKAELRELAEEWA 493
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1154-1739 |
6.28e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.60 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1154 RECAQRITEQQKAQAEVEGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEqvrslsaiylEKLKTISLVIR 1233
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELE----------AQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1234 STQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRAQAEAQqpmFDALRDELRGAQEVGERLQQRHGERDvEVE 1312
Cdd:COG3096 575 EAVEQRSELRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA---LADSQEVTAAMQQLLEREREATVERD-ELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1313 RWRERVAQLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLGAWLQDARqrqeqiQAMPLADSQAVREQL 1385
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPAR------HAIVVPDLSAVKEQL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1386 RQEKALLEE---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKVQSGSESVIQEYVDL 1456
Cdd:COG3096 725 AGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEELRAERDELAEQYAKA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1457 RTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAKELQQRMQE 1536
Cdd:COG3096 805 SFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLKEQLQLLNKLLP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1537 EVV---------RREEAAVD---AQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE 1602
Cdd:COG3096 882 QANlladetladRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1603 --RQR------GGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRAL-Q 1673
Cdd:COG3096 962 evVQRrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELeQ 1040
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1674 ALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--KRASFAEKTAQLERSLQEEHVA 1739
Cdd:COG3096 1041 ELEELGVQAdAEAEERARirrdelHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQEREQVVQAKA 1115
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
176-275 |
7.08e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 62.44 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 247
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1820553714 248 RHRQVKLVNIRNDDIADGNPKLTLGLIW 275
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1518-2756 |
9.68e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 68.66 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1518 QAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQqlrqsSEAEIQAKARQAEAAERSRLRIEEEIrvvrlq 1597
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1598 leaterqrggaegeLQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEAElalrvkaeaEAAREKqralqalee 1677
Cdd:pfam01576 77 --------------LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEE---------EAARQK--------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1678 LRLQAEEAERRLRQAEVErarqvqVALETAQRSaeaELQSKRASFAEKTAQLERSLQEEHVAV---AQLREEAERRAQQQ 1754
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAkslSKLKNKHEAMISDL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1755 AEAERAREEAERELERWQLKAN-EALRLRlqaEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEK 1833
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKLEgESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1834 QRQLAEgtAQQRLAAEqelirlRAETEQGEQQRQLLEEELARLQHE---AAAATQKRQELEAelakvRAEMEVLLASKAr 1910
Cdd:pfam01576 270 EAQISE--LQEDLESE------RAARNKAEKQRRDLGEELEALKTEledTLDTTAAQQELRS-----KREQEVTELKKA- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1911 AEEESRSTSEKSKQRLEAEAGRFRELAEEAarlralaEEAKRQRQLAEEdaARQRAEAERV-LAEKLAAISEAtrlKTEA 1989
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHTQALEELTEQL-------EQAKRNKANLEK--AKQALESENAeLQAELRTLQQA---KQDS 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1990 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE-------------RLAQLRKASDSELERQKGLVEDTLRQ 2056
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESvssllneaegkniKLSKDVSSLESQLQDTQELLQEETRQ 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2057 R-------RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQ--AELEAARQrqlaaeeeqrrreaeerV 2127
Cdd:pfam01576 484 KlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdaGTLEALEE-----------------G 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2128 QKSLAAEEEAARQRkaaLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKAhafavqqk 2198
Cdd:pfam01576 547 KKRLQRELEALTQQ---LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKA-------- 615
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2199 eqelqqtlqqeqsVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKlrKD 2278
Cdd:pfam01576 616 -------------ISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGK--NV 680
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2279 AEQEAVRRAQAEQAALRQKQAADAE-----MEKHKKFAEQTLRQ-KAQVEQELTTLRLQLEEtdhQKNLLDEELQRLKAE 2352
Cdd:pfam01576 681 HELERSKRALEQQVEEMKTQLEELEdelqaTEDAKLRLEVNMQAlKAQFERDLQARDEQGEE---KRRQLVKQVRELEAE 757
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2353 ATEAARQRSQveeeLFSVRVQME-ELSKLKARIEAENRAlilrdkdntqrflQEEAekMKQVAEEAARLSVAAQEAARLR 2431
Cdd:pfam01576 758 LEDERKQRAQ----AVAAKKKLElDLKELEAQIDAANKG-------------REEA--VKQLKKLQAQMKDLQRELEEAR 818
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2432 QLAEEDLAQQRAlAEKMLKekmqavqeatrlKAEAELLQQQKELA-QEQARR-LQEDKEQMAQQLAEETQGfqRTLEAER 2509
Cdd:pfam01576 819 ASRDEILAQSKE-SEKKLK------------NLEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDE 883
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2510 QRQLEmsaeaERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDHDAERLREAI 2589
Cdd:pfam01576 884 KRRLE-----ARIAQLEEELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKELKAKL 954
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2590 AELE---REKEKLQ---QEAKLLQLksEEMQTVQQEQLLQETQALQQSFLSEKDSLLQrerfIEQEKAKLEQlFQDEVAK 2663
Cdd:pfam01576 955 QEMEgtvKSKFKSSiaaLEAKIAQL--EEQLEQESRERQAANKLVRRTEKKLKEVLLQ----VEDERRHADQ-YKDQAEK 1027
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2664 AQqlreeqqrqqqqmeqerqrlvasmeeARQRQheaeegvrrkqeelqqLEQQRRQQEellaEENQRL---REQLQR-LE 2739
Cdd:pfam01576 1028 GN--------------------------SRMKQ----------------LKRQLEEAE----EEASRAnaaRRKLQReLD 1061
|
1290
....*....|....*..
gi 1820553714 2740 EQHRAALAHSEEVTALQ 2756
Cdd:pfam01576 1062 DATESNESMNREVSTLK 1078
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1785-2167 |
1.19e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1785 AEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQ 1864
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1865 QRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1944
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1945 ALAEEAKRQRQLAEE----DAARQRAEAERV--LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAF------ 2012
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierlee 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2013 QRRRLEEQAAQHKADIEE---RLAQLRKAS---DSELERQKglvEDTLRQRRQVEEEILALKASFEKAAAGKAELElELG 2086
Cdd:PRK02224 517 RREDLEELIAERRETIEEkreRAEELRERAaelEAEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2087 RIRS------NAEDTL-----RSKEQAELEAARQRQLaaeeeqrrreaeervqkslaaeeEAARQRKAALEEvERLKAKV 2155
Cdd:PRK02224 593 RIRTllaaiaDAEDEIerlreKREALAELNDERRERL-----------------------AEKRERKRELEA-EFDEARI 648
|
410
....*....|..
gi 1820553714 2156 EEARRLRERAEQ 2167
Cdd:PRK02224 649 EEAREDKERAEE 660
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1232-2110 |
1.56e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.06 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1232 IRSTQGAEEVLRAHEEQLKEAQAvpatlpeleatkaSLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQ--RHGERdv 1309
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQY-------------RLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1310 eVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVReQLRQEK 1389
Cdd:COG3096 349 -IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1390 ALLEEIERHGEKVEEcqrfakqyinaikdyelQLVTYKAQLEpvaspakkpkvqsgseSVIQEYVDLRTRYSELTTLTSQ 1469
Cdd:COG3096 427 ALCGLPDLTPENAED-----------------YLAAFRAKEQ----------------QATEEVLELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1470 YIKFIsETLRRMEEE-ERLAEQQRAEERER-------LAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRR 1541
Cdd:COG3096 474 FEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1542 EEAAVDAQQQKRSIQEELQQLRQSSEAEI-------QAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAegELQA 1614
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSelrqqleQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQ--EVTA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1615 LRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE------------------------------- 1663
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAErlggvllseiyddvtledapyfsalygparh 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1664 --------AAREKQRAL--------------QALEELRLQAEEAERRL------RQAEVER----------ARQVQVALE 1705
Cdd:COG3096 711 aivvpdlsAVKEQLAGLedcpedlyliegdpDSFDDSVFDAEELEDAVvvklsdRQWRYSRfpevplfgraAREKRLEEL 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1706 TAQRSAEAELQSKRASFAEKTAQLERSLQE---EHVAVAqlreeaerRAQQQAEAERAREEAERELERWQLKANEAL-RL 1781
Cdd:COG3096 791 RAERDELAEQYAKASFDVQKLQRLHQAFSQfvgGHLAVA--------FAPDPEAELAALRQRRSELERELAQHRAQEqQL 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1782 RLQAEEVAQQKSLAQAEAEKQKEEaerearrrgkAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQ---ELIRLRAE 1858
Cdd:COG3096 863 RQQLDQLKEQLQLLNKLLPQANLL----------ADETLADRLEELREELDAAQEAQAFIQQHGKALAQlepLVAVLQSD 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1859 TEQGEQQRQLLEEELARLQheaaaatQKRQELEAeLAKVRAEMEVLLASKARAE-EESRSTSEKSKQRLEAeagrfrela 1937
Cdd:COG3096 933 PEQFEQLQADYLQAKEQQR-------RLKQQIFA-LSEVVQRRPHFSYEDAVGLlGENSDLNEKLRARLEQ--------- 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1938 eeaarlralAEEAKRQRQLAEEDAARQRAEAERVLAeklaaiSEATRLKTEAEIaLKEKEAENERLRRLAEDEAfqrrrl 2017
Cdd:COG3096 996 ---------AEEARREAREQLRQAQAQYSQYNQVLA------SLKSSRDAKQQT-LQELEQELEELGVQADAEA------ 1053
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2018 EEQAAQHKADIEERLAQLRkASDSELERQKGLVE---DTLRQR-RQVEEEILALKASFEKAAAGKAELeLELGRiRSNAE 2093
Cdd:COG3096 1054 EERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSLQKRlRKAERDYKQEREQVVQAKAGWCAV-LRLAR-DNDVE 1130
|
970
....*....|....*..
gi 1820553714 2094 DTLRSKEQAELEAARQR 2110
Cdd:COG3096 1131 RRLHRRELAYLSADELR 1147
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
659-848 |
2.75e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 63.23 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 659 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 735
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 736 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 812
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1820553714 813 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 848
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1504-1728 |
2.89e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.60 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1504 AALEKQRQLAEAHAQAKAQAEREAKELQQrmQEEVvrREEAAVDAQQQKRSIQEELQ---QLRQSSEAEIQAKARQAEAA 1580
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1581 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRAQAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEAELALRVK 1659
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1660 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1728
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4524-4562 |
3.07e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.07e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 4524 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 4562
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1478-1698 |
3.50e-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: 65.56 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1478 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQE 1557
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1558 ---ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAE 1634
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1635 RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1698
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1857-2418 |
3.58e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1857 AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAG--- 1931
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRele 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1932 --------RFRELAEEAARLRALAEEAKRQRQLAEEdaARQRAEAERVLAEKLAAISEATRlktEAEIALKEKEAENERL 2003
Cdd:PRK03918 266 erieelkkEIEELEEKVKELKELKEKAEEYIKLSEF--YEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2004 RRLAEDEAFQRRRLEEQAAQHKA--DIEERLAQLR----KASDSELERQKGLVEDTLRQRRQVEEEILALKASfekaaag 2077
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELErlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR------- 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2078 KAELELELGRIRSNAEDTLRSKEQ-----AELEAARQRQLAAEEEQRRREaeerVQKSLAAEEEAARQRKAALEEVERLK 2152
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKR----IEKELKEIEEKERKLRKELRELEKVL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2153 AKVEEARRLRERAEQ-----ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAA 2227
Cdd:PRK03918 490 KKESELIKLKELAEQlkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2228 EEAEEARVQAEREAAQSRRQVEEaeRLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEM--- 2304
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEE--RLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElrk 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2305 ---EKHKKFAEQTLRQKaqvEQELTTLRlqleetdhqknlldEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2381
Cdd:PRK03918 648 eleELEKKYSEEEYEEL---REEYLELS--------------RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
570 580 590
....*....|....*....|....*....|....*..
gi 1820553714 2382 ARIEAENRALilrdkDNTQRfLQEEAEKMKQVAEEAA 2418
Cdd:PRK03918 711 KELEKLEKAL-----ERVEE-LREKVKKYKALLKERA 741
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
182-278 |
3.84e-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: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 182 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 247
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1820553714 248 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 278
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1818-2188 |
4.26e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR--------QLLEEELARLQHEAAAATQKRQE 1889
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1890 L--------------EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR----------- 1944
Cdd:COG4913 364 LeallaalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparll 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1945 ----ALAEEAKRQR----------QLAEEDAARQRAeAERVL----------AEKLAAISEA-------TRLKTEaEIAL 1993
Cdd:COG4913 444 alrdALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLggfaltllvpPEHYAAALRWvnrlhlrGRLVYE-RVRT 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1994 KEKEAENERL--RRLAE-----DEAFQ---RRRLEEQAAQHKADIEERLAQLRKA-------SDSELERQKG-------- 2048
Cdd:COG4913 522 GLPDPERPRLdpDSLAGkldfkPHPFRawlEAELGRRFDYVCVDSPEELRRHPRAitragqvKGNGTRHEKDdrrrirsr 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2049 --LVEDTLRQRRQVEEEILALKASFEKAAAGKAELelelgrirsnaedtlrskeQAELEAARQRQLAAEEEQRRREAEER 2126
Cdd:COG4913 602 yvLGFDNRAKLAALEAELAELEEELAEAEERLEAL-------------------EAELDALQERREALQRLAEYSWDEID 662
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2127 VQkSLAAEEEAARQRKAALE----EVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2188
Cdd:COG4913 663 VA-SAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1184-1736 |
6.99e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1184 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLRAHEEQLKEaqaVPATLPELE 1263
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1264 ATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLqqrhgerdvevERWRERVAQLLERWQAvLAQTDVRQRELEQLG 1343
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-----------SRLEEEINGIEERIKE-LEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1344 RQLRYYRESADPLGAWLQDARQRQEQIqampladsqavrEQLRQEKALL--EEIERHGEKVEECQRFAKQYINAIKDYEL 1421
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1422 QLVTYKAQLEPVASPAKKPKVQS---GSESVIQEYVDLRTRYSElttltsqYIKFISETLRRMEEEERlaeqqraEERER 1498
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1499 LAEVEAALEKQRQLAEAHAQAKAQAEREaKELQQRMQEEVVRREEAAvdaqqqkRSIQEELQQLrqssEAEIQAKARQAE 1578
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEY-------EKLKEKLIKL----KGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1579 AAERsrlrIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRV 1658
Cdd:PRK03918 550 KLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK-KL 624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1659 KAEAEAAREK-QRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERsLQEE 1736
Cdd:PRK03918 625 EEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LKEE 702
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1239-1429 |
7.74e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.08 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1239 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPMFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1318
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1319 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArqrQEQIQAMPLADS-QAVREQLRQEKALLEEIER 1397
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|..
gi 1820553714 1398 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1429
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1240-2017 |
1.17e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1240 EVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqpmfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERva 1319
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1320 qlLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVReQLRQEKALLE----EI 1395
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1396 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyik 1472
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQ--- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1473 fiSETLRRM--EEEERLAEQQRAEERerLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAavdaQQ 1550
Cdd:PRK04863 515 --LQQLRMRlsELEQRLRQQQRAERL--LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL----RQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1551 QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelqALRAQAEEAEAQKRQAQ 1630
Cdd:PRK04863 587 QLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERER--------ELTVERDELAARKQALD 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1631 EEAERLRRQVQDESQRKRQaeaeLALRVKAEA--------------------------------EAAREKQRAL------ 1672
Cdd:PRK04863 659 EEIERLSQPGGSEDPRLNA----LAERFGGVLlseiyddvsledapyfsalygparhaivvpdlSDAAEQLAGLedcped 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1673 --------QALEELRLQAEEAERRL------RQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE--- 1735
Cdd:PRK04863 735 lyliegdpDSFDDSVFSVEELEKAVvvkiadRQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKlqr 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1736 ----------EHVAVA--------------QLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQ 1791
Cdd:PRK04863 815 lhqafsrfigSHLAVAfeadpeaelrqlnrRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLAD 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1792 KSLAQAEAEKQKEEAEREARRRGKAEEQ----------------AVRHR-ELAEQELEKQRQ--------------LAEG 1840
Cdd:PRK04863 895 RVEEIREQLDEAEEAKRFVQQHGNALAQlepivsvlqsdpeqfeQLKQDyQQAQQTQRDAKQqafaltevvqrrahFSYE 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1841 TAQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQHEAAAATQKRQELEAELAK--VRAEMEV 1903
Cdd:PRK04863 975 DAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGA 1054
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1904 LLASKARAEE---------ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAARQRAEAER 1970
Cdd:PRK04863 1055 EERARARRDElharlsanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERR 1133
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1971 VLAEKLAAISeATRLKTEAEI---ALKEKEAENERLR---RLAEDEAFQRRRL 2017
Cdd:PRK04863 1134 LHRRELAYLS-ADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRPERKV 1185
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1571-1792 |
1.19e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1571 QAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1650
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1651 EAELALRVKAEAEAAREKQR-ALQALEELRLQAEEAERRLRQAE-VERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1728
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1729 LERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQK 1792
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1611-2069 |
1.32e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1611 ELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeAEAAREKQRALQALEELRLQAEEAERRLR 1690
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-----LEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1691 QAEveRARQVQVALETAQRSAEAELQSKRASFAEKtaqLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELE- 1769
Cdd:COG4717 150 ELE--ERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEe 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1770 -RWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAvrhrELAEQELEKQRQLAEGTAQQRLAA 1848
Cdd:COG4717 225 lEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA----GVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1849 EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRLEA 1928
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1929 EAGrfrelAEEAARLRALAEEAKRQRQLAEEdaarqRAEAERVLAEKLAAISEATRLKTEAEIalkekEAENERLRRLAE 2008
Cdd:COG4717 378 EAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEEL-----EEELEELEEELE 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2009 DEAFQRRRLEEQaaqhKADIEERLAQLrkASDSELERQKGLVEDTLRQRRQVEEEILALKA 2069
Cdd:COG4717 443 ELEEELEELREE----LAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1486-2045 |
1.41e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 64.88 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1486 RLAEQQRAEERERLAEVEAAlekQRQLAEAHAQAKAQAEREAKELQQRMQ-EEVVRREEAAVDAQQQKRSIQEELQQLRQ 1564
Cdd:COG3899 674 RALEARGPEPLEERLFELAH---HLNRAGERDRAARLLLRAARRALARGAyAEALRYLERALELLPPDPEEEYRLALLLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1565 SSEAEIQA-KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDE 1643
Cdd:COG3899 751 LAEALYLAgRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEA 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1644 SQRKRQAEAELALRVKAEA-----EAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK 1718
Cdd:COG3899 831 RALFNLGFILHWLGPLREAlellrEALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAA 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1719 RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAE 1798
Cdd:COG3899 911 AALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAA 990
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1799 AEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1878
Cdd:COG3899 991 LEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLA 1070
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1879 EAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1958
Cdd:COG3899 1071 AAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALL 1150
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1959 EDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 2038
Cdd:COG3899 1151 LLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAA 1230
|
....*..
gi 1820553714 2039 SDSELER 2045
Cdd:COG3899 1231 LALAAAL 1237
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1907-2178 |
1.46e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 64.58 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1907 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRL 1985
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREARHKK-AAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1986 KTEAEIALKEKEAENERLRRLAEDEAfqrrrleEQAAQHKADIEERL--AQLRKASDSELERQKGLVEDTlrQRRQVEEE 2063
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAA-------AAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2064 ILALKAsfEKAAAGKAELELElgrIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKA 2143
Cdd:PRK05035 586 IARAKA--KKAAQQAASAEPE---EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 1820553714 2144 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2178
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
175-281 |
1.55e-09 |
|
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: 58.75 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYLR 248
Cdd:cd21222 9 EAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELME 88
|
90 100 110
....*....|....*....|....*....|...
gi 1820553714 249 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 281
Cdd:cd21222 89 DAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1298-1605 |
1.66e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.37 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1298 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdvRQRELEqlgRQLRYYRESAdplgawlQDARQRQEQIQAMPLAD 1377
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1378 SQAVREQLRQEKALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1450
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1451 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKEL 1530
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1531 QQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAeAAERSRLRIEEEIRVVRLQLEATERQR 1605
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1472-1719 |
1.68e-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: 63.01 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1472 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQ 1551
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1552 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELQAlRAQAEEAEAQKRQAQE 1631
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREE-AEKKARQRQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1632 EAERLRRQVQDESQRKRQAEAELALRVKAEAEaAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSA 1711
Cdd:pfam13868 243 EQIELKERRLAEEAEREEEEFERMLRKQAEDE-EIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR 321
|
....*...
gi 1820553714 1712 EAELQSKR 1719
Cdd:pfam13868 322 EEEAERRE 329
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1286-2019 |
1.75e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.47 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1286 LRDELRGAQEVGERLQQrhgERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP-LGAWLQ-DA 1363
Cdd:pfam12128 263 LHFGYKSDETLIASRQE---ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDqHGAFLDaDI 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1364 RQRQEQIQAMPLADSQaVREQLRQEKALLEEIERHGEKVEECQRFAKQYINA----IKD--------YELQLVTYKAQLE 1431
Cdd:pfam12128 340 ETAAADQEQLPSWQSE-LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRdiagIKDklakireaRDRQLAVAEDDLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1432 PVASPAKKPKVQSGSESVIQEYvDLRTRYSELTTLTSQYIkFISETLRRMEEEERLAEQQRAEERERLAEVEAAlekQRQ 1511
Cdd:pfam12128 419 ALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQAT-ATPELLLQLENFDERIERAREEQEAANAEVERL---QSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1512 LAEAHAQAKAQAEReakelqqrmqeevVRREEAAVdaQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEI 1591
Cdd:pfam12128 494 LRQARKRRDQASEA-------------LRQASRRL--EERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1592 RVVRLQL--EATERQRGGaEGELQALRAQAEEAEAQKRQAQEEAERLRRQV-----QDESQRKRQAEAELALRVKAEAEA 1664
Cdd:pfam12128 559 LLHRTDLdpEVWDGSVGG-ELNLYGVKLDLKRIDVPEWAASEEELRERLDKaeealQSAREKQAAAEEQLVQANGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1665 AREKQRALQALEelrlQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQskraSFAEKTAQLERSLQeehvavaqlr 1744
Cdd:pfam12128 638 SREETFARTALK----NARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN----SLEAQLKQLDKKHQ---------- 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1745 eeaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQkslaqaeaekqKEEAEREARRRGKAEEQAVRHR 1824
Cdd:pfam12128 700 ---------------------AWLEEQKEQKREARTEKQAYWQVVEG-----------ALDAQLALLKAAIAARRSGAKA 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1825 ELAEQELEKQRQLAE-GTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEaaaATQKRQELEAELAKVRAEME 1902
Cdd:pfam12128 748 ELKALETWYKRDLASlGVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQET---WLQRRPRLATQLSNIERAIS 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1903 VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlaeeakRQRQLAEEDAARQRAEAERVLAEKLAAISEa 1982
Cdd:pfam12128 825 ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANSEQAQGSIGERLAQLED- 897
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1820553714 1983 TRLKTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 2019
Cdd:pfam12128 898 LKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1549-2093 |
1.91e-09 |
|
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: 63.89 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRAQaeeaEAQK 1626
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1627 RQAQEEAERLRRQVQDESQRKRQAEAELALrVKAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEVERAr 1698
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1699 QVQVALETAQRS-AEAELQSKRASFA--EKTAQLERSLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLKA 1775
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1776 NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAeeqavrhrELAEQELEKQRQLAEgtaqqRLAAEQELIRL 1855
Cdd:pfam05701 255 ASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAAL--------ASAKKELEEVKANIE-----KAKDEVNCLRV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1856 RAETEQGEQQRQllEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagrfre 1935
Cdd:pfam05701 322 AAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1936 lAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA--ENERLRRLAEDEAFQ 2013
Cdd:pfam05701 390 -AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQEDSP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2014 R-------------RRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAGKAE 2080
Cdd:pfam05701 469 RgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKEGKLA 547
|
570
....*....|...
gi 1820553714 2081 LELELGRIRSNAE 2093
Cdd:pfam05701 548 AEQELRKWRAEHE 560
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1469-2108 |
2.33e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1469 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDA 1548
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKRSIQEELQQLRQ---SSEAEIQA-KARQAEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAQ-- 1618
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1619 --AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEAELAlRVKAEAEAAREKQRALQAleelrlQAEEAERRLRQAEVE 1695
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1696 RARQVQvALETAQRSAEAELQSKRASFAEKTAQLERSLQeehVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1775
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1776 NEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRHRELAEQELEKQRQLA---------EGTAQQRL 1846
Cdd:pfam15921 391 KE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1847 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqheaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1922
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1923 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAISEATRL-KTEAEIALKEK 1996
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1997 EAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASDSELERQKGL--VEDTLRQRRQVEEEILALKAS 2070
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDYEVLKRN 682
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1820553714 2071 F----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAAR 2108
Cdd:pfam15921 683 FrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMK 727
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1964-2341 |
2.74e-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: 63.60 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1964 QRAEAERVLAEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasDSEL 2043
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2044 ERQKglVEDTLRQRRQVEEEILALKASFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAARQRQLAaeeeqrrre 2122
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2123 aeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHafavQQKEQE 2201
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLR----QQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2202 LQQTLQQEQSVLDRLRSEAEVARRAAeeaeearvqaeREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKlRKDAEQ 2281
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEEQRRKILE-----------KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-RREAEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2282 EavRRAQAEQAALRQKQaadaemEKHKKFAEQTLRQKAqVEQELTTLRLQLEETDHQKNL 2341
Cdd:pfam17380 541 E--RRKQQEMEERRRIQ------EQMRKATEERSRLEA-MEREREMMRQIVESEKARAEY 591
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1559-2112 |
3.09e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 63.72 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1559 LQQLRQSSEAEIQAKARQAEAAErsrlrieEEIRVVRLQLEATER--QRGGAEGELQALRaQAEEAEAQKRQAQEEAERL 1636
Cdd:COG3899 677 EARGPEPLEERLFELAHHLNRAG-------ERDRAARLLLRAARRalARGAYAEALRYLE-RALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1637 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV-QVALETAQRSAEAEL 1715
Cdd:COG3899 749 LELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFgELALALAERLGDRRL 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1716 QSK-RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1794
Cdd:COG3899 829 EARaLFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAA 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1795 AQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1874
Cdd:COG3899 909 AAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAA 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1875 RLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR 1954
Cdd:COG3899 989 AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAAL 1068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1955 QLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 2034
Cdd:COG3899 1069 LAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAA 1148
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 2035 LRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 2112
Cdd:COG3899 1149 LLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLL 1226
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1247-1967 |
3.63e-09 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 63.67 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1247 EQLKEAQAvpaTLPELEATKASLKKL-RAQAEAQQPMFDALRDELRgAQEVGERLQQRHGE---RDVEVERWRERVAQLL 1322
Cdd:PRK10246 191 EQHKSART---ELEKLQAQASGVALLtPEQVQSLTASLQVLTDEEK-QLLTAQQQQQQSLNwltRLDELQQEASRRQQAL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1323 ERWQAVL--AQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMpLADSQAVREQLR-----QEKALLEEI 1395
Cdd:PRK10246 267 QQALAAEekAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTR-LQSTMALRARIRhhaakQSAELQAQQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1396 ERHGEKVEECQRFakqyinaiKDYELQLVTYKAQLepvaSPAKKPKVQsgsesviqeyvdLRTRYSELTTLTSQYIKFIS 1475
Cdd:PRK10246 346 QSLNTWLAEHDRF--------RQWNNELAGWRAQF----SQQTSDREQ------------LRQWQQQLTHAEQKLNALPA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERlaeveaalekQRQLAEAHAQAKAQAEREAK--ELQQRMQEEVVRREEAAVDAQQQKR 1553
Cdd:PRK10246 402 ITLTLTADEVAAALAQHAEQRPL----------RQRLVALHGQIVPQQKRLAQlqVAIQNVTQEQTQRNAALNEMRQRYK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1554 SIQEELQQLRQSSEAEIQAKARQaeaAERSRLR---------------IEE----EIRVVRLQLEATERQRGGAEGELQA 1614
Cdd:PRK10246 472 EKTQQLADVKTICEQEARIKDLE---AQRAQLQagqpcplcgstshpaVEAyqalEPGVNQSRLDALEKEVKKLGEEGAA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1615 LRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeaarekqrALQALEELR--LQA-EEAERRLRQ 1691
Cdd:PRK10246 549 LRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNI--------------TLQPQDDIQpwLDAqEEHERQLRL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1692 AEVERARQVQVALETAQ-RSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaerelER 1770
Cdd:PRK10246 615 LSQRHELQGQIAAHNQQiIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEA------------------QS 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1771 WQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAV----RHRELAEQELEKQRQLAEGTAQ--- 1843
Cdd:PRK10246 677 WQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLslhsQLQTLQQQDVLEAQRLQKAQAQfdt 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1844 ----QRLAAEQELIR--LRAET-EQGEQQRQLLEEElarLQHEAAAATQKRQELEAELAKVRAEMevllaskaraeeESR 1916
Cdd:PRK10246 757 alqaSVFDDQQAFLAalLDEETlTQLEQLKQNLENQ---RQQAQTLVTQTAQALAQHQQHRPDGL------------DLT 821
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1917 STSEKSKQRLEAEAGRFRELA----EEAARLRALAEEAKRQRQL-AEEDAARQRAE 1967
Cdd:PRK10246 822 VTVEQIQQELAQLAQQLRENTtrqgEIRQQLKQDADNRQQQQALmQQIAQATQQVE 877
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
296-398 |
3.83e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.39 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 296 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 374
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1820553714 375 PEDVDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2136-2441 |
4.16e-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: 63.22 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2136 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2207
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2208 qeqsvLDRLRSEA-EVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRK---DAEQEA 2283
Cdd:pfam17380 362 -----LERIRQEEiAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAeqeEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2284 VRRAQAEQAAlRQKQAADAEMEKHKKFaeQTLRQKaQVEQELTTLRLQLEETDHQknlLDEELQRLKAEATEAARQRSQV 2363
Cdd:pfam17380 437 VRRLEEERAR-EMERVRLEEQERQQQV--ERLRQQ-EEERKRKKLELEKEKRDRK---RAEEQRRKILEKELEERKQAMI 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2364 EEELFSVRVQMEELSKLKARIEAENRAlILRDKDNTQRFLQEE---AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQ 2440
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRR-EAEEERRKQQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 1820553714 2441 Q 2441
Cdd:pfam17380 589 A 589
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4446-4483 |
4.55e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 4.55e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1820553714 4446 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4483
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1826-2057 |
4.57e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.79 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1826 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAelakvraemevll 1905
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1906 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAervlAEKLAaisEATRL 1985
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1986 KTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE----ERLAQLRKASDSELERQKGLVEDTLRQR 2057
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
181-280 |
5.59e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 56.74 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 181 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 255
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILH 280
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1814-2314 |
6.27e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1814 GKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQrqllEEELARLQHEAAAATQKRQELEAE 1893
Cdd:COG4717 35 GKSTLLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1894 LAKVRAEMEVLlaSKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1973
Cdd:COG4717 111 LEELREELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1974 EKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqhKADIEERLAQLRKASDSELERQkGLVEDT 2053
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARLLLLIAAALL-ALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2054 LRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAA 2133
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2134 EEEAARQRKAALEEVERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQS 2211
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIaaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2212 VLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLaeeqaqaraqaqaaaEKLRKDAEQEAVRRAQAEQ 2291
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL---------------AELLQELEELKAELRELAE 490
|
490 500
....*....|....*....|...
gi 1820553714 2292 AALRQKQAADAeMEKHKKFAEQT 2314
Cdd:COG4717 491 EWAALKLALEL-LEEAREEYREE 512
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
291-393 |
6.63e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 291 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 369
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1820553714 370 TRLLDPEDVDVPQPDEKSIITYVS 393
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1154-1739 |
7.18e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1154 RECAQRITEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKLEQVRSlsaiyleklktiSLVI 1232
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLSESVS------------EARE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1233 RSTQgaeevLRAHEEQLK-EAQAVPATLPELEATKASLKKLRAQ-----AEAQQPM------------FDALRDELRGAQ 1294
Cdd:PRK04863 580 RRMA-----LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQsgeefEDSQDVTeymqqllerereLTVERDELAARK 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1295 EV----GERLQQRHGERDveverwrERVAQLLERWQAVLAQTDVRQRELEQLGrqlrYYResadplgAWLQDARqrqeqi 1370
Cdd:PRK04863 655 QAldeeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YFS-------ALYGPAR------ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1371 QAMPLADSQAVREQLRQEKALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK-- 1441
Cdd:PRK04863 711 HAIVVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKri 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1442 --VQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRAEERERLAEVEAALEKQRQLAE 1514
Cdd:PRK04863 789 eqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLE 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1515 AHAQAKAQAEREAKE--------LQQRM---QEEVVRREEAAVDAQQQKRSI-------------QEELQQLRQSSEaei 1570
Cdd:PRK04863 869 QAKEGLSALNRLLPRlnlladetLADRVeeiREQLDEAEEAKRFVQQHGNALaqlepivsvlqsdPEQFEQLKQDYQ--- 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1571 QAKARQAEAaeRSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRAQAEEAEAQKRQAQEEAerlrRQVQDESQRKR 1648
Cdd:PRK04863 946 QAQQTQRDA--KQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYN 1019
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1649 QAEAELalrvKAEAEAAREK-QRALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--K 1718
Cdd:PRK04863 1020 QVLASL----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARarrdelHARLSANRSRRNQLEKQLTFCEAEMDNltK 1095
|
650 660
....*....|....*....|.
gi 1820553714 1719 RASFAEKTAQLERSLQEEHVA 1739
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKA 1116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1629-2164 |
7.51e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1629 AQEEAERLRRQVQDESQRKR---QAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRqAEVERARQVQVALE 1705
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1706 TAQRSAEAELQSKRAsFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQA 1785
Cdd:PRK03918 242 ELEKELESLEGSKRK-LEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1786 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRA 1857
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1858 ETEQGEQQRQLLEEELAR--LQHEAAAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR-----------S 1917
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytaelK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1918 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLAEKLAAISEAT 1983
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1984 RLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SDSELERQKGLVE 2051
Cdd:PRK03918 543 SLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2052 DTLRQRRQVEEEILALKASFEKAaagKAELElELGRIRSnaEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSL 2131
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590
....*....|....*....|....*....|...
gi 1820553714 2132 AAEEEAARQRKAALEEVERLKAKVEEARRLRER 2164
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1827-2035 |
7.63e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1827 AEQELEKQRQLAEGTAQQRLAAEQELIRlraeteQGEQQRqLLEEELARLQHEAAAATQKRQELEAELAKVRAEmevllA 1906
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLK------QLEKER-LAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA-----A 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1907 SKARAEEESRSTSEKSKQrLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDA---ARQRAEAErvlAEKLAAISEAT 1983
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKK-AAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAaaeAKKKAEAE---AKKKAAAEAKK 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 1984 RLKTEAEIALKEKEAENErlrRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 2035
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAK---AAAEKAAAAKAAEKAAAAKAAAEVDDLFGGL 266
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1475-2190 |
7.68e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1475 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKaQAEREAKELQQRMQEEVVRREEAAVDAQQQKRS 1554
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLPDLTADNAEDWLEEFQAKEQE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1555 IQEELQQLRQ---SSEAeiqAKARQAEAAERSRlRIEEEIRVVRLQLEATErqrggAEGELQALRAQAEEAEaQKRQAQE 1631
Cdd:PRK04863 454 ATEELLSLEQklsVAQA---AHSQFEQAYQLVR-KIAGEVSRSEAWDVARE-----LLRRLREQRHLAEQLQ-QLRMRLS 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1632 EAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEA-ERRLRQAEVERARQVQVALETAQRS 1710
Cdd:PRK04863 524 ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEArERRMALRQQLEQLQARIQRLAARAP 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1711 AEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW-QLKANEALRLRLQAEEV- 1788
Cdd:PRK04863 604 AWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLsQPGGSEDPRLNALAERFg 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1789 -------------------------AQQ----KSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAE 1839
Cdd:PRK04863 684 gvllseiyddvsledapyfsalygpARHaivvPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKI 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1840 GTAQQRLAAEQELIRL-RAETEQGEQQRQLLEEELARLQHEAAAATQKRQEL--------------------EAELAKVR 1898
Cdd:PRK04863 764 ADRQWRYSRFPEVPLFgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLhqafsrfigshlavafeadpEAELRQLN 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1899 A---EMEVLLASKARAEEESRSTSEKSKQR---LEAEAGRFRELAEE--AARLRALAEEAKRQRQlAEEDAARQRAEAER 1970
Cdd:PRK04863 844 RrrvELERALADHESQEQQQRSQLEQAKEGlsaLNRLLPRLNLLADEtlADRVEEIREQLDEAEE-AKRFVQQHGNALAQ 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1971 VlaEKLAAI-----SEATRLKTEAEIALKEKEAENERLRRLAedEAFQRRR--LEEQAAQ---HKADIEERLAQLRKASD 2040
Cdd:PRK04863 923 L--EPIVSVlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALT--EVVQRRAhfSYEDAAEmlaKNSDLNEKLRQRLEQAE 998
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2041 SELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELG----RIRSNAEDTLRSKE---QAELEAARQRQla 2113
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAEERARARRdelHARLSANRSRR-- 1076
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 2114 aeeeqrrreaeERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQE-AAQKRLQAEEKA 2190
Cdd:PRK04863 1077 -----------NQLEKQLTFCEAEMDNLTKKLRKLER---DYHEMREQVVNAKAGWCAVLRLVKDnGVERRLHRRELA 1140
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1865-2198 |
9.15e-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: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1865 QRQLLEEELARLQHEAAAATQKRQEL--EAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAAR 1942
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1943 LralaeEAKRQRQLAEEDAARQRAEAERVLAEKLAAisEATRLKtEAEIALKEKEAENERLRRlaEDEAFQRRRLEEQAA 2022
Cdd:pfam17380 342 M-----AMERERELERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQ--ELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2023 QHKADIEER-LAQLRKASDSELERQ-KGLVEDTLRQRRQVEEEilalkasfekaaagKAELELELGRIRSNAEDTLRSKE 2100
Cdd:pfam17380 412 QRKIQQQKVeMEQIRAEQEEARQREvRRLEEERAREMERVRLE--------------EQERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2101 QAELEAaRQRQLAAEEEQRRREAEERVQKSLAAEEEaaRQRKAALEEVE-RLKAKVEEARrlRERAEQESARQLQLAQE- 2178
Cdd:pfam17380 478 ELEKEK-RDRKRAEEQRRKILEKELEERKQAMIEEE--RKRKLLEKEMEeRQKAIYEEER--RREAEEERRKQQEMEERr 552
|
330 340
....*....|....*....|..
gi 1820553714 2179 --AAQKRLQAEEKAHAFAVQQK 2198
Cdd:pfam17380 553 riQEQMRKATEERSRLEAMERE 574
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1496-1965 |
9.28e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.96 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1496 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQkrsiqeelQQLRQSSEAEIQAKAR 1575
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALR--------WALAHGDAELALRLAA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1576 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQdesqrkRQAEAELA 1655
Cdd:COG3903 550 ALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAA------AAAAAAAL 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1656 LRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1735
Cdd:COG3903 624 LLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1736 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1815
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1816 AEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1895
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1896 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1965
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2411-2614 |
1.02e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2411 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATRL--KAEAELLQQQKELA--QEQARRLQED 2486
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2487 KEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2566
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1820553714 2567 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2614
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1549-1730 |
1.08e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRieeeirvvrlqleaterqrggaegELQALRAQAEEaeaQKRQ 1628
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLK------------------------QLEKERLAAQE---QKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1629 AQeEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER---ARQVQVALE 1705
Cdd:PRK09510 120 AE-EAAKQAALKQKQAEEAAAKAAAAA-KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAA 197
|
170 180
....*....|....*....|....*
gi 1820553714 1706 TAQRSAEAELQSKRASFAEKTAQLE 1730
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
300-395 |
1.17e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.54 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 300 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 355
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 356 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 395
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2135-2562 |
1.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2135 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahAFAVQQKEQELQQTLQQEQSVLD 2214
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ----LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2215 RLRseaeVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAAL 2294
Cdd:COG4717 150 ELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2295 RQkQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQM 2374
Cdd:COG4717 226 EE-ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2375 EELSKLKARIEAENRAL--ILRD----KDNTQRFLQEEAEKMKQVAEEAARLSVAAQEA--ARLRQLAEEDLAQQRALAE 2446
Cdd:COG4717 305 EELQALPALEELEEEELeeLLAAlglpPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2447 KMLKEKMQAVQEATRLKAEAELLQQQkeLAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRM 2526
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQ--LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....*...
gi 1820553714 2527 AEMSRAQ--ARAEEDAQRFRKQAEEIGEKLHRTELATQ 2562
Cdd:COG4717 463 EQLEEDGelAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1284-1716 |
1.26e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1284 DALRDELRGAQEVGERLQQRHGERDVEVERWRE-----------RVAQLLERWQAV---LAQTDVRQRELEQLGRQLRYY 1349
Cdd:PRK04863 743 DSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgraarekRIEQLRAEREELaerYATLSFDVQKLQRLHQAFSRF 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1350 RES-------ADPLGAWLQDARQRQEQIQAMPLADS--QAVREQLRQEK---ALLEEI---------ERHGEKVEECQ-- 1406
Cdd:PRK04863 823 IGShlavafeADPEAELRQLNRRRVELERALADHESqeQQQRSQLEQAKeglSALNRLlprlnlladETLADRVEEIReq 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1407 --------RFAKQYINAIkdyelqlvtykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF 1473
Cdd:PRK04863 903 ldeaeeakRFVQQHGNAL-----------AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHF 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1474 -ISETLRRMEEEERLAEQQRAeereRLAEVEAALEKQRqlaEAHAQAKAQAeREAKELQQRMQEEVVRreeaavdAQQQK 1552
Cdd:PRK04863 972 sYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERTRAR---EQLRQAQAQL-AQYNQVLASLKSSYDA-------KRQML 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1553 RSIQEELQQL--RQSSEAEIQAKARQAEaaersrlrIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQ 1630
Cdd:PRK04863 1037 QELKQELQDLgvPADSGAEERARARRDE--------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1631 EEAE-------RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKqrALQALeelrlqaeeaerRLRQAEVERARQVQVA 1703
Cdd:PRK04863 1109 EQVVnakagwcAVLRLVKDNGVERRLHRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRL 1174
|
490
....*....|...
gi 1820553714 1704 LETAQRsAEAELQ 1716
Cdd:PRK04863 1175 SEDPKR-PERKVQ 1186
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1476-1729 |
1.56e-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: 59.93 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1555
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1556 QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAER 1635
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1636 LRRQVQDESQRKRQAEAELALRVKaEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1715
Cdd:pfam13868 206 LRAKLYQEEQERKERQKEREEAEK-KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
250
....*....|....
gi 1820553714 1716 QSKRASFAEKTAQL 1729
Cdd:pfam13868 285 RMKRLEHRRELEKQ 298
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
291-398 |
1.66e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 291 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 369
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1820553714 370 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2057-2612 |
1.78e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2057 RRQVEEEILALKaSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEEQRRREAEERVQKSLAAEEE 2136
Cdd:PRK03918 147 REKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2137 AARQRKaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRL 2216
Cdd:PRK03918 225 KLEKEV---KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2217 RSEAEVARRAAEEAEEARVqaeREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQ-EAVRRAQAEQAALR 2295
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLE---EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2296 qKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE-----LFSV 2370
Cdd:PRK03918 379 -KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2371 RVQMEELSKLKARIEAENRALiLRDKDNTQRFLQEEAE--KMKQVAEEAARLSvaaqeaARLRQLAEEDLAQQRALAEKM 2448
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESEliKLKELAEQLKELE------EKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2449 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2527
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2528 EmsRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2607
Cdd:PRK03918 611 E--KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELE 686
|
....*
gi 1820553714 2608 LKSEE 2612
Cdd:PRK03918 687 KRREE 691
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1568-1700 |
1.97e-08 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 59.68 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1568 AEIQAKARQAEAAersrlrieeeIRVVRLQLEATERQRGgAEGELQALRAQAEEAEAQKRQAQEEAERLR---------R 1638
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1639 QVQDESQRKR-QAEAELAlRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1700
Cdd:COG1566 148 QELDEARAALdAAQAQLE-AAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1481-1734 |
2.01e-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: 59.55 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1481 MEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1559
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1560 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVR-----------LQLEATERQRGGAEGELQALRAQAEEAEAQKRQ 1628
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekeeereedERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1629 ---AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALE 1705
Cdd:pfam13868 188 rlrAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
|
250 260
....*....|....*....|....*....
gi 1820553714 1706 TAQRSAEAELQSKRASFAEKTAQLERSLQ 1734
Cdd:pfam13868 268 RKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1462-2056 |
2.03e-08 |
|
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: 60.92 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1462 ELTTLTSQYIKFIS---ETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQAEREA---KELQQRMQ 1535
Cdd:pfam07111 56 EGSQALSQQAELISrqlQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1536 EEVVRREeaavdAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIE--------------EEIRVVRLQLEAT 1601
Cdd:pfam07111 135 EEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkrageakqlaeaqKEAELLRKQLSKT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1602 ERQRGGAEGELQALRAQAEE---AEAQKRQAQEEAERLRRQVQ--DESQRKRQAEAELaLRVKAE------AEAAREKQR 1670
Cdd:pfam07111 210 QEELEAQVTLVESLRKYVGEqvpPEVHSQTWELERQELLDTMQhlQEDRADLQATVEL-LQVRVQslthmlALQEEELTR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1671 ALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQ----------RSAEAELQSKRASFAEKTAQLERSLQEEHVAV 1740
Cdd:pfam07111 289 KIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQDlehrdsvkqlRGQVAELQEQVTSQSQEQAILQRALQDKAAEV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1741 aqlreeaERRAQQQAEAERAREEAERELERWQLK---ANEALRLRLQAEEVAQQKslaQAEAEKQKEEAEREARRRGKAE 1817
Cdd:pfam07111 369 -------EVERMSAKGLQMELSRAQEARRRQQQQtasAEEQLKFVVNAMSSTQIW---LETTMTRVEQAVARIPSLSNRL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAEGTAQQ---RLAAEQELIRLRAETEQGEQQRQLLEEEL---ARL-QHEAAAATQKRQEL 1890
Cdd:pfam07111 439 SYAVRKVHTIKGLMARKVALAQLRQEScppPPPAPPVDADLSLELEQLREERNRLDAELqlsAHLiQQEVGRAREQGEAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1891 EAELAKVRAEMEVLLaskARAEEESRSTSekskQRLEAEAGRFRELAEEAARLRalaEEAKRQRQLAEEDAARQRAEAER 1970
Cdd:pfam07111 519 RQQLSEVAQQLEQEL---QRAQESLASVG----QQLEVARQGQQESTEEAASLR---QELTQQQEIYGQALQEKVAEVET 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1971 VLAEKLA----AISEATRLKTEAEIALKEKE----AENERLRRLaedeafqrRRLEEQAAQHKADIEERLAQlrkasdsE 2042
Cdd:pfam07111 589 RLREQLSdtkrRLNEARREQAKAVVSLRQIQhratQEKERNQEL--------RRLQDEARKEEGQRLARRVQ-------E 653
|
650
....*....|....
gi 1820553714 2043 LERQKGLVEDTLRQ 2056
Cdd:pfam07111 654 LERDKNLMLATLQQ 667
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1485-1735 |
2.04e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 60.73 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1485 ERLAEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKelQQRMQEEVVRREEAAVDAQQQkrsIQEELQQLR 1563
Cdd:PRK05035 440 AIEQEKKKAEEaKARFEARQARLEREKAAREARHKKAAEARAAKD--KDAVAAALARVKAKKAAATQP---IVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1564 QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQ---- 1639
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKakka 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1640 -VQDESQRKRQAEAELALRVKAEAEA-AREKQRALQALEELRLQAEEAERRLR-QAEVERARQVQVALETAQRSAEAELQ 1716
Cdd:PRK05035 595 aQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAED 674
|
250
....*....|....*....
gi 1820553714 1717 SKRASFAEKTAQLERSLQE 1735
Cdd:PRK05035 675 PKKAAVAAAIARAKAKKAA 693
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2249-2823 |
2.38e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.75 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2249 EEAERLKQLAEEQAQARAQAQAAAEKLRKDAEqEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2328
Cdd:TIGR00618 201 LRSQLLTLCTPCMPDTYHERKQVLEKELKHLR-EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2329 RLQLEETDHQKNLLdeelqRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEA--ENRALILRDKDNTQRFLQEE 2406
Cdd:TIGR00618 280 EETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2407 AEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALAEKMLKEKMQAVQEATRLKAEAELlQQQKELAQEQA 2480
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLCKELDILQREQATIDTRTSAFRDL-QGQLAHAKKQQ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2481 RRLQEDKEQMAQQLAEETQ-----------GFQRTLEAERQ---------RQLEMSAEAERLKLRMAEMSRAQARAEEDA 2540
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQceklekihlqeSAQSLKEREQQlqtkeqihlQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2541 QRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQeq 2620
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-- 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2621 llqetqaLQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAE 2700
Cdd:TIGR00618 592 -------ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2701 EGVR-----------RKQEELQQLEQQRRQQEELLAEENQRLREQLQRL-------EEQHRAALAHSEEVTALQVAATKT 2762
Cdd:TIGR00618 665 LSIRvlpkellasrqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeeydrefNEIENASSSLGSDLAAREDALNQS 744
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2763 LPNGRDALDGPATEAEPEHSFDGLRQKVPAQRLQEAGILSAEELQRLAQGHTTVDELARRE 2823
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLE 805
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1484-2111 |
2.44e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 60.58 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1484 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAKELQQRMQEEVVRREEA 1544
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1545 AVDAQQQKRSIQEELQQLRQSseaeiqakarqaeAAERSRLRIEEEirvvrlqleaterqrggaegELQALRAQAEEAEA 1624
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTW-------------LAEHDRFRQWNN--------------------ELAGWRAQFSQQTS 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1625 QKRQAQEEAERLrrqvqDESQRKRQAEAELALRVKA-EAEAAREKQRALQALEE--LRLQAEEAERRLRQAEVERARQvq 1701
Cdd:PRK10246 378 DREQLRQWQQQL-----THAEQKLNALPAITLTLTAdEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVAIQ-- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1702 vALETAQRSAEAELQSKRASFAEKTAQL------------------ERSLQE-----------EHVAVAQLREEAERRAQ 1752
Cdd:PRK10246 451 -NVTQEQTQRNAALNEMRQRYKEKTQQLadvkticeqearikdleaQRAQLQagqpcplcgstSHPAVEAYQALEPGVNQ 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1753 QQAEAERAreeaerelERWQLKaNEALRLRLQAEEVAQQKSlaqaeaekqkeeaerearrrgKAEEQAVRHRElAEQELE 1832
Cdd:PRK10246 530 SRLDALEK--------EVKKLG-EEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALT 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1833 KQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELArLQHEAAAATQKRQELEAELAKVRAEMEVLLASKA--- 1909
Cdd:PRK10246 579 QQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltl 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1910 ---RAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAISEATrLK 1986
Cdd:PRK10246 658 pqeDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LS 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1987 TEAEIALKEKEAENERlRRLAE-----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASDSELERQKGLVEdtlrQR 2057
Cdd:PRK10246 729 LHSQLQTLQQQDVLEA-QRLQKaqaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QT 803
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2058 RQVEEEILALKASFEKAAAGKAELELEL----GRIRSNAEDTLRSKEQAELEA-ARQRQ 2111
Cdd:PRK10246 804 AQALAQHQQHRPDGLDLTVTVEQIQQELaqlaQQLRENTTRQGEIRQQLKQDAdNRQQQ 862
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1543-1731 |
2.56e-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: 59.47 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1543 EAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLR-IEEEIRVVRLQLEATERQRGGAEGELQALRAQAEE 1621
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKeLEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1622 AEAQKRQAQEEAERlrrQVQDESQRKRQAEAelalRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER--ARQ 1699
Cdd:TIGR02794 129 AAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAkaEAA 201
|
170 180 190
....*....|....*....|....*....|..
gi 1820553714 1700 VQVALETAQRSAEAELQSKRASFAEKTAQLER 1731
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
183-277 |
2.90e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 54.65 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 183 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 254
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1820553714 255 VNIRNDDIADGNPKLTLGLIWTI 277
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1489-2168 |
3.01e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.45 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1489 EQQRAEERERLAEVEAALEKQRQLAE---AHAQAKAQAEREAKELQQRMQE------------------EVVRREEAAVD 1547
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNeikALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyhnhqrTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1548 AQQQKRSIQEELQQLRQSS---EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG----------------GA 1608
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfhtlvieRQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1609 EGELQALRAQAEEAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRlq 1681
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRdekkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1682 aeEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLER---------SLQEEHVAVAQLREEAERRAQ 1752
Cdd:TIGR00606 482 --KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqmeMLTKDKMDKDEQIRKIKSRHS 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1753 QQAEAERAREEAERELERW-QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQ--AVRHRELAEQ 1829
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEES 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1830 ELEKQRQLAEGTAQQR--LAAEQELIRLRAETEQGEQQ------------RQLLEEELARLQHEAAAATQKRQELEAELA 1895
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRamLAGATAVYSQFITQLTDENQsccpvcqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELK 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1896 KVRAEMEVLLA-SKARAEEESRSTSEKSKQRleaeaGRFRELAEEAARLRALAEEAKRQRQ--LAEEDAAR--------- 1963
Cdd:TIGR00606 720 KKEKRRDEMLGlAPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKvcltdvtim 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1964 -----QRAEAERVLAEkLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhkadieerlAQLRKA 2038
Cdd:TIGR00606 795 erfqmELKDVERKIAQ-QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ---------IQHLKS 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2039 SDSELERQKGLVEDTLRQRRQVEE-------EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 2111
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2112 LAAEEEQRRREAEERVQKSLaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2168
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1489-1722 |
3.02e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1489 EQQRAEERERLAEVEAALEKQrqLAEAHAQAkAQAEREAKELQQrmQEEVVRREEAAVDAQQQKRSIQEELQQLrQSSEA 1568
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQ--LPELRKEL-EEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEA-RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1569 EIQAKARQAEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRkr 1648
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1649 qaeaeLALRVKAEAEAAREKQRALQALEE------LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1722
Cdd:COG3206 314 -----ILASLEAELEALQAREASLQAQLAqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1790-1985 |
3.10e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.43 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1790 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1869
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1870 EEELARLQHEAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1949
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1820553714 1950 AKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRL 1985
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1889-2546 |
3.17e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.52 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1889 ELEAELAKVRAEMEVLLAskaraEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1968
Cdd:pfam15921 246 QLEALKSESQNKIELLLQ-----QHQDRIEQLISEHEVEITG-----LTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1969 ERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASDSELERQKG 2048
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2049 LVEDTLRQRRQVEEEIlalkasfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAARQrqlaaeeeqrrrEAEERVQ 2128
Cdd:pfam15921 393 LSLEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2129 KSLAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQL-AQEAAQKRLQAEEKAHAFAVQqkeqelqqtl 2206
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLeSSERTVSDLTASLQEKERAIE---------- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2207 qQEQSVLDRLRSEAEVarraaeeaeearvqaereaaqsrrQVEEAERLKQlaeeqaqaraqaqaaaeklrkdaEQEAVRR 2286
Cdd:pfam15921 514 -ATNAEITKLRSRVDL------------------------KLQELQHLKN-----------------------EGDHLRN 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2287 AQAEQAALR-QKQAADAEME--------------KHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA 2351
Cdd:pfam15921 546 VQTECEALKlQMAEKDKVIEilrqqienmtqlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2352 EATEAARQRSQV----EEELFSVRVQMEELSKLKARIEAENRAL--ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQ 2425
Cdd:pfam15921 626 RVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2426 ---EAAR--LRQLAEED-------LAQQRALAEK-----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDK 2487
Cdd:pfam15921 706 selEQTRntLKSMEGSDghamkvaMGMQKQITAKrgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2488 EQMAQQLaEETQGFQRTLeaeRQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2546
Cdd:pfam15921 786 NKMAGEL-EVLRSQERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1925-2556 |
3.32e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1925 RLEAEAGRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAEN 2000
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2001 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAS 2070
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2071 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQlaaeeeqrrreaeervqkSLAAEEEAARQRKAAL-EEVE 2149
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR------------------ELEAEIASLERRKSNIpARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2150 RLKAKVEEARRLRE------------RAEQES-------------------ARQLQLAQEAAQkRLQAEEKAHAFAVQQK 2198
Cdd:COG4913 444 ALRDALAEALGLDEaelpfvgelievRPEEERwrgaiervlggfaltllvpPEHYAAALRWVN-RLHLRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2199 EQELQQTLQQEQSVLDRLRSeaevarraaeeaeeaRVQAEREAAQSR-------RQVEEAERLKQlAEEQAQARAQAQAA 2271
Cdd:COG4913 523 LPDPERPRLDPDSLAGKLDF---------------KPHPFRAWLEAElgrrfdyVCVDSPEELRR-HPRAITRAGQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2272 AEKLRKDAEQEAVRRAQAEQAALRQKQAADAEmekhkkfAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLD--EELQRL 2349
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDNRAKLAALEAE-------LAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2350 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALilrdkdntQRFLQEEAEKMKQVAEEAARLSVAAQEAAR 2429
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAEL--------EELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2430 LRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEE----TQGFQRTL 2505
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADL 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2506 EA-----ERQRQLemsaEAERLKLRMAEMSRAQARAEED-----AQRFRKQAEEIGEKLHR 2556
Cdd:COG4913 812 ESlpeylALLDRL----EEDGLPEYEERFKELLNENSIEfvadlLSKLRRAIREIKERIDP 868
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1848-2048 |
3.41e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1848 AEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1927
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1928 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEA 1989
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1990 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKG 2048
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1815-2022 |
3.64e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAel 1894
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1895 akvRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1973
Cdd:COG4942 119 ---QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1820553714 1974 EKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 2022
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1820-2188 |
3.78e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.50 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1820 AVRHRELAEQELEKQRQLAEGTAQQRLAAE-------QELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEA 1892
Cdd:pfam02029 8 ARERRRRAREERRRQKEEEEPSGQVTESVEpnehnsyEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1893 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAER 1970
Cdd:pfam02029 88 EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1971 VLAEKLAAISEatrlKTEAEIALKEKEAENERLRRLaedeafqrrrleeqaaQHKADIEERLAQLRKASDSELERQKGLV 2050
Cdd:pfam02029 167 EEVPTENFAKE----EVKDEKIKKEKKVKYESKVFL----------------DQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2051 EDTLRQRRQVEEEilalkasfekaAAGKAELELELGRIR-SNAEdtlrsKEQAELEAARQRQLAAEEEQRRREAEERVQK 2129
Cdd:pfam02029 227 QGGLSQSQEREEE-----------AEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERR 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2130 SLAAEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2188
Cdd:pfam02029 291 KLLEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1834-2034 |
4.81e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.12 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1834 QRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRqllEEELARLQHEAAAATQKRQELEAELAKVRAEmevllaskarAEE 1913
Cdd:COG2268 191 RRKIAEIIRDARIAEAE--AERETEIAIAQANR---EAEEAELEQEREIETARIAEAEAELAKKKAE----------ERR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1914 ESRSTSEKSKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEA-----ERVLAEKLAAISEAtrlKTE 1988
Cdd:COG2268 256 EAETARAEAEAAYEIA----EANAEREVQRQLEIAEREREIELQEKEAEREEAELeadvrKPAEAEKQAAEAEA---EAE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1820553714 1989 AEIALKEKEAENERLRRLAE-DEAFQRRRLEEQAAQHKADIEERLAQ 2034
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1633-2089 |
5.07e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 59.65 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1633 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAleelRLQAEEAERRLRQAEVERARQVQVALETAqrSAE 1712
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1713 AELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1792
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1793 SLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1872
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1873 LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1952
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1953 QRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERL 2032
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2033 AQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIR 2089
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1483-1667 |
5.58e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1483 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAKELQQRMqeevvrrEEAAVDAQQQKRSIQEELQQL 1562
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRA-------AAAAKKAAAEAKKKAEAEAAK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1563 RQSSEAEIQAKARQAEAAersrlrieeeirvvrlqlEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAerlrrqvqd 1642
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKA------------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 1820553714 1643 ESQRKRQAEAELALRVKAEAEAARE 1667
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2274-2499 |
6.66e-08 |
|
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: 59.46 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2274 KLRKDAEQEAVRRAQAEQAALRQKQAADAEmekhkkfaEQTLRQ-KAQVEQELTTLRLQLEETDHQknlldeelqrlkAE 2352
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNALADKERAEAD--------RQRLEQeKQQQLAAISGSQSQLESTDQN------------AL 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2353 ATEAARQRSQVEEELFSVRVqmeELSKLKARIEA----------------ENRALILRDK-----DNTQRFLQEEAEKMK 2411
Cdd:NF012221 1601 ETNGQAQRDAILEESRAVTK---ELTTLAQGLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAK 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2412 Q--------VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2483
Cdd:NF012221 1678 QrhvdnqqkVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASA 1757
|
250
....*....|....*.
gi 1820553714 2484 QEDKEQMAQQLAEETQ 2499
Cdd:NF012221 1758 AENKANQAQADAKGAK 1773
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1443-2381 |
6.70e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1443 QSGSESVIQEYVDLRTRYSELTTLTsQYIKFIsETLRRMeeeeRLAEQQRAEERErlaeVEAALEKQRQLAEAHAQAKAQ 1522
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKFDEIFSAT-RYIKAL-ETLRQV----RQTQGQKVQEHQ----MELKYLKQYKEKACEIRDQIT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1523 AereaKELQQRMQEEVVRREEAAVDaqqqkrsiqeelqqlrqsseaEIQAKARQAEAAERSRLRIEEEIRvvrlQLEATE 1602
Cdd:TIGR00606 228 S----KEAQLESSREIVKSYENELD---------------------PLKNRLKEIEHNLSKIMKLDNEIK----ALKSRK 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1603 RQRGGAEGELQALRaqAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQA 1682
Cdd:TIGR00606 279 KQMEKDNSELELKM--EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1683 EEAERRLRQAEVER-ARQVQVALETAQRSAEAELQSKRASFAEKtaqleRSLQEEHVAVAQLREeaerraqqqaeaerar 1761
Cdd:TIGR00606 357 DRHQEHIRARDSLIqSLATRLELDGFERGPFSERQIKNFHTLVI-----ERQEDEAKTAAQLCA---------------- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1762 eeaerelerwQLKANEALRLRlQAEEVAQQKSLAQAEAEKQKEEAERearrrgkaEEQAVRHRelaeqelEKQRQLAEGT 1841
Cdd:TIGR00606 416 ----------DLQSKERLKQE-QADEIRDEKKGLGRTIELKKEILEK--------KQEELKFV-------IKELQQLEGS 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1842 AQQRLAAEQELIRLRAETEQGEQQR--QLLEEELARLQHEAAAATQKRQELEAELAKV------RAEMEVLLASKARAEE 1913
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1914 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEI- 1991
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLf 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1992 ---ALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER---------LAQLRKASDSELERQKGLVEDTLRQRRQ 2059
Cdd:TIGR00606 630 dvcGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2060 VEEEILALKASFEKaaagKAELELELGRIRSNAEDtLRSKEQAELEAARQRQLAAEEEQRRREAEERVQ-KSLAAEEEAA 2138
Cdd:TIGR00606 710 KLKSTESELKKKEK----RRDEMLGLAPGRQSIID-LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlGTIMPEEESA 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2139 RQRKAALEEVERLKAKVEEARRLRERAEQESaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLDRLR 2217
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKL-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLK 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2218 SEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQK 2297
Cdd:TIGR00606 864 SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2298 QAADAEMEK--------HKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELqRLKAEATEAARQRSQVEEELFS 2369
Cdd:TIGR00606 944 NDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDM-RLMRQDIDTQKIQERWLQDNLT 1022
|
970
....*....|..
gi 1820553714 2370 VRVQMEELSKLK 2381
Cdd:TIGR00606 1023 LRKRENELKEVE 1034
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4177-4213 |
8.33e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 8.33e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 4177 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4213
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1853-2158 |
8.48e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1853 IRLRA-ETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1925
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1926 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAervlaeKLAAISEATRLKTEAEIALKEKEAenerlrr 2005
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKA------KKAAQQAANAEAEEEVDPKKAAVA------- 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2006 lAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAsdselerqkglvedtlrqrrqveeeilALKASFEKAAAGKAELELEL 2085
Cdd:PRK05035 584 -AAIARAKAKKAAQQAASAEPEEQVAEVDPKKA---------------------------AVAAAIARAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2086 grIRSNAEDTLRSKEQAELEAARQRQLAAeeeqrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 2158
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1815-1970 |
9.51e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1894
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1895 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EAARLRALAEEAKRQRQLAeedAARQRAEAER 1970
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEAAKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1499-1911 |
1.03e-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: 58.71 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1499 LAEVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE----------- 1567
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1568 --------AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQ 1639
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1640 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKR 1719
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1720 ASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1799
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1800 EKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1879
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 1820553714 1880 AAAATQKRQELEAELAKVRAEMEVLLASKARA 1911
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2304-2607 |
1.03e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2304 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKAR 2383
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2384 IEAENRAL------ILRDKDNTQRFLQEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2455
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2456 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLeaerqrqlemsaeaERLKLRMAEMSRAQAR 2535
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI--------------EELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 2536 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2607
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1476-1698 |
1.30e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.16 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1555
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELE------QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1556 QEELQQLRQssEAEIQAKARQAEAAERsrlrieeeirvvrlqleatERQRGGAEGELQALRAQAEEAEAQKRQAQEEAER 1635
Cdd:TIGR02794 142 RKAKEEAAK--QAEEEAKAKAAAEAKK-------------------KAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1636 LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1698
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1385-1786 |
1.34e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1385 LRQEKALLEEIERHGEKVEECQrfakQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRtrySELT 1464
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE---AELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1465 TLTSQYikfisETLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrREE 1543
Cdd:COG4717 143 ELPERL-----EELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAE----LEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1544 AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGA----EGELQALRAQA 1619
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARq 1699
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1700 vQVALETAQRSAEAELQSKrasfAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1779
Cdd:COG4717 373 -AALLAEAGVEDEEELRAA----LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
....*..
gi 1820553714 1780 RLRLQAE 1786
Cdd:COG4717 448 LEELREE 454
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1615-1736 |
1.35e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.58 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1615 LRAQAEEAEAQKRQaqEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEeAERRLRQAEV 1694
Cdd:COG2268 197 IIRDARIAEAEAER--ETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAEA 273
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1820553714 1695 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEE 1736
Cdd:COG2268 274 NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAE 315
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1457-1590 |
1.37e-07 |
|
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: 56.14 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1457 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreakelQQ 1532
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEE------LL 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1533 RMQEEVVRREEAAVDAQQQKRSIQEEL----QQLRQSSEAEIQAKARQAEAA-----ERSRLRIEEE 1590
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1827-2042 |
1.42e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1827 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1906
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1907 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1975
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1976 LAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSE 2042
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2287-2756 |
1.66e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2287 AQAEQAAlRQKQAADAEMEKHkkfaEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE 2366
Cdd:PRK02224 227 EQREQAR-ETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2367 LF-------SVRVQMEELSKLKARIE---AENRALILRDKDNTQRF------LQEEAEKMKqvaEEAARLSVAAQEAARL 2430
Cdd:PRK02224 302 AGlddadaeAVEARREELEDRDEELRdrlEECRVAAQAHNEEAESLredaddLEERAEELR---EEAAELESELEEAREA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2431 RQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-------------- 2496
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecg 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2497 ---ETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEE------DAQRFRKQAEEIGEKLHRTELATQEKVTL 2567
Cdd:PRK02224 459 qpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRER 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2568 VQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQlksEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIE 2647
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERIESLERIRTLLAAIADAEDEIERLREKR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2648 QEKAKLEQLFQDEVAKAQQLREEQQRQQQQmeqerqrlvASMEEARQRQHEAEE------GVRRKQEELQQLEQQRRQQE 2721
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDE---------ARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAV 686
|
490 500 510
....*....|....*....|....*....|....*
gi 1820553714 2722 ELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQ 2756
Cdd:PRK02224 687 ENELEELEELRERREALENRVEALEALYDEAEELE 721
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1874-2604 |
1.69e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1874 ARLQHEAAAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1950
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1951 KRQRQLAEEDAAR---QRAEAERVLAEKLAAISEATRLKTEAEIalkekEAENERLR---RLAEDEAfQRRRLEEQAAQH 2024
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRV-----QAENARLEmhfKLKEDHE-KIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2025 KADIEERLAQLRKASDSELERQKGL---VEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSkeq 2101
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2102 aeleaarQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV---EEARRLRERAEQESARQLQLAQE 2178
Cdd:pfam05483 312 -------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcslEELLRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2179 AAQKRLQAEEKAHAFAVQQKEQelqqtlqqeqsvLDRLRSEAevarraaeeaeearvqaereaAQSRRQVEEAERLKQLA 2258
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE------------LEELKKIL---------------------AEDEKLLDEKKQFEKIA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2259 EEQaqaraqaqaaaeklrKDAEQEAVRRAQAeqaalRQKQAADAEME--KHKKFAEQTLRQKAQVEQELTTLRLQLEETD 2336
Cdd:pfam05483 432 EEL---------------KGKEQELIFLLQA-----REKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIELT 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2337 HQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELskLKARIEAENRALILRDKDNTQR--FLQEEAE---KMK 2411
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--LKQIENLEEKEMNLRDELESVReeFIQKGDEvkcKLD 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2412 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMA 2491
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2492 QQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQ---------------ARAEEDAQRFRKQAEEIGEKLHR 2556
Cdd:pfam05483 650 QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSELGL 729
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1820553714 2557 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAK 2604
Cdd:pfam05483 730 YKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1513-1727 |
1.74e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1513 AEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEI- 1591
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAEIEERREELg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1592 -RVVRLQ------------------------LEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQR 1646
Cdd:COG3883 90 eRARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1647 KRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKT 1726
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
.
gi 1820553714 1727 A 1727
Cdd:COG3883 250 G 250
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1863-2038 |
1.85e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1863 EQQRQLLEEELAR-LQHEAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1941
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1942 RLRALAEeakrqrQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 2021
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 1820553714 2022 AQHKADIEERLAQLRKA 2038
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1824-2601 |
1.86e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1824 RELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--HEAAAATQKRQELEAELAK 1896
Cdd:PRK04863 282 RVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1897 VraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvlaEKL 1976
Cdd:PRK04863 360 L----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ---QAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1977 AAISEATRLKTEAEIALKEKEAenerlrrlaedeafqrrRLEEQAAQHKADIEERLaqlrkasdsELERQKGLVEDTLRQ 2056
Cdd:PRK04863 421 QALERAKQLCGLPDLTADNAED-----------------WLEEFQAKEQEATEELL---------SLEQKLSVAQAAHSQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2057 RRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR-QLAAEEEQRRREAEERVQKSLAAEE 2135
Cdd:PRK04863 475 FEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDED 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2136 EAARQRKAALEEVERLKAKVEEA--RRLRERAEQESARQL--QLAQEaAQKRLQAEEKAHAFAVQ--QKEQELQQTLQQE 2209
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEAreRRMALRQQLEQLQARiqRLAAR-APAWLAAQDALARLREQsgEEFEDSQDVTEYM 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2210 QSVLDRLRSEAEVARRAAEEAEEARVQAEReaaQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEA------ 2283
Cdd:PRK04863 634 QQLLERERELTVERDELAARKQALDEEIER---LSQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSAlygpar 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2284 ----------VRRAQAEQ-----------------------AALRQK----QAADAEMeKHKKFAEQTLRQKAQVEQELT 2326
Cdd:PRK04863 711 haivvpdlsdAAEQLAGLedcpedlyliegdpdsfddsvfsVEELEKavvvKIADRQW-RYSRFPEVPLFGRAAREKRIE 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2327 TLRLQLEE--TDHQKNLLD-EELQRL--------------------KAEATEAARQRSQVEEELFS----VRVQMEELSK 2379
Cdd:PRK04863 790 QLRAEREElaERYATLSFDvQKLQRLhqafsrfigshlavafeadpEAELRQLNRRRVELERALADhesqEQQQRSQLEQ 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2380 LKARIEAENRAL----ILRDKDNTQRFlqEEAEKMKQVAEEAAR--------LSVAAQEAARLRQLAE--EDLAQQRALA 2445
Cdd:PRK04863 870 AKEGLSALNRLLprlnLLADETLADRV--EEIREQLDEAEEAKRfvqqhgnaLAQLEPIVSVLQSDPEqfEQLKQDYQQA 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2446 EKMLKE-KMQA---------------VQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLAEETQgFQRTLE 2506
Cdd:PRK04863 948 QQTQRDaKQQAfaltevvqrrahfsyEDAAEMLAKNSDLnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ-VLASLK 1026
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2507 AERQRQLEMSAEAERlklRMAEMS-RAQARAEEdaqRFRKQAEEIGEKLHRTELATQEkvtLVQTLEIQRQQSDHDAERL 2585
Cdd:PRK04863 1027 SSYDAKRQMLQELKQ---ELQDLGvPADSGAEE---RARARRDELHARLSANRSRRNQ---LEKQLTFCEAEMDNLTKKL 1097
|
890
....*....|....*.
gi 1820553714 2586 REAIAELEREKEKLQQ 2601
Cdd:PRK04863 1098 RKLERDYHEMREQVVN 1113
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1294-1728 |
1.92e-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: 57.75 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1294 QEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGawlqdarqrqeqiqam 1373
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN---------------- 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1374 plADSQAVREQLRQEKALLEEIERHGEKVEECQrfakQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEY 1453
Cdd:TIGR00606 758 --RDIQRLKNDIEEQETLLGTIMPEEESAKVCL----TDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1454 VDLRTRYSELTTltsqyikfisetlrRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKA---QAEREAKEL 1530
Cdd:TIGR00606 832 QEKQHELDTVVS--------------KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEV 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1531 QQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEG 1610
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKET 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1611 ELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALEELRLQAEEAERR 1688
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENelKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1820553714 1689 LRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1728
Cdd:TIGR00606 1058 KLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFR 1097
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1818-2334 |
2.04e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 57.95 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEkqrqlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1897
Cdd:COG3899 722 AEALRYLERALELLP-----PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYA 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1898 ----------RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1967
Cdd:COG3899 797 nlgllllgdyEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAA 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1968 AERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQK 2047
Cdd:COG3899 877 AAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAA 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2048 GLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERV 2127
Cdd:COG3899 957 ALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAAL 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2128 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQ 2207
Cdd:COG3899 1037 LAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALAL 1116
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2208 QEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRA 2287
Cdd:COG3899 1117 AAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALL 1196
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1820553714 2288 QAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEE 2334
Cdd:COG3899 1197 AALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1674-2112 |
2.06e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 57.72 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1674 ALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ---------LR 1744
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1745 EEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHR 1824
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1825 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVL 1904
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1905 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATR 1984
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1985 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEI 2064
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1820553714 2065 LALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 2112
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
176-283 |
2.41e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 52.70 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 248
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 1820553714 249 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 283
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2385-2612 |
2.64e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2385 EAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLS-----VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA 2459
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2460 TRLKAEAELLQQQK-ELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEE 2538
Cdd:COG4913 319 DALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2539 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE-LEREKEKLQQEAKLLQLKSEE 2612
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1814-2056 |
2.78e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.88 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1814 GKAEEQAVRHRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheaaaATQKRQEL 1890
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1891 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1970
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1971 VLAEKlaaiseatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASDSELERQKGL 2049
Cdd:pfam15709 447 AEAEK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 1820553714 2050 VEDTLRQ 2056
Cdd:pfam15709 516 AQEQARQ 522
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1479-1740 |
3.00e-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: 56.20 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1479 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaqakAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1558
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLL-------LQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1559 LQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaEGELQALRAQAEEAEaQKRQAQEEAERLRR 1638
Cdd:pfam15558 94 SRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALR---EQNSLQLQERLEEAC-HKRQLKEREEQKKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1639 QVQDESQR-KRQA-EAELALRVKAEAEAARE--KQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1714
Cdd:pfam15558 170 QENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEER 249
|
250 260
....*....|....*....|....*.
gi 1820553714 1715 LQSKRASFAEKTAQLERSLQEEHVAV 1740
Cdd:pfam15558 250 QEHKEALAELADRKIQQARQVAHKTV 275
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2240-2779 |
3.39e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.16 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2240 EAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKD--AEQEAVRRAQAEQAAL--RQKQAADAEMEKHKkfAEQTL 2315
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsAADAAVAKDRSELEALedQHGAFLDADIETAA--ADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2316 RQKAQVEQELTTLRLQLEETDHQKnlLDEELQRLKAEATEA-ARQRSQVEEELFSVRvqmEELSKLKARIEAENRAL--I 2392
Cdd:pfam12128 349 LPSWQSELENLEERLKALTGKHQD--VTAKYNRRRSKIKEQnNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALesE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2393 LRDKDNTQ-RFLQEEAEKMKQVAEEA-ARLSVA----------------------AQEAARLRQL-AEEDLAQQRALAEK 2447
Cdd:pfam12128 424 LREQLEAGkLEFNEEEYRLKSRLGELkLRLNQAtatpelllqlenfderierareEQEAANAEVErLQSELRQARKRRDQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2448 MLKEKMQAVQEATRLKAEAELLQQQ------------------------KELAQEQARRLQEDKEQMAQQLAEETQGFQR 2503
Cdd:pfam12128 504 ASEALRQASRRLEERQSALDELELQlfpqagtllhflrkeapdweqsigKVISPELLHRTDLDPEVWDGSVGGELNLYGV 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2504 TLEAERQRQLEMSAEAERLKLRMAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQR 2575
Cdd:pfam12128 584 KLDLKRIDVPEWAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2576 QQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFL---SEKDSLLQR-----ERFIE 2647
Cdd:pfam12128 664 SEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2648 QEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEE 2727
Cdd:pfam12128 744 GAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERA 822
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2728 NQRLREQLQRLEEQHRAALAHSEE----VTALQVAATKTLPNGRDALDGPATEAEP 2779
Cdd:pfam12128 823 ISELQQQLARLIADTKLRRAKLEMerkaSEKQQVRLSENLRGLRCEMSKLATLKED 878
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1534-1702 |
3.45e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 56.69 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1534 MQEEVVRREEAAVDAQQQkrsiqeELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegeLQ 1613
Cdd:COG1193 497 LPEEIIERARELLGEESI------DVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------EE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1614 ALRAQAEEAEAQKRQAQEEAERLRRQVQDEsqrkrqaeaelalrvKAEAEAAREKQRALQALEElRLQAEEAERRLRQAE 1693
Cdd:COG1193 565 ILEKAREEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAKP 628
|
....*....
gi 1820553714 1694 VERARQVQV 1702
Cdd:COG1193 629 AKPPEELKV 637
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1471-1714 |
3.53e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1471 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQ 1550
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1551 QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAE----EAEAQK 1626
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1627 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALET 1706
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*...
gi 1820553714 1707 AQRSAEAE 1714
Cdd:COG3883 258 AAGSAGAA 265
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1482-1647 |
3.61e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.62 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1482 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQ 1561
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1562 LRQSSEAEIQAKARQAEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRAQAEEAEAQK------RQAQ 1630
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 1820553714 1631 EEAERLRRQVQDESQRK 1647
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1593-1732 |
3.77e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.44 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1593 VVRLQLEATERQRGGAEGELQALRAQAEEAEAQkRQAQEEAERLRRQVQdesqrkrQAEAELALrvkAEAEAARekQRAL 1672
Cdd:COG1566 73 LARLDPTDLQAALAQAEAQLAAAEAQLARLEAE-LGAEAEIAAAEAQLA-------AAQAQLDL---AQRELER--YQAL 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1673 --------QALEELRLQAEEAERRLRQAEVERAR-QVQVALETAQRSAEAELQSKRASFAEKTAQLERS 1732
Cdd:COG1566 140 ykkgavsqQELDEARAALDAAQAQLEAAQAQLAQaQAGLREEEELAAAQAQVAQAEAALAQAELNLART 208
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1879-2715 |
5.12e-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: 56.52 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1879 EAAAATQKRQELEAELAKVRAEMEVLLASKA-------RAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL----- 1946
Cdd:TIGR00618 57 RSEVIRSLNSLYAAPSEAAFAELEFSLGTKIyrvhrtlRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVihdll 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1947 ---AEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 2020
Cdd:TIGR00618 137 kldYKTFTRVVLLPQGEFAQflkAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2021 AAQHKADIEERLAQLRKASDSELERQKGLVE--DTLRQRRQVEEEILALKASFEKAAAGKAELEL---ELGRIRSNAEDT 2095
Cdd:TIGR00618 217 YHERKQVLEKELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqeRINRARKAAPLA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2096 LRSKEQAELEAARQRQLAAEEEQRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQL 2175
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRA-----KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2176 AQeaaqkrlQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRseaevarraaeeaeearvqaeREAAQSRRQVEEAERLK 2255
Cdd:TIGR00618 372 CQ-------QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ---------------------REQATIDTRTSAFRDLQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2256 QlaeeqaqaraqaqaaaEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEK-HKKFAEQTLRQKAQVEQELTTLRLQLEE 2334
Cdd:TIGR00618 424 G----------------QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2335 TdhqKNLLDEELQRLKAEATEAARQRSQVEEElfsvRVQMEELSKLKARIEA-ENRALILRDK-DNTQRFLQEEAEKMKQ 2412
Cdd:TIGR00618 488 K---KAVVLARLLELQEEPCPLCGSCIHPNPA----RQDIDNPGPLTRRMQRgEQTYAQLETSeEDVYHQLTSERKQRAS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2413 VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKEQ 2489
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQ 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2490 MAQQLAEETQGFQRTLEAERQRQlemsaEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2569
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVRE-----HALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2570 TLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQE 2649
Cdd:TIGR00618 715 EYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR 794
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2650 KAKLEQLFQDEV---AKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQ 2715
Cdd:TIGR00618 795 EEDTHLLKTLEAeigQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2311-2745 |
5.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2311 AEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRLKAEATEAARQRSQVEEELfSVRVQMEELSKLKARIEAENRA 2390
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2391 LI-LRDKDNTQRFLQEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2469
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2470 QQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRKQAE 2548
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2549 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllqETQAL 2628
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---------IAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2629 QQSFLSEKDSLLQRERFIEQEKAKLEQL--FQDEVAKAQQLREEQQRQQQQME--QERQRLVASMEEARQRQHEAEEGVR 2704
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELeeLEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELA 456
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1820553714 2705 RKQEELQQLEQQRRQQEELLAEEnqRLREQLQRLEEQHRAA 2745
Cdd:COG4717 457 ELEAELEQLEEDGELAELLQELE--ELKAELRELAEEWAAL 495
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2139-2429 |
5.30e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.11 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2139 RQRKAALEEVERLKAKVEEARrlrERAEqesARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQtlqqeqsvLDRLRS 2218
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAK---ARFE---ARQARLEREKAAREARHKKAAEARAAKDKDAVAAA--------LARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2219 EAEVARRAAEEAeearvqaerEAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQ 2298
Cdd:PRK05035 498 KKAAATQPIVIK---------AGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAAN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2299 AADAEMEKHKKFA-----EQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEElfsvrvq 2373
Cdd:PRK05035 569 AEAEEEVDPKKAAvaaaiARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPV------- 641
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2374 meelSKLKARIEAEN-RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAAR 2429
Cdd:PRK05035 642 ----DPRKAAVAAAIaRAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1560-1727 |
5.49e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.11 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1560 QQLRQSsEAEIQAKARQAEAAERSRLRIEEeiRVVRLQLEATERqrggaegELQALRAQAEEAEAQKRQAQEEAERLRRQ 1639
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAAR-------EARHKKAAEARAAKDKDAVAAALARVKAK 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1640 VQDESQRKRQAEAELALRVKAEAEA-AREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK 1718
Cdd:PRK05035 499 KAAATQPIVIKAGARPDNSAVIAAReARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPK 578
|
....*....
gi 1820553714 1719 RASFAEKTA 1727
Cdd:PRK05035 579 KAAVAAAIA 587
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1447-1683 |
5.59e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1447 ESVIQEYVD--LRTRYSElttlTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ---RQLAEAHAQ-AK 1520
Cdd:COG3206 155 NALAEAYLEqnLELRREE----ARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKlllQQLSELESQlAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1521 AQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEA 1600
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1601 tERQRGGAEGELQALRAQAEEAEAQKRQAQeeaerLRRQVQDESQRkrqaEAELAlRVKAEAEAAREK-QRALQALEELR 1679
Cdd:COG3206 310 -EAQRILASLEAELEALQAREASLQAQLAQ-----LEARLAELPEL----EAELR-RLEREVEVARELyESLLQRLEEAR 378
|
....
gi 1820553714 1680 LQAE 1683
Cdd:COG3206 379 LAEA 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1463-1700 |
6.04e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1463 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAKELQQrMQEEVVR 1540
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1541 REEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggAEGELQALRAQ-A 1619
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEaAREKQRALQALEELrlqAEEAERRLRQAEVERARQ 1699
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVAREL---YESLLQRLEEARLAEALT 384
|
.
gi 1820553714 1700 V 1700
Cdd:COG3206 385 V 385
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3858-3893 |
6.09e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 6.09e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1820553714 3858 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3893
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1475-1713 |
6.15e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.64 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1475 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvrREEAAVDAQQQKRS 1554
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSW--EKEEKRDSRLGRYK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1555 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE----------------------RQRGGAEGEL 1612
Cdd:pfam02029 130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEevkdekikkekkvkyeskvfldQKRGHPEVKS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1613 QA--------------------LRAQAEEAEAQKRQAQEEAERLRRQVQD-ESQ-----RKRQAEAELALrvkAEAEAAR 1666
Cdd:pfam02029 210 QNgeeevtklkvttkrrqgglsQSQEREEEAEVFLEAEQKLEELRRRRQEkESEefeklRQKQQEAELEL---EELKKKR 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1820553714 1667 EKQRALQALEELRLQAEEAERRLRQAEVERARQVQValetAQRSAEA 1713
Cdd:pfam02029 287 EERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEI----ERRRAEA 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1471-1671 |
6.56e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1471 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvRREEAAVDAQQ 1550
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ--KEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1551 QKRSIQEELQQLRQSSEAE------------IQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQ 1618
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1619 AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRA 1671
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1103-1642 |
7.61e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.75 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1103 QQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRI-TEQQKAQAEVEGLGKGVARLS 1181
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLcKELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1182 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRSTQGAEEVLRAHEEQLKEAQAVpaTLPE 1261
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1262 LEATKASLKKLRAQAEAQQPMFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1332
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1333 DVRQRELEQLGRQLRYYRESADPLGAWLQDAR---QRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGEKVEECQrfa 1409
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1410 kQYINAIKDYELQLvTYKAQLEPVASPAKKPKVQsgSESVIQEYVDLRTRYSELTTLT---SQYIKFISETLRRMEEEER 1486
Cdd:TIGR00618 643 -LKLTALHALQLTL-TQERVREHALSIRVLPKEL--LASRQLALQKMQSEKEQLTYWKemlAQCQTLLRELETHIEEYDR 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1487 LAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAEREAKELQQRMQEEVV------RREEAAVDAQQQKRSIQEEL 1559
Cdd:TIGR00618 719 EFNEIENASSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAalqtgaELSHLAAEIQFFNRLREEDT 798
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1560 QQLRQsSEAEIQAKARQAEAAersRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQ 1639
Cdd:TIGR00618 799 HLLKT-LEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
...
gi 1820553714 1640 VQD 1642
Cdd:TIGR00618 875 SDK 877
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2249-2570 |
8.66e-07 |
|
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: 55.35 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2249 EEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRraqaeqAALRQKQAADAEMEKHKKFAEQTLrqkaqvEQELTTL 2328
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIK------KATESLEEQLAAAEAEQELEESKR------ETETGIQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2329 RLQlEETDHQKNLLDEELQRLKAEATE--AARQRSQVEEELFSVRVQMEElskLKARIEAENRALilrdKDNTQRFLQEE 2406
Cdd:COG5185 340 NLT-AEIEQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIES---TKESLDEIPQNQ----RGYAQEILATL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2407 AEKMKQVAEEAARLSVAaqeaarLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqARRLQ 2484
Cdd:COG5185 412 EDTLKAADRQIEELQRQ------IEQATSSNEEVSKLLneLISELNKVMREADEESQSRLEEAYDEINRSVRSK-KEDLN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2485 EDKEQMAQQLAEETQGFQrTLEAERQRQLE-----MSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2559
Cdd:COG5185 485 EELTQIESRVSTLKATLE-KLRAKLERQLEgvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAA 563
|
330
....*....|.
gi 1820553714 2560 ATQEKVTLVQT 2570
Cdd:COG5185 564 NLRTAVIDELT 574
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2453-2598 |
8.93e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.41 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2453 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLAEEtQGFQRTLEAERQRQLEMSAEAERLKL 2524
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2525 RMAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2598
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2388-2754 |
9.19e-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: 55.73 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2388 NRALILRDKDNTQRflQEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2462
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2463 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF--QRTLEAERQRQLEMSAEAERLkLRMAE 2528
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2529 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2608
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2609 KSEEMQtvqqeqllqetqalqqsflsekdslLQRERFIEQEKAKLEQLFQdEVAKAQQLREEQQRQQQQMEQERQRLVAS 2688
Cdd:COG3096 505 RSQQAL-------------------------AQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 2689 MEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR------LREQLQRLEEQHRAALAHSEEVTA 2754
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTA 630
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2285-2481 |
9.22e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.42 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2285 RRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQkaQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEAteaarqrSQVE 2364
Cdd:pfam05667 299 RFTHTEKLQFTNEAPAATSSPPTKVETEEELQQ--QREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2365 EELFSVRVQMEELSKLKARIEaenRAL-ILRDKDNT----QRFLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEED 2437
Cdd:pfam05667 370 EELEELKEQNEELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKE 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1820553714 2438 LAQQRALAE-KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2481
Cdd:pfam05667 447 DESQRKLEEiKELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4280-4308 |
9.95e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.95e-07
10 20
....*....|....*....|....*....
gi 1820553714 4280 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4308
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2411-2615 |
1.07e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2411 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2490
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2491 AQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2570
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820553714 2571 LEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2615
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3599-3635 |
1.44e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.48 E-value: 1.44e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 3599 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 3635
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2303-2740 |
1.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2303 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA------EATEAARQRSQVEEELFSVRVQMEE 2376
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2377 LSKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2454
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2455 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRMAEM 2529
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2530 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-EAKL 2605
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2606 LQLKSEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQqrqqqqmeqerqrl 2685
Cdd:PRK03918 542 KSLKKELEK--------------LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER-------------- 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 2686 VASMEEARQRQHE---AEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQRLEE 2740
Cdd:PRK03918 594 LKELEPFYNEYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1441-1655 |
1.92e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1441 KVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1515
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1516 --HAQAKAQAEREAKELQQRMQEevvRREEAavdaqQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIrv 1593
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAPA---RREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 1594 vrlqleaTERQRggaegELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1655
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4063-4100 |
2.01e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.01e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1820553714 4063 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 4100
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1151-1743 |
2.04e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.42 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1151 EPARECAQRITEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIYlEKLKTISL 1230
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHTR-QQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1231 VIRSTQGAEEVLRAHeeQLKEAQAVPATLPELeatkaslkklrAQAEAQQPMFDALRDELRG-----AQEVGERLQQRhg 1305
Cdd:PRK10246 319 RLQSTMALRARIRHH--AAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1306 erdveveRWRERVAQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLQDARQRQEQIQAmplADSQA 1380
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1381 VREQLRQEKALLEEIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1433
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1434 ASPAKKPKVQSGSESVIQEYVDLRtrySELTTLTSQYIKFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1513
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1514 EAHAQAKAQAEREAKELQQRMQEEVVRREEAAvdAQQQKRSIQEELQQLRQSSEAEIQAKARQ--AEAAERSRL--RIEE 1589
Cdd:PRK10246 596 DDIQPWLDAQEEHERQLRLLSQRHELQGQIAA--HNQQIIQYQQQIEQRQQQLLTALAGYALTlpQEDEEASWLatRQQE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1590 EIRVVRLQLEATERQRGGAE--------GELQALRAQAEEAEAQK-RQAQEEAERLRRQVQ-------DESQRKRQAEAE 1653
Cdd:PRK10246 674 AQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQAQ 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1654 LALRVKAEAEAAREKQRALQALEELRLQAEEAERRLrqaevERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1733
Cdd:PRK10246 754 FDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQ 828
|
650
....*....|
gi 1820553714 1734 QEEHVAVAQL 1743
Cdd:PRK10246 829 QELAQLAQQL 838
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1509-1637 |
2.38e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 53.13 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1509 QRQLAEAHAQ-AKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKArQAEAAERSRLRI 1587
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1588 EEEIRVVRLQLEATERQRGGAEgELQALRAQAEEAEAQKRQAQEEAERLR 1637
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
181-289 |
2.57e-06 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 50.06 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 181 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 247
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1820553714 248 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 289
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2289-2743 |
2.67e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2289 AEQAALRQKQAADAEMEKHKKFaeqtLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEelf 2368
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKF----IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2369 sVRVQMEELSKLKARIEAENRALILRDKdNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqraLAEKM 2448
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2449 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEmsAEAERLKLRMAE 2528
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK--EELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2529 MSRAQARAEEDAQRFRKQA-----EEIGEKLHRTELATQEKVTLVQTLEIQRQQ---------SDHDAERLREAIAELER 2594
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEieeeiSKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2595 -EKEKLQQEAKLLQLKSEEMQTvqqeqllqetqalqQSFLSEKDSLLQRERFIEQEKA---KLEQLFQDEVAKAQQLREE 2670
Cdd:PRK03918 464 iEKELKEIEEKERKLRKELREL--------------EKVLKKESELIKLKELAEQLKEleeKLKKYNLEELEKKAEEYEK 529
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2671 QQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQRLEEQHR 2743
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1364-1696 |
2.84e-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: 53.36 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1364 RQRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGE---KVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKP 1440
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1441 KVQSG-SESVIQEYVDlrtrysELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERER---LAEVEAALEKQRQLAEAH 1516
Cdd:pfam07888 121 LAQRAaHEARIRELEE------DIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERkqlQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1517 AQAK-AQAEREAKELQqrMQEEVVRREEAAVDAQQQKRSIQEELQQLR------QSSEAEIQAKARQAEAAERSRLRIEE 1589
Cdd:pfam07888 195 QELRnSLAQRDTQVLQ--LQDTITTLTQKLTTAHRKEAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1590 EIRVVRLQLEATERQRGGAEGELQALRAQ-AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREK 1668
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
330 340
....*....|....*....|....*...
gi 1820553714 1669 QRALQALEELRLQAEEAERRLRQAEVER 1696
Cdd:pfam07888 353 DCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1557-1929 |
2.84e-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: 53.36 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1557 EELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERL 1636
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1637 RRQVQDESQRKRQAEAELALRVKA-EAEAAREKQRALQALEELRLQAEEAERRLRQAEVERA--RQVQVALETAQ---RS 1710
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAerKQLQAKLQQTEeelRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1711 AEAELQSKRASFAEKTAQLERsLQEEhvaVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQ 1790
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQ-LQDT---ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1791 QKSlaqaeaekqkeeaerearrRGKAEEQAVRHR--ELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRql 1868
Cdd:pfam07888 266 QRD-------------------RTQAELHQARLQaaQLTLQLADASLALREGRA--RWAQERETLQQSAEADKDRIEK-- 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1869 LEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAE 1929
Cdd:pfam07888 323 LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASlrvAQKEKEQLQAE 386
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2394-2549 |
2.85e-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: 53.42 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2394 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2470
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2471 QQKELAQEQARRLQEDKE---QMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRaqaRAEEDAQRF---- 2543
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 1820553714 2544 -RKQAEE 2549
Cdd:pfam15709 512 aMKQAQE 518
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2395-2698 |
2.95e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2395 DKDNTQRFLQEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRAL---------AEKMLKEKMQAVQEATRLKAE 2465
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMdrqaaiyaeQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2466 AELLQ-QQKELAQEQARRLQEDKEQMAQQlaEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFR 2544
Cdd:pfam17380 360 RELERiRQEEIAMEISRMRELERLQMERQ--QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2545 KQAEEigEKLHRTELATQEkvtlvqtlEIQRQqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqllqe 2624
Cdd:pfam17380 438 RRLEE--ERAREMERVRLE--------EQERQ---QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-------- 496
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2625 tqaLQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQmeqerqrlvaSMEEARQRQHE 2698
Cdd:pfam17380 497 ---LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ----------EMEERRRIQEQ 557
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1629-1886 |
3.07e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1629 AQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALEELRLQAEEAERRLR--QAEVERARQVQVALET 1706
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1707 AQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1786
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1787 EVAQQKSLAQaeaekqkeeaerearrrgkaEEQAVRHRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQQR 1866
Cdd:COG4942 171 AERAELEALL--------------------AELEEERAALEALKAERQKLLAR--------LEKELAELAAELAELQQEA 222
|
250 260
....*....|....*....|
gi 1820553714 1867 QLLEEELARLQHEAAAATQK 1886
Cdd:COG4942 223 EELEALIARLEAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1827-2157 |
3.37e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1827 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1906
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1907 SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ----LAEEDAARQRAEAERVLAEKLAAISEA 1982
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAEQALDELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1983 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEE 2062
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2063 EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK 2142
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
330
....*....|....*
gi 1820553714 2143 AALEEVERLKAKVEE 2157
Cdd:COG4372 356 LELLSKGAEAGVADG 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1484-1743 |
3.55e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1484 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQE--EVVRREEAAVDAQQQKrsiQEELQQ 1561
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkEELRQSREKHEELEEK---YKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1562 LRQSSEAEIQAKARQAEAAERSRLRIEEEIRVvrLQLEATERqrggaEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQ 1641
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKT--LTQRVLER-----ETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1642 DESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAE--VERARQVQVALETAQRSAEAeLQSKR 1719
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEalLEELRSLQERLNASERKVEG-LGEEL 260
|
250 260
....*....|....*....|....
gi 1820553714 1720 ASFAEKTAQLERSLQEEHVAVAQL 1743
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQL 284
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1918-2189 |
3.62e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1918 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEA-EIALKEK 1996
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1997 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfeKAAA 2076
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2077 GKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK-V 2155
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270
....*....|....*....|....*....|....
gi 1820553714 2156 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2189
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE 290
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
181-288 |
3.95e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 49.66 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 181 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 247
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1820553714 248 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 288
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1360-1586 |
4.55e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1360 LQDARQRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakk 1439
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1440 pKVQSGSESVIQEYVDL------RTRYSELTTLTSQyiKFISETLRRMEEEERLAEQQRA------EERERLAEVEAALE 1507
Cdd:COG4942 94 -ELRAELEAQKEELAELlralyrLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREqaeelrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1508 KQRqlaeahaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQsSEAEIQAKARQAEAAERSRLR 1586
Cdd:COG4942 171 AER-------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1970-2741 |
4.85e-06 |
|
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: 53.15 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1970 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqHKADIEERLAQLRKASDSELERQKgl 2049
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGYELLKEK-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2050 vEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAED-TLRSKEQAELEAARQRQLAAEEEQRRREAEERVQ 2128
Cdd:TIGR02169 233 -EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2129 KSLAAEEEAARQRKAALEEVERLKAKVEEARR----LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAvqqkeqelqq 2204
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEReieeERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA---------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2205 tlqqeqSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQlaeeqaqaraqaqaaaeklrkdaeqeAV 2284
Cdd:TIGR02169 382 ------ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA--------------------------AI 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2285 RRAQAEQAALR-QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEA---TEAARQR 2360
Cdd:TIGR02169 430 AGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQArasEERVRGG 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2361 SQVEEELFS----VRVQMEELSKLKAR------IEAENR--ALILRDKDNTQR---FLQEEA---------EKMKQVAEE 2416
Cdd:TIGR02169 510 RAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMRDERRD 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2417 AARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAEAELLQ 2470
Cdd:TIGR02169 590 LSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGGILFS 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2471 QQKElaqEQARRLQEDKEQMAQQLAeetqGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEI 2550
Cdd:TIGR02169 670 RSEP---AELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2551 GEKLhrtelatqekvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-----EAKLLQLKSEEMQtvQQEQLLQET 2625
Cdd:TIGR02169 743 EEDL--------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQ--AELSKLEEE 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2626 QALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEE---G 2702
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESrlgD 886
|
810 820 830
....*....|....*....|....*....|....*....
gi 1820553714 2703 VRRKQEELQQLEQQRRQQEELLAEENQRLREQLQRLEEQ 2741
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2279-2504 |
5.36e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2279 AEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAAR 2358
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2359 --QRSQVEEELFSVRVQMEELSKLKARIEAENRaLILRDKD--NTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQL 2433
Cdd:COG3883 94 alYRSGGSVSYLDVLLGSESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKaELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2434 AEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRT 2504
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1199-1641 |
5.59e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1199 TLRSELEltlGKLEqvRSLSAIY-----LEKLKTISLVIRSTQgaeEVLRAHEEQL-----------KEAQAVPATLPE- 1261
Cdd:pfam15921 437 AMKSECQ---GQME--RQMAAIQgknesLEKVSSLTAQLESTK---EMLRKVVEELtakkmtlesseRTVSDLTASLQEk 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1262 ---LEATKASLKKLRAQAEAQQPMFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVAQLLE-------RWQAV 1328
Cdd:pfam15921 509 eraIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrTAGAM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1329 LAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGEKVEECQrf 1408
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR-- 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1409 aKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEERLA 1488
Cdd:pfam15921 667 -NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1489 eqqraeererlaeVEAALEKQRQLAEAHAQAKAqaereakelqqrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQssEA 1568
Cdd:pfam15921 726 -------------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ--EL 778
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1569 EIQAKARQAEAAERSRLRIEEEirvvRLQLEATERqrggaegELQALRAQAEEAEAQKRQAQEEAERLRRQVQ 1641
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQER----RLKEKVANM-------EVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3531-3563 |
5.64e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 5.64e-06
10 20 30
....*....|....*....|....*....|...
gi 1820553714 3531 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 3563
Cdd:pfam00681 7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2072-2554 |
5.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2072 EKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERvQKSLAAEEEAARQRKAALEEVERL 2151
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2152 KAKVEEARRLRERAEQESARqlqlaqeaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAE 2231
Cdd:COG4717 128 LPLYQELEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2232 EARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKK-- 2309
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2310 ----------FAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAArqrsqveEELFSVRVQMEELSK 2379
Cdd:COG4717 279 lflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2380 LKARIE-AENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmqAVQE 2458
Cdd:COG4717 352 LLREAEeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2459 ATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEAER--LKLRMAE--MSRAQ 2533
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEewAALKLALelLEEAR 506
|
490 500
....*....|....*....|..
gi 1820553714 2534 ARAEEDAQ-RFRKQAEEIGEKL 2554
Cdd:COG4717 507 EEYREERLpPVLERASEYFSRL 528
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
756-848 |
5.91e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 756 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 835
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1820553714 836 ALQTQWSWMLQLC 848
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1196-2062 |
6.03e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1196 AAPTLRsELELTLGKLEQVRSLSAIYLEKLKTISLVIRST--------QGAEEVLRAHE-------EQLKEAQAVPATLP 1260
Cdd:TIGR00606 187 ALETLR-QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYEneldplkNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1261 ELEATKASLKKLRAQAEAQQPMFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRERVaqllerwqavlaqtdvrQREL 1339
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDC-----------------QREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1340 EQLGRQLRYYRESADPLgawlqDARQRQEQIQAMPLADSQAVREQLRQEKAL---LEEIER-----------HGEKVEEC 1405
Cdd:TIGR00606 329 EKLNKERRLLNQEKTEL-----LVEQGRLQLQADRHQEHIRARDSLIQSLATrleLDGFERgpfserqiknfHTLVIERQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1406 QRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTRYSELTTLT--SQYIKFISETLRRM 1481
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLEgsSDRILELDQELRKA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1482 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKELQQRMQEEVVRREEAAVDAQQQK---RSIQEE 1558
Cdd:TIGR00606 484 ERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKiksRHSDEL 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1559 LQQLRQSSEAEIQAKARQAEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAE-----AQKRQAQE-E 1632
Cdd:TIGR00606 563 TSLLGYFPNKKQLEDWLHSKSKEINQTR--DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdVCGSQDEEsD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1633 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ-------RALQALEELRLQAEEAERRLRQA------------E 1693
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLApdklksteselkK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1694 VERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQL 1773
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1774 KANEALRlrlqaeEVAQQKSlaqaeAEKQKEEAEREARRRGKAEEQAVRHRELAeQELEKQRQLAEGTAQQRLAAEQELI 1853
Cdd:TIGR00606 800 ELKDVER------KIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVV-SKIELNRKLIQDQQEQIQHLKSKTN 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1854 RLRAETEQ---GEQQRQLLEEELARLQHEA----AAATQKRQE---LEAELAKVRAEMEVLLASK----ARAEEESRSTS 1919
Cdd:TIGR00606 868 ELKSEKLQigtNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISSKetsnKKAQDKVNDIK 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1920 EKSKQRLEAEAGRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE------AERVLAEKLaaisea 1982
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNL------ 1021
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1983 TRLKTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEE 2062
Cdd:TIGR00606 1022 TLRKRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1906-2105 |
6.51e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1906 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAISEATRL 1985
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1986 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEIL 2065
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1820553714 2066 ALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 2105
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1847-1942 |
6.54e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.65 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1847 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1926
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 1820553714 1927 EAEAGRFrELAEEAAR 1942
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1489-1671 |
6.68e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1489 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAavdaqqqkrsiqeELQQLRQSSEA 1568
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-------------EEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1569 EIQAKARQAEAAERSRLRIEEEIRVVRLQLEAterqrggAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1648
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 1820553714 1649 QAEAELALRVKAEAEAAREKQRA 1671
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRK 185
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
291-398 |
6.72e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 291 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 369
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1820553714 370 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 398
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2276-2596 |
6.77e-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: 51.99 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2276 RKDAEQEAVRRAQAEQA----ALRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQknlldeeLQRLKA 2351
Cdd:pfam19220 91 RLAKLEAALREAEAAKEelriELRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2352 EATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEkmkqvaeeaarlsVAAQEAARLR 2431
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERER 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2432 QLAEEDLAQQRALAEKM-LKEKMQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAEETQGFQRT---LEA 2507
Cdd:pfam19220 228 AEAQLEEAVEAHRAERAsLRMKLEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2508 ERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLR 2586
Cdd:pfam19220 305 DLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLK 377
|
330
....*....|
gi 1820553714 2587 EaiaELEREK 2596
Cdd:pfam19220 378 E---ELQRER 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1880-2111 |
7.21e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1880 AAAATQKRQELEAELAKVRAEMEVL---LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1956
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1957 AEEDAARQRAEAERVLAeKLAAISEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRlEEQAAQHKADIEErLAQLR 2036
Cdd:COG4942 95 LRAELEAQKEELAELLR-ALYRLGRQPPLA-----LLLSPEDFLDAVRRLQYLKYLAPAR-REQAEELRADLAE-LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2037 KASDSELERQKglvedtlRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 2111
Cdd:COG4942 167 AELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1818-2109 |
7.32e-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: 51.99 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQH-------EAAAATQKRQEL 1890
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1891 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1969
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1970 rvlaEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SDSELERQ 2046
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2047 KGLVEDTLRQRRQVEEEILALKASFEKAAagkAELELELGRIRSNaedtlRSKEQAELEAARQ 2109
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQAN---RRLKEELQRERAE-----RALAQGALEIARE 399
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1498-1679 |
7.74e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1498 RLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmqeeVVRREEAAVDAQQQKRSIQEELQQLRQSSEaeiQAKARQA 1577
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1578 EAaersrlRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL--- 1654
Cdd:COG1579 84 NV------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELeae 157
|
170 180
....*....|....*....|....*..
gi 1820553714 1655 --ALRVKAEAEAAREKQRALQALEELR 1679
Cdd:COG1579 158 leELEAEREELAAKIPPELLALYERIR 184
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2300-2521 |
8.64e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2300 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEE-LS 2378
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2379 KLKARIEAENRALILRDKDNTQRFLQEeAEKMKQVAEEAARLsVAAQEAARlrqlaeEDLAQQRALAEKMLKEKMQAVQE 2458
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 2459 ATRLKAEAELLQQQKE-----LAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAER 2521
Cdd:COG3883 166 LEAAKAELEAQQAEQEallaqLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2094-2498 |
8.88e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2094 DTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQrkaALEEVERLKAKVEEARRLRERAEQESaRQL 2173
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSASSEELSEEK-DAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2174 QLAQEAAQKRLQAEEKAHAFAVQQKEQELQQtlqqeqsvLDRLRSEAevarraaeeaeearvqaerEAAQSRRQVEEAER 2253
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETE--------LERMKERA-------------------KKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2254 lKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTlrqkaQVEQELTTLRLQLE 2333
Cdd:pfam07888 174 -KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE-----ALLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2334 ETDHQKNLLDEELqrlkaeaTEAARQRSQVEEELFSVRVQMEELSKLKARIE---AENRALILRDKDNTQRFLQEEAEKM 2410
Cdd:pfam07888 248 ASERKVEGLGEEL-------SSMAAQRDRTQAELHQARLQAAQLTLQLADASlalREGRARWAQERETLQQSAEADKDRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2411 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQM 2490
Cdd:pfam07888 321 EKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQL 397
|
....*...
gi 1820553714 2491 AQQLAEET 2498
Cdd:pfam07888 398 EQRLETVA 405
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1488-1916 |
8.90e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.83 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1488 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1567
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1568 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRK 1647
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1648 RQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTA 1727
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1728 QLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1807
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1808 REARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKR 1887
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 1820553714 1888 QELEAELAKVRAEMEVLLASKARAEEESR 1916
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1446-1734 |
9.27e-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: 51.76 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1446 SESVIQEyvDLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-A 1519
Cdd:pfam15450 219 AESSLRE--ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1520 KAQAERE-AKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE------AAERSRLRIEEEir 1592
Cdd:pfam15450 295 KGQLEESqAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1593 VVRLQLEATERQRGGAEGE-LQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarekqra 1671
Cdd:pfam15450 373 TLGLKLSEAKKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKA------- 445
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 1672 lqaleelrlqaeeaerrlRQAEVERARQ--------VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQ 1734
Cdd:pfam15450 446 ------------------REFEVEAMRQelaallssVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1564-1778 |
9.93e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1564 QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDE 1643
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1644 SQRKRQAEA--------ELALRVKAEAEAAREKQRALQALEELRLQAEEAerrlrQAEVERARQVQVALETAQRSAEAEL 1715
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1716 QSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1778
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1540-1679 |
1.00e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.20 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1540 RREEAAVD-AQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlriEEEIRVVRLQLEATER---QRGGAEGELQAL 1615
Cdd:COG1566 79 TDLQAALAqAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAA-----QAQLDLAQRELERYQAlykKGAVSQQELDEA 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1616 RAQAEEAEAQKRQAQEEAERLRRQVQDESQrKRQAEAELalrvkAEAEAAREKQRALQALEELR 1679
Cdd:COG1566 154 RAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQAELNLARTTIR 211
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1222-1690 |
1.09e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1222 LEKLKTISLVIRSTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraQAEAQQpMFDALRDELRGAQEVGERLQ 1301
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1302 QRHGERDVEVERWRERVAQLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLQDARQRQEQIqampl 1375
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1376 ADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK-PKVQSGSESVIQEYV 1454
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwVKLAQDTGLNLRSPE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1455 DLRTRYSEL-----------TTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL---------- 1512
Cdd:pfam05557 280 DLSRRIEQLqqreivlkeenSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgy 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1513 ------------AEAHAQAKAQAEREAKELQQRMQeevVRREEAAVDAQQQKRSIQEELQQLrQSSEAEIQAKARQAEAA 1580
Cdd:pfam05557 359 railesydkeltMSNYSPQLLERIEEAEDMTQKMQ---AHNEEMEAQLSVAEEELGGYKQQA-QTLERELQALRQQESLA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1581 ERSRLRIE-----EEIRVVRLQLEATERQRGGAEGEL--QALR------------------AQAEEAEAQKRQA-QEEAE 1634
Cdd:pfam05557 435 DPSYSKEEvdslrRKLETLELERQRLREQKNELEMELerRCLQgdydpkktkvlhlsmnpaAEAYQQRKNQLEKlQAEIE 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1635 RLRRQVqdesqRKRQAEAELALRVKAEAEAAREKQralqaLEELRLQAEEAERRLR 1690
Cdd:pfam05557 515 RLKRLL-----KKLEDDLEQVLRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
178-277 |
1.10e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 47.65 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 178 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 253
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1820553714 254 LVNIRNDDIADGNPKLTLGLIWTI 277
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4065-4103 |
1.20e-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: 1.20e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 4065 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 4103
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1815-2109 |
1.20e-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: 52.14 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQE 1889
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEESRAVTKELTTLAQGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1890 LEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRALAEEAKRQRQLAE 1958
Cdd:NF012221 1632 LDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAGVAQGEQNQANAE 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1959 EDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERlaqlRKA 2038
Cdd:NF012221 1710 QDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNR----QGA 1785
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2039 SDSELERQKGLVEDtlrqrrqVEEEILALKASFEKAAAGKaelelelgrirsNAEDtLRSKEQAELEAARQ 2109
Cdd:NF012221 1786 AGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG-LTEQEQEALEGATN 1836
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2318-2870 |
1.33e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2318 KAQVEQELTTLRLQLEETDHQKNLLDEELQRlkaEATEAARQRSQVEEELFSVRVQMEELSKLKAriEAENRALILRDKD 2397
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2398 NTQ-RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2472
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2473 ----KELAQEQARRLQEDKEQMaQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEmsraqaraEEDAQRFRKQAE 2548
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2549 EIGEKLHRTElatQEKVTLVQT-------LEIQ----RQQSDHDAERLREAIAELEREKEK---LQQEAKLLQLKSEEMq 2614
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQArekeihdLEIQltaiKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKEL- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2615 TVQQEQLLQETQALQQSFLSEKDsllQRERFIEQekakLEQLFQDEVakaqqlreeqqRQQQQMEQERQRLVASMEEARQ 2694
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKK---QEERMLKQ----IENLEEKEM-----------NLRDELESVREEFIQKGDEVKC 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2695 RQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQRLEEQH-------RAALAHSEEVTALQVAATKTlpngr 2767
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHqenkalkKKGSAENKQLNAYEIKVNKL----- 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2768 dALDGPATEAEPEHSFDGLRQKVPAQRLQEAGIL-----------SAEELQR---LAQGHTTVDELARREDVRH----YL 2829
Cdd:pfam05483 642 -ELELASAKQKFEEIIDNYQKEIEDKKISEEKLLeevekakaiadEAVKLQKeidKRCQHKIAEMVALMEKHKHqydkII 720
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1820553714 2830 QGRSSIAGLLLKPTSEKLSVYAALQRQLLSPGTALILLEAQ 2870
Cdd:pfam05483 721 EERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1476-1713 |
1.38e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 51.13 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAEREAKelqqrmqeevvrreeAAVDAQQ 1550
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAK---------------AAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1551 QKRSIQEELQQLRQSSEAEIQAKARqAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqalRAQAEEAEAQKRQAQ 1630
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAK-AKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA------KAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1631 EEAERLRRQVQDESQRKRQAEAelalrVKAEAeAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1710
Cdd:PRK07735 151 EEVTEEEEETDKEKAKAKAAAA-----AKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
...
gi 1820553714 1711 AEA 1713
Cdd:PRK07735 225 QGN 227
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1618-1751 |
1.45e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1618 QAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElalRVKAEAEAAREKQRALQALEELRlQAEEAERRLRQAEVERA 1697
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE---RLAAQEQKKQAEEAAKQAALKQK-QAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1698 RQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRA 1751
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKA 203
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2406-2565 |
1.47e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.03 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2406 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2485
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2486 DKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2565
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1540-1893 |
1.52e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1540 RREEAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQA 1619
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1699
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1700 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1779
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1780 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1859
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 1820553714 1860 EQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1893
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1406-1737 |
1.65e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.17 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1406 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1484
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1485 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA--------KELQQRMQEEVVRREEAAVDAQQQKRSIQ 1556
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1557 EELQQLRQsSEAEIQAKarQAEAaerSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRAQAEEAEAQKRQA------ 1629
Cdd:NF033838 201 RDEEKIKQ-AKAKVESK--KAEA---TRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1630 --------QEEAERLRRQVQDE-------SQRKRQAEAElalRVKAEAEAAREKQR-------ALQALEELRLQAEEAER 1687
Cdd:NF033838 272 epatpdkkENDAKSSDSSVGEEtlpspslKPEKKVAEAE---KKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDV 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1688 RLRQAEVERARQV--QVALETAQRSAEAELQSKRA--SFAEKTAQLERSLQEEH 1737
Cdd:NF033838 349 KVKEAELELVKEEakEPRNEEKIKQAKAKVESKKAeaTRLEKIKTDRKKAEEEA 402
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2240-2429 |
1.67e-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: 51.11 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2240 EAAQSRRQVEEAERLKQlaeeqaqaraQAQAAAEKLRKDAEQEAVRRAqaEQAALRQKQAADAEMEKHKKFAEQTLRQKA 2319
Cdd:pfam15709 349 EVERKRREQEEQRRLQQ----------EQLERAEKMREELELEQQRRF--EEIRLRKQRLEEERQRQEEEERKQRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2320 QVEQElttlRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEElfsvrvQMEELSKLKARIEAENRALILRDKDNT 2399
Cdd:pfam15709 417 AQERA----RQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM------QLAEEQKRLMEMAEEERLEYQRQKQEA 486
|
170 180 190
....*....|....*....|....*....|....*
gi 1820553714 2400 QRFLQEEAEKMKQVAEEAARLSVA-----AQEAAR 2429
Cdd:pfam15709 487 EEKARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1916-2082 |
1.70e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1916 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALK 1994
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1995 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQR--RQVEEEILALKASFE 2072
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 1820553714 2073 KAAAGKAELE 2082
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2281-2749 |
1.77e-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: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2281 QEAVRRAQAEQAALRQKQAADAEMEKHKKFAE--QTLRQKAQVEQELTTLRLQLEETDHqknlLDEELQRLKAEATEAAR 2358
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAelEYLRAALRLWFAQRRLELLEAELEE----LRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2359 QRSQVEEELFSVRVQM-----EELSKLKARIEAENRALilRDKDNTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQ 2432
Cdd:COG4913 317 RLDALREELDELEAQIrgnggDRLEQLEREIERLEREL--EERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2433 LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAqeqARRLQEDKEQMAQQLAEETQ------------- 2499
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI---PARLLALRDALAEALGLDEAelpfvgelievrp 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2500 --------------GFQRTLEAERQRQLEMSAEAERLKLRM-------AEMSRAQARAEEDAQRFrkqAEEIGEKLH--- 2555
Cdd:COG4913 472 eeerwrgaiervlgGFALTLLVPPEHYAAALRWVNRLHLRGrlvyervRTGLPDPERPRLDPDSL---AGKLDFKPHpfr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2556 ---RTELATQEKVTLVQTLEIQRQQS----------------DHDAERL-----------REAIAELEREKEKLQQEAKL 2605
Cdd:COG4913 549 awlEAELGRRFDYVCVDSPEELRRHPraitragqvkgngtrhEKDDRRRirsryvlgfdnRAKLAALEAELAELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2606 LQLKSEEMQTVQQEQLLQETQALQ-QSFLSEKDSLLQRERFIEQEKAKLEQL--FQDEVAKAQQLREEQQRQQQQMEQER 2682
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2683 QRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEEnQRLREQLQRLEEQHRAALAHS 2749
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEER 774
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1479-1594 |
1.82e-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: 51.11 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1479 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-EREAKELQQRMQEEVVRREEAAVD---------A 1548
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKR----SIQEELQQLRQSSEAEiqaKARQAEAAERsRLRIEEEIRVV 1594
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAE---EKARLEAEER-RQKEEEAARLA 508
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1819-2761 |
1.86e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1819 QAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAeLAKVR 1898
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1899 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1970
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1971 VLAEKLAAISEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---AQHKADIEERLAQLRKASDSELERQK 2047
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2048 GLVEDTLRQRRQVEEEILALKasFEKAAAGKAElelelgrirsNAEDTLRSKEQAELEAARQRqlaaeeeqrrreaeerv 2127
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELK--FVIKELQQLE----------GSSDRILELDQELRKAEREL----------------- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2128 qkSLAAEEEAARQRKAALEEVERLKAKVEEARRlreraeqesarqlQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQ 2207
Cdd:TIGR00606 488 --SKAEKNSLTETLKKEVKSLQNEKADLDRKLR-------------KLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2208 QEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRrqveeaERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRA 2287
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTR------DRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2288 QAEQAAlrQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEEL 2367
Cdd:TIGR00606 627 KLFDVC--GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2368 FSVRVQMEELSKLKARIEAEnRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSvaaQEAARLRQLAEEDlaqqralaEK 2447
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKR-RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN---RDIQRLKNDIEEQ--------ET 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2448 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQedkeqmaqQLAEETQG--FQRTLEAERQRQLEMSAEAERLKLR 2525
Cdd:TIGR00606 773 LLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIA--------QQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSK 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2526 MAEMSRAQARAEEDAQRFRKQAEEIG-EKLHRTELATQEKVTLVQTLEIQR--QQSDHDAERLREAIAELEREKEKLQQE 2602
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKsEKLQIGTNLQRRQQFEEQLVELSTevQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2603 AKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSllqrERFIEQEKAKLEQLFQDEVAKaqqlreeqqrqqqqmeqer 2682
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI----ENKIQDGKDDYLKQKETELNT------------------- 981
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2683 qrLVASMEEARQRQHEAEEGVRrkqeeLQQLEQQRRQQEELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQVAATK 2761
Cdd:TIGR00606 982 --VNAQLEECEKHQEKINEDMR-----LMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMK 1053
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2277-2602 |
1.88e-05 |
|
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: 50.19 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2277 KDAEQEAVRRAQAEQAALRQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEA 2356
Cdd:pfam15905 45 KDASTPATARKVKSLELKKKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2357 ARQRSQVEEELFSVRVQMEELSKLKARIEAENRAlilrdkDNTQRflqeeaekmkqvaeeaaRLSVAAQEAARLRQLAEE 2436
Cdd:pfam15905 114 VREKTSLSASVASLEKQLLELTRVNELLKAKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2437 DLAQQRALAEKMLKeKMQAVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRqLEMS 2516
Cdd:pfam15905 171 KMKEVMAKQEGMEG-KLQVTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2517 AEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREK 2596
Cdd:pfam15905 247 QLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEH 323
|
....*.
gi 1820553714 2597 EKLQQE 2602
Cdd:pfam15905 324 QKLQQK 329
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1824-2508 |
2.00e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1824 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAEteQGEQQRQLLEEELARLQHEAAAAT-----QKRQELEAELAKVR 1898
Cdd:PRK10246 233 KQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQ--QALAAEEKAQPQLAALSLAQPARQlrphwERIQEQSAALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1899 ---AEMEVLLASKARAEEESRSTSEKSKQRLEAEAG----------RFRELAEEAARLRALAEEAKRQRQlaEEDAARQR 1965
Cdd:PRK10246 311 qqiEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslntwlaehdRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1966 AEAERvlaEKLAAISEATRLKTEAEIAlkEKEAENERLRRLaedeafqRRRLEEQAAQHkADIEERLAQLrKASDSELER 2045
Cdd:PRK10246 389 LTHAE---QKLNALPAITLTLTADEVA--AALAQHAEQRPL-------RQRLVALHGQI-VPQQKRLAQL-QVAIQNVTQ 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2046 QKGLVEDTLRQRRQveeeilALKASFEKAAAGKAELELElGRIRSNAEdtlrskEQAELEAARQRQLAAEEEQRRreaee 2125
Cdd:PRK10246 455 EQTQRNAALNEMRQ------RYKEKTQQLADVKTICEQE-ARIKDLEA------QRAQLQAGQPCPLCGSTSHPA----- 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2126 rVQKSLAAEEEAARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQ 2204
Cdd:PRK10246 517 -VEAYQALEPGVNQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2205 TLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQsrRQVEEAErlKQLAEEQAQARAQAQAAAEKLRKDAEQEAV 2284
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHN--QQIIQYQ--QQIEQRQQQLLTALAGYALTLPQEDEEASW 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2285 RRAQAEQAALRQKQaadaeMEKHKKFAEQTlrqkAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--ATEAARQRSQ 2362
Cdd:PRK10246 667 LATRQQEAQSWQQR-----QNELTALQNRI----QQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQclSLHSQLQTLQ 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2363 VEEELFSVRVQmeelsKLKARIEAENRALILRDKDNTQRFLQEEaEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2442
Cdd:PRK10246 738 QQDVLEAQRLQ-----KAQAQFDTALQASVFDDQQAFLAALLDE-ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2443 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2508
Cdd:PRK10246 812 QHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1364-1683 |
2.03e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.21 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1364 RQRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ 1443
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1444 SGSESVIQEYVDLRTRYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKA 1521
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1522 QAereakelqqrMQEEVVRReEAAVDaqqqkrsiQEELQQLRQSSEAEIqakAR-QAEAAERSRLRIEEEIRVVRLQLEa 1600
Cdd:PRK10929 176 TA----------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQALRNQLN- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1601 TERQRggaegelqalraQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL---ALRVKAEA----EAAREKQRALQ 1673
Cdd:PRK10929 233 SQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQ 300
|
330
....*....|
gi 1820553714 1674 ALEELRLQAE 1683
Cdd:PRK10929 301 ALNTLREQSQ 310
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1489-1616 |
2.07e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 49.88 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1489 EQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAKELQQRMQEEVVrreeaavdaQQQKRSIQEELQQLRQSSE 1567
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEaAEQERKLLEEQQRELEQKL---------EDQERSYEEHLRQLKEKME 247
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1820553714 1568 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1616
Cdd:cd16269 248 EERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2281-2495 |
2.13e-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: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2281 QEAVRRAQAEQAALRQK-QAADAEMEkhkkfAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAarQ 2359
Cdd:COG3206 188 RKELEEAEAALEEFRQKnGLVDLSEE-----AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--L 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2360 RSQVEEELFSVRVQME-ELSKLKARIEAENRALilrdkdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2438
Cdd:COG3206 261 QSPVIQQLRAQLAELEaELAELSARYTPNHPDV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2439 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqarRLQEDKEQMAQQLA 2495
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ---RLEEARLAEALTVG 386
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1499-1593 |
2.18e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1499 LAEVEAALEKQRQLAEAHAQAKAQAEREAkelqQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR-QSSEAEIQAKARQA 1577
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1820553714 1578 EAAERSRLRI---EEEIRV 1593
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
181-288 |
2.36e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 47.31 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 181 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 247
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1820553714 248 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 288
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2274-2556 |
2.48e-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: 49.92 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2274 KLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKNLLDEELQRL 2349
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2350 KAEATEAARQRSQVEEELFSVRVQMEELSKL-----KARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAA 2424
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2425 QEAARLRQLAEE------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKEL-AQEQARRLQEDK---EQMAQQL 2494
Cdd:pfam13868 191 AQQEKAQDEKAErdelraKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELkERRLAEEAEREEeefERMLRKQ 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2495 AEETQGFQRTLEAERQRQLEMSAEAERL-KLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHR 2556
Cdd:pfam13868 271 AEDEEIEQEEAEKRRMKRLEHRRELEKQiEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2343-2549 |
2.49e-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: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2343 DEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIlRDKDNTQRFLQEEAEKMKQVAEEAARLSV 2422
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2423 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2494
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2495 AEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEE 2549
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
176-284 |
2.54e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.52 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 246
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1820553714 247 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 284
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1654-1902 |
2.61e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1654 LALRVKAEAEAAREKQRALQALEElRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1733
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1734 QEEHVAVAQLREEAERRAQQQAEAerareeaerelerWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1813
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1814 GKAEEQAVRHRELAEQELEKQRQLAEGTAQQRlaaeqeliRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1893
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 1820553714 1894 LAKVRAEME 1902
Cdd:COG4942 229 IARLEAEAA 237
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2940-2976 |
2.63e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.63e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 2940 IRLLEAQIATGGVIDPVHSHRVPVDVAYQRGYFNEEM 2976
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1604-1737 |
2.69e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1604 QRGGAEGELQALRAQAEEAEAQ-KRQAQEEAerlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALEELRLQA 1682
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVErKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQ 403
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 1683 EEAER---RLRQAEVERARQVQVA----LETAQRSAEAELQSKRASFAEKTAQLERSLQEEH 1737
Cdd:pfam15709 404 EEEERkqrLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ 465
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1484-1731 |
2.73e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.41 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1484 EERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQAKAQaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR 1563
Cdd:pfam05667 210 ERNAAELAAAQEWEEEWNSQGL---ASRLTPEEYRKRKR-TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1564 QSSEAEIQAK-------------ARQAEAAERS-----------RLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQA 1619
Cdd:pfam05667 286 GSSTTDTGLTkgsrfthteklqfTNEAPAATSSpptkveteeelQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAEAQKRQAQEEAERLRRQVqdesQRKRQAEAEL--------ALRVKAEAEAAR--------EKQRA--LQALEELRL- 1680
Cdd:pfam05667 366 KQVEEELEELKEQNEELEKQY----KVKKKTLDLLpdaeeniaKLQALVDASAQRlvelagqwEKHRVplIEEYRALKEa 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1681 ---QAEEAERRLRQAEVERARQVQVAletaqrsaeAELQSKRASFAEKTAQLER 1731
Cdd:pfam05667 442 ksnKEDESQRKLEEIKELREKIKEVA---------EEAKQKEELYKQLVAEYER 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2289-2458 |
3.03e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2289 AEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELF 2368
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2369 SVRVQmEELSKLKARIEAENRALILRDKDnTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2448
Cdd:COG1579 84 NVRNN-KEYEALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 1820553714 2449 LKEKMQAVQE 2458
Cdd:COG1579 162 EAEREELAAK 171
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1599-1736 |
3.07e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.84 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1599 EATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElalrvKAEAEAAREKQRALQALEEL 1678
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA-----KQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 1679 RLQAEEAerRLRQAEVERARQvqvALETAQRSAEAELQSKRASFAEKTAQLERSLQEE 1736
Cdd:TIGR02794 125 KAKQAAE--AKAKAEAEAERK---AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEA 177
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3934-3970 |
3.11e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.11e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 3934 LRLLDAQLATGGIVDPHLGFHLPLEVAYQRGYLNKDT 3970
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1474-1679 |
3.28e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1474 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQK 1552
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1553 RSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRAQAEEAEAQKR----- 1627
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1628 ------QAQEEAERLRRQVQDESQRKrQAEAELALR--VKAEAEAAREKQRALQALEELR 1679
Cdd:COG1842 156 sgidsdDATSALERMEEKIEEMEARA-EAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2400-2609 |
3.28e-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: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2400 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2479
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2480 ARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2559
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2560 ATQEKvtlvqTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2609
Cdd:pfam13868 191 AQQEK-----AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ 235
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1440-1633 |
3.39e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1440 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQ- 1518
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1519 -AKAQAEREAKELQQRMQEEVVRREE---AAVDAQQQ----KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEE 1590
Cdd:COG3206 263 pVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQiaalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1820553714 1591 IRV---VRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEA 1633
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2141-2659 |
3.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2141 RKAALEEVERLKAKVEEARRLRERAE--QESARQLQLAQEAAQKRLQAEEKAhAFAVQQKEQELQQTLQQEQSVLDRLRS 2218
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEdaREQIELLEPIRELAERYAAARERL-AELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2219 EAEVARRAAEEAEEARVQAEREAAQSRRQVEEA------ERLKQLAEEQAQaraqaqaaaekLRKDAEQEAVRRAQAEQA 2292
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQirgnggDRLEQLEREIER-----------LERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2293 ALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRV 2372
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2373 QMEELSKLKA---RIEAEnraLI-LRDKD-----------NTQRF-LQEEAEKMKQVAE----EAARLSVAAQEAARLRQ 2432
Cdd:COG4913 448 ALAEALGLDEaelPFVGE---LIeVRPEEerwrgaiervlGGFALtLLVPPEHYAAALRwvnrLHLRGRLVYERVRTGLP 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2433 LAEEDLAQQRALAEKM----------LKEKMQAVQEATRLKAEAELLQQQKELAQE------------------------ 2478
Cdd:COG4913 525 DPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCVDSPEELRRHPRAITRAgqvkgngtrhekddrrrirsryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2479 --QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLklrmaEMSRAQARAEEDAQRFRKQAEEIGEKLHR 2556
Cdd:COG4913 605 gfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-----QRLAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2557 TELATQEkvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEK 2636
Cdd:COG4913 680 LDASSDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
570 580 590
....*....|....*....|....*....|...
gi 1820553714 2637 DSLLQRERF----------IEQEKAKLEQLFQD 2659
Cdd:COG4913 756 AAALGDAVErelrenleerIDALRARLNRAEEE 788
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1815-2030 |
3.56e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 50.33 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRH--------RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1886
Cdd:PRK05035 447 KAEEAKARFearqarleREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1887 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE--EAKRQRQLAEEDAARQ 1964
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARakAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1965 RAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 2030
Cdd:PRK05035 607 VAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2903-2939 |
4.05e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.05e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 2903 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 2939
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4273-4301 |
4.05e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.05e-05
10 20
....*....|....*....|....*....
gi 1820553714 4273 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4301
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1849-2032 |
4.09e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1849 EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1927
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1928 AEagrfrelaeeaarlralAEEAKRQRQLAEEDAARQRAEAErvlaEKLAAISEATRLKTEAEIALKEKEAENErlRRLA 2007
Cdd:COG1579 96 KE-----------------IESLKRRISDLEDEILELMERIE----ELEEELAELEAELAELEAELEEKKAELD--EELA 152
|
170 180
....*....|....*....|....*
gi 1820553714 2008 EDEAfQRRRLEEQAAQHKADIEERL 2032
Cdd:COG1579 153 ELEA-ELEELEAEREELAAKIPPEL 176
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1815-1982 |
4.17e-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: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELArlqhEAAAATQKRQELEAEL 1894
Cdd:TIGR02794 99 AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKA----KAAAEAKKKAEEAKKK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1895 AKVRAEMEVLLASKARAeEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1974
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAKA-EEAKAKAEAAKAKAAAEA------AAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
....*...
gi 1820553714 1975 KLAAISEA 1982
Cdd:TIGR02794 248 KQGGARGA 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2408-2769 |
4.18e-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: 50.07 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2408 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQED 2486
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2487 keqmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2566
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2567 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqQEQLLQETQALQQSFLSEKDSLLQRERFI 2646
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-LEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2647 EQEKAKLEQL------FQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRkqeelqqleqqRRQQ 2720
Cdd:TIGR02169 395 EKLKREINELkreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-----------LAAD 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1820553714 2721 EELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQVAATKTLPNGRDA 2769
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1480-1698 |
4.20e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.62 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1480 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1559
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1560 QQLRQSSEAEIQAKARQAEAAERSRlrieeeirvvrlqleaterqrggAEGELQALRAQAEEAEaqkrQAQEEAERLRRQ 1639
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEALKAKDHK-----------------------AFDLKQESKASEKEAE----DKELEAQKKREP 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1640 VQDESQR-KRQAEAElalrVKAEAEAAREKQR---------ALQALEELRLQAEEAERRLRQAEVERAR 1698
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAIDSSNpvyglkvvdPITNLSELVLIDLKTEVRLRESAQQTIR 397
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2389-2585 |
4.20e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2389 RALILRDKDNTQRFLQEEAEKMKQVAEEAarLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQeatRLKAEAEL 2468
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---NLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2469 LQQQKELAQEQARRLQEDKEQMAQQLAEetqgfQRTLEAERQRQLE----MSAEAERLKLrmaeMSRAQARAEEDAQRFR 2544
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEE-----LEELIEEQLQELErisgLTAEEAKEIL----LEKVEEEARHEAAVLI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1820553714 2545 KQAEEIGEklhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2585
Cdd:PRK12704 176 KEIEEEAK-----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1507-1638 |
4.25e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.57 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1507 EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQL--RQSSEAEIQAKARQAEAAERSR 1584
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1585 LRIEEEIRVVRLQLEATERQRGGAEGELQalraqaeeaEAQKRQAQEEAERLRR 1638
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1544-1725 |
4.49e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1544 AAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAE 1623
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1624 AQKRQA--QEEAERLRRQVQDESQRKRQAEAELaLRVKAEAEAAREKQRALQA-LEELRLQAEEAERRLRQAEVERARQv 1700
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIESLKRRISDLEDEI-LELMERIEELEEELAELEAeLAELEAELEEKKAELDEELAELEAE- 157
|
170 180
....*....|....*....|....*
gi 1820553714 1701 qvaletaqrsaEAELQSKRASFAEK 1725
Cdd:COG1579 158 -----------LEELEAEREELAAK 171
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3487-3521 |
4.51e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.51e-05
10 20 30
....*....|....*....|....*....|....*
gi 1820553714 3487 LLQGSGCLAGIYLEDSKEKVSIYEAMRRGLLRPST 3521
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1475-1957 |
4.64e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1475 SETLRRMEEEERLAEQQRAEE--RERLAEVEAALEKQRQLAEA-----HAQAKAQAEREAKELQ-QRMQEEVVRREEAAV 1546
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAEllRKQLSKTQEELEAQVTLVESlrkyvGEQVPPEVHSQTWELErQELLDTMQHLQEDRA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1547 DAQQQKRSIQEELQQLRQS---SEAEIQAKARQAEAAE-------RSRL-RIEEEIRVVRLQLEATERQRggaEGELQAL 1615
Cdd:pfam07111 260 DLQATVELLQVRVQSLTHMlalQEEELTRKIQPSDSLEpefpkkcRSLLnRWREKVFALMVQLKAQDLEH---RDSVKQL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1616 RAQAEEAEAQKRQAQEEAERLRRQVQDESqrkrqaeAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAeVE 1695
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKA-------AEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFV-VN 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1696 RARQVQVALETA-----QRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER 1770
Cdd:pfam07111 409 AMSSTQIWLETTmtrveQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1771 WQLKANEALRL-------------------RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQEL 1831
Cdd:pfam07111 489 ERNRLDAELQLsahliqqevgrareqgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1832 EKQRQLAeGTAQQRLAAEQElIRLRAETEQGEQQRQLLEEELAR-------LQHEAAAATQKRQELEaelakvraemevl 1904
Cdd:pfam07111 569 TQQQEIY-GQALQEKVAEVE-TRLREQLSDTKRRLNEARREQAKavvslrqIQHRATQEKERNQELR------------- 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1905 laskaRAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1957
Cdd:pfam07111 634 -----RLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLA 681
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3231-3267 |
4.93e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.93e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 3231 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPQEQG 3267
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2375-2502 |
4.96e-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: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2375 EELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQLAEEDLAQQRALAE--KMLKEK 2452
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEK 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2453 MQavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQ 2502
Cdd:cd16269 246 ME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2392-2751 |
4.96e-05 |
|
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: 50.06 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2392 ILRDKDNTQRFLQEEA---EKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL---AEKmlKEKMQAVQEATRlKA 2464
Cdd:TIGR02168 149 IIEAKPEERRAIFEEAagiSKYKERRKETERKLERTRENlDRLEDILNELERQLKSLerqAEK--AERYKELKAELR-EL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2465 EAELLQQQKELAQEQARRLQEDKEQMAQQLAEEtqgfqrtleaerQRQLEMS-AEAERLKLRMAEMSRAQARAEEDAQRF 2543
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEEL------------TAELQELeEKLEELRLEVSELEEEIEELQKELYAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2544 RKQAEEIgeklhrtelaTQEKVTLVQtleiQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQ 2623
Cdd:TIGR02168 294 ANEISRL----------EQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2624 ETQALQQSFLSEKDSLLQRERfIEQEKAKLEQLFQDEvakaqqlreeqqrqqqqmEQERQRLVASMEEARQRQHEAEEGV 2703
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQ-LETLRSKVAQLELQI------------------ASLNNEIERLEARLERLEDRRERLQ 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1820553714 2704 RRKQEELQQLEQQRRQQEELLAEENQRLREQLQRLEEQHRAALAHSEE 2751
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1814-1936 |
5.17e-05 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 48.28 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1814 GKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQH-----EAAAATQKR 1887
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1888 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1936
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2346-2559 |
5.50e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2346 LQRLKAEATEAARQRSQVEEElfsvrvQMEELSKLKARIEAENRALilrdkdnTQRFLQEEAEKmKQvAEEAARLSVAAQ 2425
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL-------EKERLAAQEQK-KQ-AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2426 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQGFQRT 2504
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2505 LEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2559
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1540-1878 |
5.85e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1540 RREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQA 1619
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1699
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1700 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1779
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1780 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1859
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330
....*....|....*....
gi 1820553714 1860 EQGEQQRQLLEEELARLQH 1878
Cdd:COG4372 323 ELAKKLELALAILLAELAD 341
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
180-281 |
5.88e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.49 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 180 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 255
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHF 281
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2240-2515 |
6.11e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2240 EAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQ--EAVRRAQAE--QAALRQKQAADAEMEKHKKFAEQTL 2315
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQmdEIVERIQEEdqAEAEEKLEKQRQLREEIDEFNEEQA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2316 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQ-VEEELFSVRVQMEELSKLKARIEAENRALILR 2394
Cdd:pfam13868 141 EWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQDEKAERDELRAKLYQEEQERKER 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2395 DKdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML---KEKMQAVQEATRLKAEAELLQQ 2471
Cdd:pfam13868 221 QK---EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEdeeIEQEEAEKRRMKRLEHRRELEK 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1820553714 2472 QKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEM 2515
Cdd:pfam13868 298 QIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1609-1743 |
6.12e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.60 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1609 EGELQALRAQAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERR 1688
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 1689 LRQ--AEVERARQvQVALETAQRSAEAELQSK----RASFAEKTAQLERSLQEEHVAVAQL 1743
Cdd:pfam09787 141 IKDreAEIEKLRN-QLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1929-2048 |
6.47e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 49.56 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1929 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLAEKLAAISEATRLKTEAEIA-LKEKEAE 1999
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2000 NERLRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA---SDSE-LERQKG 2048
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKAgweADSKtLRFSKG 261
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2409-2758 |
6.49e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2409 KMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALaekmLKEKMQAvqeatrlKAEAELLQQQKELAQEQARRLQEDKE 2488
Cdd:pfam02463 166 RLKRKKKEALK--KLIEETENLAELIIDLEELKLQE----LKLKEQA-------KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2489 QMAQQLAEEtqgFQRTLEAERQRQLEMSAEAErlklrmaemsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlV 2568
Cdd:pfam02463 233 KLNEERIDL---LQELLRDEQEEIESSKQEIE-----------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE---E 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2569 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqlLQETQALQQSFLSEKDSLLQRERFIEQ 2648
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE-----LKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2649 EKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEA-----EEGVRRKQEELQQLEQQRRQQEEL 2723
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeekkEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350
....*....|....*....|....*....|....*
gi 1820553714 2724 LAEENQRLREQLQRLEEQHRAALAHSEEVTALQVA 2758
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1815-1986 |
6.81e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLeeelarlqheaaaatqkrqELEAE 1893
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLL-------------------ELQAE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1894 LAKVRAemevllASKARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVL 1972
Cdd:PTZ00491 708 SAAVES------SGQSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAK 778
|
170
....*....|....
gi 1820553714 1973 AEKLAAIsEATRLK 1986
Cdd:PTZ00491 779 AKELADI-EATKFE 791
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2398-2865 |
6.91e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.20 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2398 NTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2477
Cdd:COG4995 7 LALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2478 EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2557
Cdd:COG4995 87 LALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2558 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKD 2637
Cdd:COG4995 167 ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2638 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQR 2717
Cdd:COG4995 247 AAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2718 RQQEELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQVAATktlpngrdaldgpATEAEPEHSFDGLRQKVPAQRLQE 2797
Cdd:COG4995 327 LAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLL-------------LLAALLALLLEALLLLLLALLAAL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2798 AGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLLLKP--TSEKLSVYAALQRQLLSPGTALI 2865
Cdd:COG4995 394 LLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2316-2614 |
7.03e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2316 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRD 2395
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2396 KDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKEL 2475
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE--REEEREAEREEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2476 AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLH 2555
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2556 RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2614
Cdd:pfam13868 262 EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2350-2540 |
7.05e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2350 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAAR 2429
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2430 LRQLAEEDLAQQrALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfQRTLEAER 2509
Cdd:TIGR02794 126 AKQAAEAKAKAE-AEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK-AKAEAAKA 203
|
170 180 190
....*....|....*....|....*....|.
gi 1820553714 2510 QRQLEMSAEAERLKLRMAEMsRAQARAEEDA 2540
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAA-EAERKADEAE 233
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2239-2602 |
7.55e-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: 48.74 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2239 REAAQSRRQVEEAErlkqlaeeqaqaraqaqaaaeklrkdaEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAeQTLRQK 2318
Cdd:pfam07888 73 RQRRELESRVAELK---------------------------EELRQSREKHEELEEKYKELSASSEELSEEKD-ALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2319 AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRAL--ILRDK 2396
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2397 DNTQRFLQEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKE 2474
Cdd:pfam07888 205 DTQVLQLQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2475 LAQ------EQARRLQEDKEQMAQqlaeETQGFQRTLEAERQRQLEMSAEAERLklrmaemsraqaraEEDAQRFRKQAE 2548
Cdd:pfam07888 281 AAQltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRL--------------EERLQEERMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2549 EIgeklhRTELATQEKVTLVQTLEIQRQQSDhdaerLREAIAELEREKEKLQQE 2602
Cdd:pfam07888 343 KL-----EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1479-1652 |
7.90e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.79 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1479 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREakelqQRMQEEVVRREEAAVDAQQQK-RSIQE 1557
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRR-FEEIRLRKQRLEEE-----RQRQEEEERKQRLQLQAAQERaRQQQE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1558 ELQQLRQSSEAEIQAKARQAEAAERSRLRiEEEIRVVrlqlEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEaerlR 1637
Cdd:pfam15709 427 EFRRKLQELQRKKQQEEAERAEAEKQRQK-ELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE----R 497
|
170
....*....|....*
gi 1820553714 1638 RQVQDESQRKRQAEA 1652
Cdd:pfam15709 498 RQKEEEAARLALEEA 512
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1496-1872 |
7.91e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1496 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvRREEAAVDAQQQKRSIQEELQQLRQSSEAEiqaKAR 1575
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERL-AELEAKRQAEEEAREAKAEAEQRAAELAAE---AAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1576 QAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1655
Cdd:COG3064 78 KLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1656 LRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1735
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1736 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1815
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1816 AEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1872
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALA 368
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2387-2830 |
8.60e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2387 ENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA 2466
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2467 ELLQQQKELAQEQARRLQEDKEQMAQqlaEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2546
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRAR---IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2547 AEEIGEKLHRT------ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKE------KLQQE----AKLLQLKS 2610
Cdd:TIGR00618 320 MRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhihTLQQQkttlTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2611 EEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASME 2690
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2691 EARQRQHEaeegvrrkqeelqqlEQQRRQQEELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQVAATKTLPNGRDAl 2770
Cdd:TIGR00618 480 QIHLQETR---------------KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS- 543
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2771 dgpatEAEPEHSFDGLRQKvpAQRLQEAGILSAEELQRLAQGHTTVDELARR-----EDVRHYLQ 2830
Cdd:TIGR00618 544 -----EEDVYHQLTSERKQ--RASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitVRLQDLTE 601
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2314-2546 |
8.69e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2314 TLRQKAQVEQELTTLRLQleetdhQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIL 2393
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2394 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2467
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2468 LLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2546
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2421-2699 |
8.86e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.06 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2421 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAEeTQG 2500
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLAA-ISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2501 FQRTLEAERQRQLEMSAEAERlklrmaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2580
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2581 DAE---RLREAIAE--LEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSllqrerfiEQEKAKLEQ 2655
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1820553714 2656 LFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQR-QHEA 2699
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1961-2192 |
8.96e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1961 AARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASD 2040
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2041 SELERQKGLVEDTL----RQRRQVEEEILALKASFEKAAAGKAELElELGRIRSNAEDTLRsKEQAELEAARQRQLAAee 2116
Cdd:COG4942 97 AELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELR-ADLAELAALRAELEAE-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2117 eqrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2192
Cdd:COG4942 173 -----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1814-1995 |
9.25e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1814 GKAEEQAVRHRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEAAAATQKRQELEA 1892
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1893 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDaarqrAEAERV 1971
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 1820553714 1972 LAEKLAAISEATRLKTEAEIALKE 1995
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1488-1649 |
9.44e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 48.75 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1488 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1567
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1568 AEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQAlRAQAEEAEAQKRQAQEEAERLRRQVQDESQRK 1647
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQA-EAERGERGRREERGRDGDDRDRRDRREQGDRR 215
|
..
gi 1820553714 1648 RQ 1649
Cdd:PRK12678 216 EE 217
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1564-1718 |
9.47e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.86 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1564 QSSEAEIQAKARQAEA-AERSRLRIEEEIRVvrlqleatERQRggaegeLQALRAQAEEAEAQ-----KRQAQEEAERLR 1637
Cdd:PTZ00491 664 QEAAARHQAELLEQEArGRLERQKMHDKAKA--------EEQR------TKLLELQAESAAVEssgqsRAEALAEAEARL 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1638 RQVQDE-SQRKRQAEAElalRVKAEAEAAREKQRALQALEELRLQAE---EAERRLRQAEVERARQVQVAL--ETAQRSA 1711
Cdd:PTZ00491 730 IEAEAEvEQAELRAKAL---RIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATKFERIVEALgrETLIAIA 806
|
....*....
gi 1820553714 1712 EA--ELQSK 1718
Cdd:PTZ00491 807 RAgpELQAK 815
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2828-2866 |
9.81e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 42.31 E-value: 9.81e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 2828 YLQGRSSIAGLLLKPTSEKLSVYAALQRQLLSPGTALIL 2866
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1549-1689 |
9.93e-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: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKRSIQEELQQLRQ---SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEG--ELQALRAQAEEAE 1623
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1624 AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALE----ELRLQAEEAERRL 1689
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEaeleELEAEREELAAKI 172
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1620-1699 |
1.09e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.79 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL----RVKAE--AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1692
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAqqqeLVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 1820553714 1693 EVERARQ 1699
Cdd:PRK11448 218 RKEITDQ 224
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1158-1708 |
1.10e-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: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1158 QRITEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQG 1237
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1238 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPMFDALRDELRGAQE-------VGERLQQRHGERDVE 1310
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRI 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1311 VERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQamplaDSQAVREQLRQEKA 1390
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIP-----KLKLPLKSIAVLEI 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1391 LLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESvIQEYVDLRTRYSELTT---LT 1467
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEG-LAEKSEVKASLSELTKellEI 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1468 SQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQR----MQEEVVRREE 1543
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKideeEEEEEKSRLK 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1544 A------AVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRA 1617
Cdd:pfam02463 759 KeekeeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1618 QAEEAEAQKRQ--AQEEAERLrrqvqDESQRKRQAEAELALRVKaEAEAAREKQRALQALEELRLQAEEAERRLRQAEVE 1695
Cdd:pfam02463 839 ALELKEEQKLEklAEEELERL-----EEEITKEELLQELLLKEE-ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL 912
|
570
....*....|...
gi 1820553714 1696 RARQVQVALETAQ 1708
Cdd:pfam02463 913 EEKENEIEERIKE 925
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4522-4559 |
1.11e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1820553714 4522 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 4559
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1931-2177 |
1.13e-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: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1931 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 2010
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2011 AFQRRRLEEQAAQHKADIEE------RLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELE 2084
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2085 LGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2163
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 1820553714 2164 RAEQESAR-QLQLAQ 2177
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1784-1960 |
1.15e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1784 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRHRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1859
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1860 EQGEQQRQLLEEELArlQHEAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1934
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 1820553714 1935 ELAEEAARLRALAEEAKRQRQLAEED 1960
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1648-1932 |
1.18e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1648 RQAEAELALRVKAEAEAAREKQR--ALQAleelRLQAEEAERRLRQAevERARQVQVALETAQRSAEAELQSKRASFAEK 1725
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAREARHK--KAAEARAAKDKDAVAAALARVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1726 TAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAErelerwQLKANEALRLRLQAEEVAQQKSlaqAEAEKQKEE 1805
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADP------KKAAVAAAIARAKAKKAAQQAA---NAEAEEEVD 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1806 AEREARRRGKAEEQAvrhRELAEQELEKQRQLAEGTAQQRLAAEQELIrLRAETEQGEQQRQLLEEElarlqheaaAATQ 1885
Cdd:PRK05035 577 PKKAAVAAAIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAI-ARAKAKKAEQQANAEPEE---------PVDP 643
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1820553714 1886 KRQELEAELAKVRAEmevlLASKARAEEESRSTSEKSKQRLEAEAGR 1932
Cdd:PRK05035 644 RKAAVAAAIARAKAR----KAAQQQANAEPEEAEDPKKAAVAAAIAR 686
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4103-4137 |
1.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.22e-04
10 20 30
....*....|....*....|....*....|....*
gi 1820553714 4103 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4137
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
181-278 |
1.24e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 181 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 247
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1820553714 248 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 278
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2285-2655 |
1.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2285 RRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLkaeatEAARQRSQVE 2364
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2365 EELFSVrvqMEELSKLKARIEAenraliLRDKDNTQRFLQEEAEKMKQVAEEAARlSVAAQEAARLRQLAE--EDLAQQR 2442
Cdd:COG4717 139 AELAEL---PERLEELEERLEE------LRELEEELEELEAELAELQEELEELLE-QLSLATEEELQDLAEelEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2443 ALAEKMLKekmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA--------------- 2507
Cdd:COG4717 209 AELEEELE---EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2508 -------ERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFR----KQAEEIGEKLHRTElATQEKVTLVQTLEIQRQ 2576
Cdd:COG4717 286 lallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdLSPEELLELLDRIE-ELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2577 QSDHDAER---LREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKL 2653
Cdd:COG4717 365 LEELEQEIaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL 444
|
..
gi 1820553714 2654 EQ 2655
Cdd:COG4717 445 EE 446
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1814-2146 |
1.31e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1814 GKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1893
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1894 LAKVRAEMEVLLASKARAEEES---RSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1970
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAeelQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1971 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLV 2050
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2051 EDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKS 2130
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330
....*....|....*.
gi 1820553714 2131 LAAEEEAARQRKAALE 2146
Cdd:COG4372 329 ELALAILLAELADLLQ 344
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1233-1684 |
1.37e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.26 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1233 RSTQGAEEVLRAHEEQLKEAQAVPA----------------TLPELEATKASLKKLRAQAEAQQPM-------FDALrdE 1289
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqladvkTICEQEARIKDLEAQRAQLQAGQPCplcgstsHPAV--E 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1290 LRGAQEVGERlQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARQRQEQ 1369
Cdd:PRK10246 519 AYQALEPGVN-QSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDD 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1370 IQamPLADSQAVRE----QLRQEKALLEEIERHGEKVEEcqrfakqyinaikdYELQLVTYKAQLEPVASPAKKPKVQSG 1445
Cdd:PRK10246 598 IQ--PWLDAQEEHErqlrLLSQRHELQGQIAAHNQQIIQ--------------YQQQIEQRQQQLLTALAGYALTLPQED 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1446 SESviqeyvdlrtrySELTTltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1525
Cdd:PRK10246 662 EEA------------SWLAT----------------RQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEET 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1526 EAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1605
Cdd:PRK10246 714 VALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1606 GGAegelQALRAQAEEAEAQKRQAQEE-------AERLRRQVQDESQRKRQ---AEAELALRVKAEAEAAREKQRALQAL 1675
Cdd:PRK10246 794 QQA----QTLVTQTAQALAQHQQHRPDgldltvtVEQIQQELAQLAQQLREnttRQGEIRQQLKQDADNRQQQQALMQQI 869
|
....*....
gi 1820553714 1676 EELRLQAEE 1684
Cdd:PRK10246 870 AQATQQVED 878
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2415-2756 |
1.38e-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: 48.43 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2415 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2494
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2495 AEETQGFQRTLEAERQRQL-EMSAEAERLKLR---MAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQT 2570
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKqEIEKEEEKLAQVlkeNKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2571 LEIQRQQSDHDAERLREAIAELEREKeKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEK 2650
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2651 AKLEQLFQdEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEgvRRKQEELQQLEQQRRQQEELLAEENQR 2730
Cdd:pfam02463 398 ELKSEEEK-EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT--EEKEELEKQELKLLKDELELKKSEDLL 474
|
330 340
....*....|....*....|....*.
gi 1820553714 2731 LREQLQRLEEQHRAALAHSEEVTALQ 2756
Cdd:pfam02463 475 KETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1515-2003 |
1.39e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1515 AHAQAKAQAEREAKELQQR------MQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERsrlr 1586
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAkaaktpAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDnfPKLSAELRQQLNNER---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1587 ieEEIRVVRLQLEAterqrggAEGELQALRAQAEEAEaQKRQAQEEAERLRRQVQDESQ-RKRQAEAELALrvkAEAEaa 1665
Cdd:PRK10929 93 --DEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAREISDSLSQlPQQQTEARRQL---NEIE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1666 rekqRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSA--EAELQSKRASFAEK-TAQLERSLQEEHvavAQ 1742
Cdd:PRK10929 158 ----RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQALR---NQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1743 LREEAerraqqqaeaerareeaerelerwQLKANEAL-RLRLQAEEVAQ-QKSLAqaeaekqkeeaerearrrgkaeEQA 1820
Cdd:PRK10929 231 LNSQR------------------------QREAERALeSTELLAEQSGDlPKSIV----------------------AQF 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1821 VRHRELAeQELEKQRQ-LAEGTAQQRLAAEQELIRLRAETEQGEQQRQL-----LEEELaRLQHEAAAATQKRQELEAEL 1894
Cdd:PRK10929 265 KINRELS-QALNQQAQrMDLIASQQRQAASQTLQVRQALNTLREQSQWLgvsnaLGEAL-RAQVARLPEMPKPQQLDTEM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1895 AKVRAemevllaskaraeeesrstsekskQRLeaeagRFRELAEEAARLRALAEE-----AKRQRQLAEEDAARQRAEAE 1969
Cdd:PRK10929 343 AQLRV------------------------QRL-----RYEDLLNKQPQLRQIRQAdgqplTAEQNRILDAQLRTQRELLN 393
|
490 500 510
....*....|....*....|....*....|....*...
gi 1820553714 1970 RVLAEKLAAISEATRLK---TEAEIALKE-KEAENERL 2003
Cdd:PRK10929 394 SLLSGGDTLILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1493-1735 |
1.41e-04 |
|
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: 46.53 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1493 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLRQSSEAEIQA 1572
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1573 KARqaeaaersrlrieeeirvvRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEA 1652
Cdd:pfam12795 74 ILA-------------------SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1653 ELALRVKAEAEAAREKQRALQA--------LEELRLQAEEAERR--LRQAEVERARQVQVALETAQRSAEAELQSKRASF 1722
Cdd:pfam12795 135 RLNGPAPPGEPLSEAQRWALQAelaalkaqIDMLEQELLSNNNRqdLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQE 214
|
250
....*....|....
gi 1820553714 1723 AEKT-AQLERSLQE 1735
Cdd:pfam12795 215 AEQAvAQTEQLAEE 228
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1478-1642 |
1.45e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.22 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1478 LRRMEEEERLAEQQRAEERERLAEVEAA--LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1555
Cdd:pfam00038 136 LKKNHEEEVRELQAQVSDTQVNVEMDAArkLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1556 QEELQQLR---QSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqRGgaEGELQALRAQAEEAEAQKRQAQEE 1632
Cdd:pfam00038 216 KEEITELRrtiQSLEIELQSLKKQKASLERQLAETEE---------------RY--ELQLADYQELISELEAELQETRQE 278
|
170
....*....|
gi 1820553714 1633 AERLRRQVQD 1642
Cdd:pfam00038 279 MARQLREYQE 288
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1485-1736 |
1.51e-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: 48.28 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1485 ERLAEQQRAEERERLAEVEaalekqrqlaeahaqakaQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQE---E 1558
Cdd:pfam10174 453 ERLKEQREREDRERLEELE------------------SLKKENKDLKEKvsaLQPELTEKESSLIDLKEHASSLASsglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1559 LQQLRQSSEAEIQA-------------KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQ 1625
Cdd:pfam10174 515 KDSKLKSLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1626 K---------------RQAQEEAERLR--RQVQDESQRKRQAEAELALRVK-AEAEAAREKQRA--LQALEELRLQAEEA 1685
Cdd:pfam10174 595 KndkdkkiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDAT 674
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1686 ERRLRQAEV--------------ERARQVQVALETAQRSAEAELQSKRASFA--EKTAQLERSLQEE 1736
Cdd:pfam10174 675 KARLSSTQQslaekdghltnlraERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE 741
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1839-2188 |
1.53e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.98 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1839 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1918
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1919 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA 1998
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1999 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGK 2078
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2079 AELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2158
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350
....*....|....*....|....*....|
gi 1820553714 2159 RRLRERAEQESARQLQLAQEAAQKRLQAEE 2188
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAE 462
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2353-2778 |
1.66e-04 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 48.07 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2353 ATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQ 2432
Cdd:COG5281 2 AALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2433 LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2512
Cdd:COG5281 82 AALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAA--AAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2513 LEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAEL 2592
Cdd:COG5281 160 AAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2593 EREKEKLQQEAKLLQLKSEEmQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQ 2672
Cdd:COG5281 240 ASAAAQALAALAAAAAAAAL-ALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2673 RQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQR--LEEQHRAALAHSE 2750
Cdd:COG5281 319 AAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAgaKAALAEYADSATN 398
|
410 420
....*....|....*....|....*...
gi 1820553714 2751 EVTALQVAATKTLPNGRDALDGPATEAE 2778
Cdd:COG5281 399 VAAQVAQAATSAFSGLTDALAGAVTTGK 426
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1832-2314 |
1.69e-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: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1832 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAA--AATQKRQELEAELAKVRAEM--EVLLAS 1907
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeEAREAKAEAEQRAAELAAEAakKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1908 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRqrqlaEEDAARQRAEAERVLAEKLAAISEATRLKT 1987
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRK-----AEEEAKRKAEEERKAAEAEAAAKAEAEAAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1988 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILAL 2067
Cdd:COG3064 159 AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2068 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE 2147
Cdd:COG3064 239 ATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2148 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAA 2227
Cdd:COG3064 319 AAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2228 EEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKH 2307
Cdd:COG3064 399 GLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
....*..
gi 1820553714 2308 KKFAEQT 2314
Cdd:COG3064 479 DLLLLGG 485
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4412-4445 |
1.70e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....
gi 1820553714 4412 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4445
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1485-1649 |
1.72e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.98 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1485 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQ 1564
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1565 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGaEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDES 1644
Cdd:PRK12678 158 ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
....*
gi 1820553714 1645 QRKRQ 1649
Cdd:PRK12678 237 DARGD 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1451-1791 |
1.73e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1451 QEYVDLRTRYSELTT---LTSQYIKFISETLRRMEEEERLAE-QQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAER 1525
Cdd:COG4717 102 EELEELEAELEELREeleKLEKLLQLLPLYQELEALEAELAElPERLEElEERLEELRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1526 EAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQ-------- 1597
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAALEERLKEARlllliaaa 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1598 ----------LEATERQRGGA----EGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1663
Cdd:COG4717 258 llallglggsLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1664 AAREKQRALQALEELRLQAEEAERRLRQAEVERARQV----------------------QVALETAQRSAEAELQSKRAS 1721
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaeeYQELKEELEELEEQLEELLGE 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1722 FAE-----KTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKAnEALRLRLQAEEVAQQ 1791
Cdd:COG4717 418 LEEllealDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ-ELEELKAELRELAEE 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2239-2655 |
1.75e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2239 REAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAAlrqkQAAdaemEKHKKFAEQTLRQK 2318
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDY----QAA----SDHLNLVQTALRQQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2319 AQVE---QELTTLRLQLEETDHQKNLLDEELQRLKAEATEAarqrsqvEEELFSVRVQMEELSKlkARIEAENRAL---- 2391
Cdd:COG3096 347 EKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAA-------EEEVDSLKSQLADYQQ--ALDVQQTRAIqyqq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2392 ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQlaeeDLAQQRALAEKMLKEKMQAVQEATRLKAEAELlQQ 2471
Cdd:COG3096 418 AVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVL----ELEQKLSVADAARRQFEKAYELVCKIAGEVER-SQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2472 QKELAQEQARRLQEDK------EQMAQQLAEETQGFQRTLEAERQRQlEMSAEAERLKLRMAEMSRAQARAEEDAQRFRK 2545
Cdd:COG3096 493 AWQTARELLRRYRSQQalaqrlQQLRAQLAELEQRLRQQQNAERLLE-EFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2546 QAEEIGEKlhRTELATQEkvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQET 2625
Cdd:COG3096 572 QAAEAVEQ--RSELRQQL-----EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATV 644
|
410 420 430
....*....|....*....|....*....|
gi 1820553714 2626 qalqqsflsEKDSLLQRERFIEQEKAKLEQ 2655
Cdd:COG3096 645 ---------ERDELAARKQALESQIERLSQ 665
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2288-2520 |
1.82e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2288 QAEQAALRQKQAADAEmekhkKFAEQtlrQKAQVEQELTTLRLQLEETDHQKNL--LDEELQRLKAEATEAARQRSQVEE 2365
Cdd:COG3206 162 LEQNLELRREEARKAL-----EFLEE---QLPELRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2366 ELFSVRVQMEELSKLKARIEAENRALIlrDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALA 2445
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2446 EKMLKEkmqAVQEATRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAE 2520
Cdd:COG3206 312 QRILAS---LEAELEALQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2279-2741 |
1.84e-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: 48.19 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2279 AEQEAVRRAQAEQAALRQKQAAD---------AEMEKHKKFAEQTL----RQKAQVEQELTTLRLQLEETDHQKNLLDEE 2345
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDlestvsqlrSELREAKRMYEDKIeeleKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2346 LQRLKAEATEAARQRSQVEEE--------------LFSVRVQMEELSKLKARIEAENRALILRDKDNTQR---FLQEEAE 2408
Cdd:pfam15921 379 LQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmaAIQGKNE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2409 KMKQVAEEAARLSVAAQeaaRLRQLAEEDLAQQRALAEK---------MLKEKMQAVQ----EATRLKAEAEL-LQQQKE 2474
Cdd:pfam15921 459 SLEKVSSLTAQLESTKE---MLRKVVEELTAKKMTLESSertvsdltaSLQEKERAIEatnaEITKLRSRVDLkLQELQH 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2475 LAQE--QARRLQEDKEQMAQQLAEEtqgfQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2552
Cdd:pfam15921 536 LKNEgdHLRNVQTECEALKLQMAEK----DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2553 KLHRTELATQEKVTLVQTLEIQR-QQSDHDAERLReAIAELEREKEKLQQEAKL------------------LQLKSEEM 2613
Cdd:pfam15921 612 LKDKKDAKIRELEARVSDLELEKvKLVNAGSERLR-AVKDIKQERDQLLNEVKTsrnelnslsedyevlkrnFRNKSEEM 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2614 QTVQQEQLLQETQAlqQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQqqqmeqerqrlVASMEEAR 2693
Cdd:pfam15921 691 ETTTNKLKMQLKSA--QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK-----------IQFLEEAM 757
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820553714 2694 QRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQRLEEQ 2741
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3821-3857 |
1.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 3821 HYLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 3857
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1818-2013 |
1.99e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1894
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1895 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1959
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1960 DAARQRAEAERVLAEKLAAIS-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 2013
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
318-395 |
2.02e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 43.45 E-value: 2.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 318 DNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 395
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1101-1526 |
2.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1101 HYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRITEQQKAQAEVEGL 1173
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1174 GKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLR------AHEE 1247
Cdd:COG4717 169 EAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEneleaaALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1248 QLKEAQAVPATLPELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQA 1327
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1328 VLAQTDVRQREleqlgrQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVREQLRQEKAL--LEEIERHGEKVEEC 1405
Cdd:COG4717 324 LLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVedEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1406 QrfakQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEyvdLRTRYSELTTLTSQYIKFISEtLRRMEEEE 1485
Cdd:COG4717 398 Q----ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE---LEELEEELEELREELAELEAE-LEQLEEDG 469
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1820553714 1486 RLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE 1526
Cdd:COG4717 470 ELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1455-1790 |
2.25e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1455 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAKELQQRM 1534
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1535 QEEVVRREEAAvDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQA 1614
Cdd:COG4372 94 AELAQAQEELE-SLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1615 LRAQAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1694
Cdd:COG4372 169 LEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1695 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1774
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|....*.
gi 1820553714 1775 ANEALRLRLQAEEVAQ 1790
Cdd:COG4372 327 KLELALAILLAELADL 342
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3268-3304 |
2.28e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.28e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 3268 LRLLDAQLSTGGVVDPSKSHHVPLDVAYARGCLDEET 3304
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1563-1716 |
2.40e-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: 46.65 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1563 RQSSEAEIQAKARQAEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERlRRQV 1640
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1641 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQ 1716
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3562-3593 |
2.86e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.86e-04
10 20 30
....*....|....*....|....*....|..
gi 1820553714 3562 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 3593
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1818-2099 |
2.92e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1897
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1898 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1977
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1978 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 2057
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1820553714 2058 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSK 2099
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1815-2008 |
2.92e-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: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1894
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1895 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1974
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 1820553714 1975 KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 2008
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1239-1955 |
3.01e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.05 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1239 EEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqpmfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1317
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1318 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplgAWLQDARQRQEQIQAMPLADSQavrEQLRQEKALLEEIER 1397
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE----AKQLAEAQKEAELLRKQLSKTQ---EELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1398 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTSQY 1470
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1471 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKeLQQRMQEEvvrreeaAVDAQ 1549
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDK-------AAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1550 QQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQA 1629
Cdd:pfam07111 370 VERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1630 QEEAER--LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEEL--RLQAEEAERRLRQAEVERARQVQVAle 1705
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVA-- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1706 taqRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1785
Cdd:pfam07111 527 ---QQLEQELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1786 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1860
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1861 QGEQQR-----QLLEEE----LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1926
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 1820553714 1927 EAEAGRFRELAEEAARLRALAEEAKRQRQ 1955
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2309-2476 |
3.20e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.38 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2309 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKNLLDEElqrlkAEATEAARQRSQVEEELFSVRVQMEELSKlkarieaen 2388
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALRS--------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2389 ralILRDKDNTQRFLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2466
Cdd:COG3524 243 ---YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 1820553714 2467 EllQQQKELA 2476
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1664-1976 |
3.39e-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: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1664 AAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASfAEKTAQLERSLQEEHVAVAQL 1743
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEERE-QKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1744 REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRH 1823
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1824 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAatQKRQELEAELAKVRAEMEV 1903
Cdd:pfam13868 188 RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE--LKERRLAEEAEREEEEFER 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1904 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKL 1976
Cdd:pfam13868 266 MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1476-1671 |
3.40e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.24 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEER---LAEQQRAEererlaeveaaLEKQRQLAEAHAQAKAQAEREAKELQQRMQ----------EEVVRRE 1542
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE-----------LDASRALAEKQKHELDTEKRCAEELKEAMQmamegharmlEQYADLE 1120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1543 EAAVDAQQQKRSIQEELQQLRQsseAEIQAKARQAE-------AAERSRLRI--EEEIRVVRLQLEATERQ-RGGAE--- 1609
Cdd:PLN03188 1121 EKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVerEKERRYLRDENKSLQAQlRDTAEavq 1197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 1610 --GELQALRAQAEEA--EAQKR--QAQEEAERLRRQVqDESQRKRQAEAELALRVKAEAEAAREKQRA 1671
Cdd:PLN03188 1198 aaGELLVRLKEAEEAltVAQKRamDAEQEAAEAYKQI-DKLKRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2482-2811 |
3.44e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2482 RLQEDKEQMAQQLAEETQGFQRT--LEAERQRQLE-MSAEAERlklrmAEMSRAQARAEEDAQR--FRKQAEEIGEKLHR 2556
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLedILNELERQLKsLERQAEK-----AERYKELKAELRELELalLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2557 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEK 2636
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2637 DSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRkqeelqqleqQ 2716
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----------L 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2717 RRQQEELLAEEN------QRLREQLQRLEEQHRAALAHSEEV-TALQVAATKTLPNGRDALDgpATEAEPEHSFDGLRQK 2789
Cdd:TIGR02168 385 RSKVAQLELQIAslnneiERLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEELE--EELEELQEELERLEEA 462
|
330 340
....*....|....*....|....*..
gi 1820553714 2790 VPAQRLQEAGILSA-----EELQRLAQ 2811
Cdd:TIGR02168 463 LEELREELEEAEQAldaaeRELAQLQA 489
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1530-2163 |
3.58e-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: 47.02 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1530 LQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1609
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1610 gELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElaLRVKAEaeaarekqralQALEELRLQAEEAERRL 1689
Cdd:pfam05483 159 -LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1690 RQAEVERARQV-----QVALETAQrSAEAELQSKRASFAektaqlersLQEEHVAVAQLREEAERRAQQQAEAERAREEA 1764
Cdd:pfam05483 225 QHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTFL---------LEESRDKANQLEEKTKLQDENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1765 ERELERwqlkaneaLRLRLQaEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRHRELAEQELEKQR---QLAEGT 1841
Cdd:pfam05483 295 TKELED--------IKMSLQ-RSMSTQKALEEDLQIAT------------KTICQLTEEKEAQMEELNKAKaahSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1842 AQQRLAAEQELIRLRAET-EQGEQQRQLLEEELARLQHEAAAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESR 1916
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRlEKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1917 STSEKSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLkteaeialkek 1996
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL----------- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1997 eaENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGL--VEDTLRQRR--------QVEEEILA 2066
Cdd:pfam05483 500 --ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARS 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2067 LKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKsLAAEEEAARQR----- 2141
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfeeii 656
|
650 660 670
....*....|....*....|....*....|....*.
gi 1820553714 2142 --------------KAALEEVERLKAKVEEARRLRE 2163
Cdd:pfam05483 657 dnyqkeiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2344-2552 |
3.76e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2344 EELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKM-----KQVAEEAA 2418
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2419 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLA 2495
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2496 EETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2552
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1522-1684 |
3.77e-04 |
|
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: 45.74 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1522 QAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQ-AKARQAEAAERSRLRIEEEirvVRLQLEA 1600
Cdd:pfam12037 59 QAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDElARKRYQDQLEAQRRRNEEL---LRKQEES 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1601 TERQrggaegelQALRAQAeeaeaQKRQAQEEAERLRRQVqdesqrkrqaeaeLALRVKAEAE--AAREKQRALQALEEL 1678
Cdd:pfam12037 136 VAKQ--------EAMRIQA-----QRRQTEEHEAELRRET-------------ERAKAEAEAEarAKEERENEDLNLEQL 189
|
....*.
gi 1820553714 1679 RLQAEE 1684
Cdd:pfam12037 190 REKANE 195
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2132-2644 |
3.77e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.16 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2132 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQS 2211
Cdd:COG3899 738 DPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2212 VLDRlRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAeklrkDAEQEAVRRAQAEQ 2291
Cdd:COG3899 818 ALAE-RLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAA-----AAAAAAAALAAAAA 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2292 AALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR 2371
Cdd:COG3899 892 AAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAA 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2372 VQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2451
Cdd:COG3899 972 LAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAA 1051
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2452 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSR 2531
Cdd:COG3899 1052 AAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARA 1131
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2532 AQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSE 2611
Cdd:COG3899 1132 AAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLA 1211
|
490 500 510
....*....|....*....|....*....|...
gi 1820553714 2612 EMQTVQQEQLLQETQALQQSFLSEKDSLLQRER 2644
Cdd:COG3899 1212 LALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2343-2563 |
3.98e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2343 DEELQRLKAEATEAARQRSQveEELfsVRVQMEELSKLKARIEAENRALILRDKDNTqrflqEEAEKMKQVAEEAARLSV 2422
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEAR--KRL--VAKHGAEISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2423 AAQEAARLRQLAEEDLAQQRALAekmlkekmqavqeATRLKAEAELLQQQKELAQEQARrlQEDKEQMAQQLAEETQGfq 2502
Cdd:PRK07735 75 AKQKREGTEEVTEEEKAKAKAKA-------------AAAAKAKAAALAKQKREGTEEVT--EEEKAAAKAKAAAAAKA-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2503 RTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2563
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE 198
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1906-2192 |
4.01e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.67 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1906 ASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRL 1985
Cdd:pfam09731 101 VAEEEKEATKDAAEAKAQLPKSEQE---KEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1986 KTEAEIALKEKEAENERLRRLAEDeafQRRRLEEQAAQHKADIEERLAQLRKASDSELE-----RQKGLVEDTLRQRRQV 2060
Cdd:pfam09731 178 EKATDSALQKAEALAEKLKEVINL---AKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEkvekaQSLAKLVDQYKELVAS 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2061 EEEILA--LKASFEKAAAGKAELELelgrIRSNAEDTLRSKEQAELEAArQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2138
Cdd:pfam09731 255 ERIVFQqeLVSIFPDIIPVLKEDNL----LSNDDLNSLIAHAHREIDQL-SKKLAELKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2139 RQRKAALEEV-----ERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2192
Cdd:pfam09731 330 EELSARLEEVraadeAQLRLEFEREReEIRESYEEKLRTELERQAEAHEEHLKDVLVEQE 389
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2296-2496 |
4.03e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2296 QKQAADAEMEKHKKFAEQT--LRQKAQVEQElttlRLQLEEtdhQKNLLDEELQRLKAEATEAARQRSQVEEElfsVRVQ 2373
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLE---KERLAAQEQKKQAEEAAKQAALKQKQAEE---AAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2374 MEELSKLKAriEAENRALilrdkdntqrflqeeAEKMKQVAEEAARLSVAAQEAarlrQLAEEdlAQQRALAEkmlkEKM 2453
Cdd:PRK09510 141 AAAAAKAKA--EAEAKRA---------------AAAAKKAAAEAKKKAEAEAAK----KAAAE--AKKKAEAE----AAA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1820553714 2454 QAVQEAtRLKAEAELLQQQKELAQEQARRlqEDKEQMAQQLAE 2496
Cdd:PRK09510 194 KAAAEA-KKKAEAEAKKKAAAEAKKKAAA--EAKAAAAKAAAE 233
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1739-2194 |
4.09e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.93 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1739 AVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1818
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1819 QAVRHRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVR 1898
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1899 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1978
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1979 ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRR 2058
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2059 QVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2138
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2139 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2194
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1488-1602 |
4.13e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1488 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ-AKAQAERE-AKELQQRM----------QEEVVRREEAAVDAQQQKRSI 1555
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlAAAQAQLDlAQRELERYqalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1820553714 1556 QEELQQLRQSSEAEIQAKARQAEAAErsrlrIEEEIRVVRLQLEATE 1602
Cdd:COG1566 168 QAQLAQAQAGLREEEELAAAQAQVAQ-----AEAALAQAELNLARTT 209
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1494-1724 |
4.18e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1494 EERERLAEVEAAL-------EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS 1566
Cdd:pfam13868 3 ENSDELRELNSKLlaakcnkERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1567 EAEIQAKARQAEAAERSRLRIEEEIRVV----RLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQD 1642
Cdd:pfam13868 83 EEREQKRQEEYEEKLQEREQMDEIVERIqeedQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1643 ESQRKRQAEAELALRVKAEAEAAREKQRALQALEE----------LRLQAEEAERRLRQAEVERARQVQVALETAQRSAE 1712
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQdekaerdelrAKLYQEEQERKERQKEREEAEKKARQRQELQQARE 242
|
250
....*....|..
gi 1820553714 1713 AELQSKRASFAE 1724
Cdd:pfam13868 243 EQIELKERRLAE 254
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1496-1605 |
4.33e-04 |
|
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: 45.74 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1496 RERLAEVEAALEKQRQLAEAH-AQAKAQAEREAKELQQRMQEEVVRREEAavDAQQQKRSIQEELQQLRQSSEAEIQAKA 1574
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEkAIEAERAKAEAAEAEQELLREKQKEEEQ--MMEAQERSYQEHVKQLIEKMEAEREQLL 260
|
90 100 110
....*....|....*....|....*....|.
gi 1820553714 1575 RQAEAAERSRLRIEEEIRVVRLQLEATERQR 1605
Cdd:pfam02841 261 AEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2866-2899 |
4.36e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.36e-04
10 20 30
....*....|....*....|....*....|....
gi 1820553714 2866 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2899
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1482-1730 |
4.48e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1482 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAK-------ELQQRMQEEVVRREEAAVDAQQQKRS 1554
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgqgglDEEEAFLDRTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1555 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEI--RVVRLQLEATE-RQRGGAEGELQALRAQAEEAEAQKRQAQE 1631
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1632 EAERLRRQV-QDESQRKRQAEAELALRVKA------------EAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1698
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESkvfldqkrghpeVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 1820553714 1699 QVQVALETAQRS----AEAELQSKRASFAEKTAQLE 1730
Cdd:pfam02029 245 EAEQKLEELRRRrqekESEEFEKLRQKQQEAELELE 280
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2288-2502 |
4.68e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2288 QAEQAALRQKQAADAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRS--- 2361
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2362 ---QVEEELFSVRVQMEELSklKARIEAENRALILRDK---------DNTQRfLQEEAEKMKQVAEEAARLSVAAQEAAR 2429
Cdd:PRK11281 122 slrQLESRLAQTLDQLQNAQ--NDLAEYNSQLVSLQTQperaqaalyANSQR-LQQIRNLLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2430 LRQLAeedLAQQRALAEKMLK--EKMQAVQEATR--LKAEAELLQQQKELAQE--QARRLQEDKEQMAQ-QLAEETQGFQ 2502
Cdd:PRK11281 199 AEQAL---LNAQNDLQRKSLEgnTQLQDLLQKQRdyLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQEaQSQDEAARIQ 275
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1832-2107 |
4.78e-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: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1832 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQL-----LEEELARLqheaaaaTQKRQELEAELAKVRAEMEV 1903
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQYdsnrrLGERIQDI-------TFWKSELEKELEELDEEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1904 LLASKARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAAR 1963
Cdd:pfam03148 76 LLEEKRRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1964 QRAEAErvLAEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLR 2036
Cdd:pfam03148 154 HKLEKD--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSIL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2037 KASDSELERQKGLVEDTLRQRrqVEEeilalkasFEKAaagKAELELELGRIRSNAEDTlrSKEQAELEAA 2107
Cdd:pfam03148 232 EQTANDLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEL--EKNIEALEKA 287
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1565-1699 |
4.85e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1565 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERlRRQVQDES 1644
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1645 QRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1699
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3487-3521 |
4.87e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.39 E-value: 4.87e-04
10 20 30
....*....|....*....|....*....|....*
gi 1820553714 3487 LLQGSGCLAGIYLEDSKEKVSIYEAMRRGLLRPST 3521
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1473-1535 |
4.92e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.79 E-value: 4.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1473 FISETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAEREAKELQQRMQ 1535
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1612-1736 |
5.43e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1612 LQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEaarekQRALQALEELRLQAEEAERRLRQ 1691
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1820553714 1692 AEVERARQVqvaletaqrsAEAELQSKRASFAEKTAQLERSLQEE 1736
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3897-3933 |
5.57e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.57e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1820553714 3897 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 3933
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2421-2597 |
5.62e-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: 46.10 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2421 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQaVQEATRLKAEAELLQQQKelaQEQARRLQEDKEQMAQQLAEETQG 2500
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMRRLE-VERKRREQEEQRRLQQEQ---LERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2501 FQRTLEAERQRQ--------LEMSAEAERLKLRMAEMSR------------AQARAEEDAQRFRKQAEEIGEKLHR-TEL 2559
Cdd:pfam15709 392 RKQRLEEERQRQeeeerkqrLQLQAAQERARQQQEEFRRklqelqrkkqqeEAERAEAEKQRQKELEMQLAEEQKRlMEM 471
|
170 180 190
....*....|....*....|....*....|....*...
gi 1820553714 2560 ATQEKvtlvqtLEIQRQQSDHDAERLREAIAELEREKE 2597
Cdd:pfam15709 472 AEEER------LEYQRQKQEAEEKARLEAEERRQKEEE 503
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1586-1720 |
5.74e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1586 RIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1665
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1666 REKQRalQALEELRLQAEEAERRLRQAE--VERARQVQVALETAQRSAEAELQSKRA 1720
Cdd:COG1842 100 AEALE--AQLAQLEEQVEKLKEALRQLEskLEELKAKKDTLKARAKAAKAQEKVNEA 154
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2339-2810 |
5.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2339 KNLLDEELQRLKAEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENRALIlrdkdntqrflqEEAEKMKQVAEEAA 2418
Cdd:PRK04863 260 KHLITESTNYVAADYMRHANERRVHLEEALELR---RELYTSRRQLAAEQYRLV------------EMARELAELNEAES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2419 RLSVAAQEAARLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLAE 2496
Cdd:PRK04863 325 DLEQDYQAASDHLNLVQTALRQQEKIerYQADLEELEERLEEQNEVVEEA---DEQQEENEARAEAAEEEVDELKSQLAD 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2497 ETQGF--QRTLEAERQRQLEMSAEAERLklrMAEMSRAQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVQTLeiq 2574
Cdd:PRK04863 402 YQQALdvQQTRAIQYQQAVQALERAKQL---CGLPDLTADNAEDWLEEFQAKEQEATEEL----LSLEQKLSVAQAA--- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2575 RQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSllqrERFIEQEKAKLE 2654
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA----ERLLAEFCKRLG 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2655 QLFQDEvakaqqlrEEQQRQQQQMEQERQRLVASMEEARQRQheaeEGVRRKQeelqqleqqrrqqeellaeenQRLREQ 2734
Cdd:PRK04863 548 KNLDDE--------DELEQLQEELEARLESLSESVSEARERR----MALRQQL---------------------EQLQAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2735 LQRLEEQHRAALAHSEEVTALQVAATKTLPNGRDALDGPATEAEPEHSFDGLRQKVPAQ---------RLQEAGILSAEE 2805
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARkqaldeeieRLSQPGGSEDPR 674
|
....*
gi 1820553714 2806 LQRLA 2810
Cdd:PRK04863 675 LNALA 679
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1608-1717 |
6.03e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1608 AEGELQALRAQAE-EAEAQKR----QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEElRLQA 1682
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE-ELEK 114
|
90 100 110
....*....|....*....|....*....|....*
gi 1820553714 1683 EEAERRLRQAEVERARQVqvaLETAQRSAEAELQS 1717
Cdd:PRK12704 115 KEKELEQKQQELEKKEEE---LEELIEEQLQELER 146
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1473-1689 |
6.63e-04 |
|
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: 44.29 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1473 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAKELQQRMQEEVVRREEAAVDAQQQ- 1551
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRLEQQTEQAKKLEEKAQAALTKGNEEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1552 KRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQE 1631
Cdd:pfam04012 85 AREALAEKKSLEKQAEALETQLAQQRSAVEQ-----------LRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 1632 EAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQaLEELRLQAEEAERRL 1689
Cdd:pfam04012 154 LGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1805-1982 |
6.64e-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: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1805 EAerearrrgkaeEQAVRHRELAEQELEKQRQLAEgtaqqrlaaeqelIRLRAETEQGEQQRQLLEEElarlqheaaaaT 1884
Cdd:COG2268 229 EQ-----------EREIETARIAEAEAELAKKKAE-------------ERREAETARAEAEAAYEIAE-----------A 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1885 QKRQELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ----RQLAEED 1960
Cdd:COG2268 274 NAEREVQRQLEIAEREREIELQEKEAEREEAE---LEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEaegkRALAEAW 350
|
170 180
....*....|....*....|..
gi 1820553714 1961 AARQRAEAERVLAEKLAAISEA 1982
Cdd:COG2268 351 NKLGDAAILLMLIEKLPEIAEA 372
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3194-3228 |
6.65e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 6.65e-04
10 20 30
....*....|....*....|....*....|....*
gi 1820553714 3194 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 3228
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2275-2480 |
6.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2275 LRKDAEQEAvrrAQAEQAALRQKQAADAEMEKHKKFAEQtlrqkaQVEQELTTLRLQLEETDHQKNlldEELQRLKaeat 2354
Cdd:PRK12704 25 RKKIAEAKI---KEAEEEAKRILEEAKKEAEAIKKEALL------EAKEEIHKLRNEFEKELRERR---NELQKLE---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2355 eaarQRSQVEEElfSVRVQMEELSKLKARIEAENRAL--ILRDKDNTQRFLQEEAEKMKQVAEEAARLSvaAQEA-ARLR 2431
Cdd:PRK12704 89 ----KRLLQKEE--NLDRKLELLEKREEELEKKEKELeqKQQELEKKEEELEELIEEQLQELERISGLT--AEEAkEILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2432 QLAEEDLAQQRAlaeKMLKE-KMQAVQEATRlKAEAELLQQQKELAQEQA 2480
Cdd:PRK12704 161 EKVEEEARHEAA---VLIKEiEEEAKEEADK-KAKEILAQAIQRCAADHV 206
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1546-1692 |
7.25e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1546 VDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvvrlqleaterqrggAEGELQALRAQAEEAEAQ 1625
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1626 KRQAQEEAERLRRQVQdesqrkrQAEAElalrvkaeaEAAREKQRALQALEELRLqaEEAERR------LRQA 1692
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1769-2252 |
7.41e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1769 ERWQLKANEALRLRLQAEEVAQQKSLAQ--AEAEKQKEEAERearrrgKAEEQAVRHRELAEQELEKQRQLAEGTAQQRL 1846
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKriRLLEKREAEAEE------ALREQAELNRLKKKYLEALNKKLNEKESQLAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1847 A--------------------AEQELIRLRAETEQGEQQRQLLE----------EELARLQHEAAAATQKRQELEAELAK 1896
Cdd:pfam05557 102 ArevisclknelselrrqiqrAELELQSTNSELEELQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1897 VRAEMEVLLASKarAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLA 1973
Cdd:pfam05557 182 QEQDSEIVKNSK--SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1974 E----KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASDSE---LERQ 2046
Cdd:pfam05557 260 ElqswVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2047 KGLVEDTLRQRRQVEEEILALKA---SFEKAAAGKAELELELGRIRSNAEDTLRSKEQ-AELEAARQRQLAAEEEQRRRE 2122
Cdd:pfam05557 338 KALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAEDMTQKMQAHnEEMEAQLSVAEEELGGYKQQA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2123 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQEAAQKR---LQAEEKAHAF 2193
Cdd:pfam05557 418 QTLERELQALRQQESLADPSYSKEEVDSLRRKLETLElerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAE 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2194 AVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAE 2252
Cdd:pfam05557 498 AYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2428-2603 |
7.50e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.76 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2428 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLAEETQG 2500
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2501 FQRTLEAERQRQLemsaeAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2580
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 1820553714 2581 DAERLREAIAELEREKEKLQQEA 2603
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2305-2538 |
7.75e-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: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2305 EKHKKFAEQTLrqkAQVEQELTTLRLQLE-----ETDHQKNLLDEELQRLKAEATEAAR-QRSQVEEElfsVRVQMEELS 2378
Cdd:COG2268 147 EDREKFAEKVQ---EVAGTDLAKNGLELEsvaitDLEDENNYLDALGRRKIAEIIRDARiAEAEAERE---TEIAIAQAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2379 KLKARIEAENRALIL--------RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlK 2450
Cdd:COG2268 221 REAEEAELEQEREIEtariaeaeAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-A 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2451 EKMQAVQEAT-RLKAEAEllqQQKELAQEQArrlqeDKEQMAQQLAEETQGFQRTLEAERqrqlEMSAEAERLKL--RMA 2527
Cdd:COG2268 300 EREEAELEADvRKPAEAE---KQAAEAEAEA-----EAEAIRAKGLAEAEGKRALAEAWN----KLGDAAILLMLieKLP 367
|
250
....*....|.
gi 1820553714 2528 EMSRAQARAEE 2538
Cdd:COG2268 368 EIAEAAAKPLE 378
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1476-1580 |
7.86e-04 |
|
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: 44.31 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQ-------AEREAKELQQRMQEEVVRREEA-- 1544
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKqkaaesaSKSLAKPERKVSQEEAKEVLQEwe 148
|
90 100 110
....*....|....*....|....*....|....*..
gi 1820553714 1545 -AVDAQQQKRsiQEELQQLRQSSEAEIQAKARQAEAA 1580
Cdd:pfam13904 149 rKKLEQQQRK--REEEQREQLKKEEEEQERKQLAEKA 183
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1497-1668 |
8.13e-04 |
|
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: 43.41 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1497 ERLAEVEAALEK-QRQLAEAHAQAKAQAEREAKELQQRMQ---EEVVRREEAAVDAQQQKrsIQEELQQLRQsseaeiQA 1572
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQkdlEEVRAKLEPYLEELQAK--LGQNVEELRQ------RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1573 KARQAEAAERSRLRIEEEIRVVRlqlEATERQRGGAEGELQALRAQAEEAEAQKRQ-----AQEEAERLRRQVQDESQRK 1647
Cdd:pfam01442 76 EPYTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPYAEELRQklaerLEELKESLAPYAEEVQAQL 152
|
170 180
....*....|....*....|.
gi 1820553714 1648 RQAEAELALRVKAEAEAAREK 1668
Cdd:pfam01442 153 SQRLQELREKLEPQAEDLREK 173
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1937-2310 |
8.36e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1937 AEEAARLRALAEEAKRQRQLAEEDAARQraEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDeafQRRR 2016
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQ--VTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREER---RQKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2017 LEEQAAQHK------ADIEERLAQlrKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRS 2090
Cdd:pfam02029 79 LQEALERQKefdptiADEKESVAE--RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2091 NAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2170
Cdd:pfam02029 157 EEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2171 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRseaevarraaeeAEEARVQAEREAAQSRRQVEE 2250
Cdd:pfam02029 237 EEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELK------------KKREERRKLLEEEEQRRKQEE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2251 AERlkqlaeeqaqaraqaqaaaeKLRKDAE----QEAVRRAQAEQAALRQKQAADAEMEKHKKF 2310
Cdd:pfam02029 305 AER--------------------KLREEEEkrrmKEEIERRRAEAAEKRQKLPEDSSSEGKKPF 348
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1815-1974 |
8.59e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.05 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEA 1892
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1893 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1968
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....*.
gi 1820553714 1969 ERVLAE 1974
Cdd:COG1842 207 EDELAA 212
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1512-1718 |
8.82e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.23 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1512 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKarqaeaaersrlrieeei 1591
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1592 rvvrlQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeaarekQRA 1671
Cdd:COG3524 222 -----LIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSL------------ASL 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1820553714 1672 LQALEELRLQAEEAERRLRQAeverarqvQVALETAQrsAEAELQSK 1718
Cdd:COG3524 285 LAEYERLELEREFAEKAYTSA--------LAALEQAR--IEAARQQR 321
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1505-1958 |
8.85e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1505 ALEKQRQLAEAHAQA---KAQAEREAKELQQrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---EIQAKARQAE 1578
Cdd:pfam05557 22 ELEHKRARIELEKKAsalKRQLDRESDRNQE-LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEAlnkKLNEKESQLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1579 AAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQ---DESQRKRQAEAELA 1655
Cdd:pfam05557 101 DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1656 LRV-------KAEAEAAR--EKQRALQALEE--------------LRLQAEEAERRLRQAEVERARQVQVALE------- 1705
Cdd:pfam05557 181 SQEqdseivkNSKSELARipELEKELERLREhnkhlnenienkllLKEEVEDLKRKLEREEKYREEAATLELEkekleqe 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1706 ------TAQ------RSAEA------ELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERE 1767
Cdd:pfam05557 261 lqswvkLAQdtglnlRSPEDlsrrieQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1768 LERWQ------------LKAN-EALRLRLQAEEVAQQKSLAQAEAE----KQKEEAEREARRRGKAEEQAVRHRELA--- 1827
Cdd:pfam05557 341 VRRLQrrvllltkerdgYRAIlESYDKELTMSNYSPQLLERIEEAEdmtqKMQAHNEEMEAQLSVAEEELGGYKQQAqtl 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1828 EQELEKQRQlAEGTAQQRLAAE------QELIRLRAETEQGEQQRQLLEEELAR--------------LQHEAAAATQKR 1887
Cdd:pfam05557 421 ERELQALRQ-QESLADPSYSKEevdslrRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAY 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820553714 1888 QELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAEAGRFRELAEeaarLRALAEEA-KRQRQLAE 1958
Cdd:pfam05557 500 QQRKNQLEKLQAEIERL---KRLLKKLEDDLEQVLRLPETTSTMNFKEVLD----LRKELESAeLKNQRLKE 564
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1474-1638 |
9.56e-04 |
|
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: 43.90 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1474 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQK 1552
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEeLAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1553 RSIQEELQQLRQSSEAEIQAKARQA----------EAAERSRLRIEEEIrvvrLQLEATERQRGGAEGElQALRAQAEEA 1622
Cdd:pfam04012 125 TKIQQLKAKKNLLKARLKAAKAQEAvqtslgslstSSATDSFERIEEKI----EEREARADAAAELASA-VDLDAKLEQA 199
|
170
....*....|....*.
gi 1820553714 1623 EAQKRQAQEEAERLRR 1638
Cdd:pfam04012 200 GIQMEVSEDVLARLKA 215
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1509-1674 |
9.82e-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: 44.72 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1509 QRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAER-SRLRI 1587
Cdd:pfam00529 53 PTDYQAALDSAEAQL-AKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDlARRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1588 EEEIRVV-RLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALrvkAEAEAA 1665
Cdd:pfam00529 132 LAPIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIaEAEAELKL---AKLDLE 208
|
....*....
gi 1820553714 1666 REKQRALQA 1674
Cdd:pfam00529 209 RTEIRAPVD 217
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1927-2438 |
1.02e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 45.62 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1927 EAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRL 2006
Cdd:COG3899 753 EALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARA 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2007 AEDEAFqrrrleeqAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELG 2086
Cdd:COG3899 833 LFNLGF--------ILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAAL 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2087 RIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2166
Cdd:COG3899 905 AAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAA 984
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2167 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAEREAAQSRR 2246
Cdd:COG3899 985 AAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAA 1064
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2247 QVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAemekhkkfaeqtLRQKAQVEQELT 2326
Cdd:COG3899 1065 AAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL------------AALALAAAARAA 1132
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2327 TLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEE 2406
Cdd:COG3899 1133 AALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLAL 1212
|
490 500 510
....*....|....*....|....*....|..
gi 1820553714 2407 AEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2438
Cdd:COG3899 1213 ALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1683-2019 |
1.09e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.10 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1683 EEAERRLRQAEVERARqvqvaLETAQRSAEAELQSKRASFAE----KTAQLERS---LQEEHVAVAQLREEAERRAQQQA 1755
Cdd:pfam03528 4 EDLQQRVAELEKENAE-----FYRLKQQLEAEFNQKRAKFKElylaKEEDLKRQnavLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1756 EAERAREEAerelERWQLKANEALRLRLQaEEVAqqkSLAQAEAEKQKEEAEREARRRGKAEEQAVRHRELAEQEL-EKQ 1834
Cdd:pfam03528 79 NIKAVATVS----ENTKQEAIDEVKSQWQ-EEVA---SLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIaDLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1835 RQLAEGTAQQRLaaEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAelAKVRAEMEVLLASKA-RAEE 1913
Cdd:pfam03528 151 RRLSEGQEEENL--EDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEA--SKMKELNHYLEAEKScRTDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1914 ESR-STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL---AEKLAAISEATRLKTEA 1989
Cdd:pfam03528 227 EMYvAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLmrdMQRMESVLTSEQLRQVE 306
|
330 340 350
....*....|....*....|....*....|
gi 1820553714 1990 EIALKEKEaENERLRRLAEDEAFQRRRLEE 2019
Cdd:pfam03528 307 EIKKKDQE-EHKRARTHKEKETLKSDREHT 335
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2406-2541 |
1.11e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.39 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2406 EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2481
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2482 RLQEDKEQmaQQLAEetqgfqrtLEAERQRQLeMSAEAERLKLRMAEMSR----AQARAEEDAQ 2541
Cdd:PTZ00491 761 QELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3822-3860 |
1.11e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1820553714 3822 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 3860
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2331-2607 |
1.17e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2331 QLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL-SKLKARIEAENRALILRDKDNTQrfLQEEAEK 2409
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELnAQVKELREEAQELREKRDELNEK--VKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2410 MKQVAEEAARLSvaaQEAARLRQLAEEDLAQQRALAEkmLKEKMQAVQ-----EATRLKAEAELLQQQKELAQE-QARRL 2483
Cdd:COG1340 80 RDELNEKLNELR---EELDELRKELAELNKAGGSIDK--LRKEIERLEwrqqtEVLSPEEEKELVEKIKELEKElEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2484 QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRA--QARAEEDA-----QRFRKQAEEIGEKLHR 2556
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEadELRKEADElhkeiVEAQEKADELHEEIIE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2557 T-----ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQ-QEAKLLQ 2607
Cdd:COG1340 235 LqkelrELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTtEELKLLQ 291
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2392-2599 |
1.21e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2392 ILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2465
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2466 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQR 2542
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2543 FRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL 2599
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1474-1579 |
1.23e-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: 44.21 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1474 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAK------AQ--AEREAKELQQRMQEEV-V 1539
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEvakiqmQQkiMEKEAEKKISEIEDEMhL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1820553714 1540 RREEAAVDAQQQKRSIQEELQQLRQSSE----AEIQAKARQAEA 1579
Cdd:cd03406 237 AREKARADAEYYRALREAEANKLKLTPEylelKKYQAIANNTKI 280
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1935-2080 |
1.23e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1935 ELAEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 2013
Cdd:COG2268 196 EIIRDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 2014 RRRLEEQAAQHKADIEERLAQLRKasdsELERQkglvedtlRQRRQVEEEILALKASFEKAAAGKAE 2080
Cdd:COG2268 276 EREVQRQLEIAEREREIELQEKEA----EREEA--------ELEADVRKPAEAEKQAAEAEAEAEAE 330
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2317-2659 |
1.25e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2317 QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENralilrDK 2396
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI------DK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2397 DNTQRFLQEEaekmkqvaeeaaRLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ-K 2473
Cdd:TIGR04523 192 IKNKLLKLEL------------LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2474 ELAQEQarrlQEDKEQMAQQLAEETQGFQRTLEAERQRQlEMSAEAERLKlrmaemsraqaraeedaqrfrKQAEEIGEK 2553
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN---------------------NQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2554 LHRTELATQEKVtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvqqeqllqetqaLQQSFL 2633
Cdd:TIGR04523 311 ELKSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN------------EIEKLK 376
|
330 340
....*....|....*....|....*.
gi 1820553714 2634 SEKDSLLQRERFIEQEKAKLEQLFQD 2659
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN 402
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2309-2763 |
1.28e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2309 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEN 2388
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2389 RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2468
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2469 LQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2548
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2549 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQAL 2628
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2629 QQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQHEAEEGVRRKQE 2708
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2709 ELQQLEQQRRQQEELLAEENQRLREQLQRLEEQHRAALAHSEEVTALQVAATKTL 2763
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1352-1583 |
1.31e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1352 SADPLgawLQDARQRQEQIQAMpLADSQAVREQLRQE-KALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQL 1430
Cdd:COG3883 13 FADPQ---IQAKQKELSELQAE-LEAAQAELDALQAElEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1431 EPVASPAKKPKVQSGSESVI---QEYVDLRTRYSELTTLTSQYikfiSETLRRMEEEERLAEQQRAEERERLAEVEAALE 1507
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1508 KQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERS 1583
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2287-2502 |
1.41e-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: 44.20 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2287 AQAEQAALRQKQAA--DAEMEKHKKFAEQTLRQ----KAQVEQELTTLRLQLEETDHqknllDEELQRLKAEATEAARQR 2360
Cdd:pfam02841 37 AQIENSAAVQKAIAhyEQQMAQKVKLPTETLQElldlHRDCEKEAIAVFMKRSFKDE-----NQEFQKELVELLEAKKDD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2361 SQVEEELFSVRVQMEELSKLKARIEAENRA----------LILRDKDNT------------------QRFLQEEA----- 2407
Cdd:pfam02841 112 FLKQNEEASSKYCSALLQDLSEPLEEKISQgtfskpggykLFLEERDKLeakynqvprkgvkaeevlQEFLQSKEaveea 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2408 ---------EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQ 2472
Cdd:pfam02841 192 ilqtdqaltAKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEH 269
|
250 260 270
....*....|....*....|....*....|
gi 1820553714 2473 KElaQEQARRLQEDKEQMAQQLAEETQGFQ 2502
Cdd:pfam02841 270 KL--QEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1367-1649 |
1.43e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1367 QEQIQAM-----PLADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpk 1441
Cdd:PRK11281 42 QAQLDALnkqklLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1442 vqsgsesviqeyvdlRTRYSELttltsqyikfiseTLRRMEE--EERLAEQQRAeererlaeveaalekQRQLAEAHAQ- 1518
Cdd:PRK11281 115 ---------------RETLSTL-------------SLRQLESrlAQTLDQLQNA---------------QNDLAEYNSQl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1519 --AKAQAEREAKEL---QQRMQEevVRREEAAVDAQQqkRSIQEELQQLRQSSEAEIQAKA--RQAEAAERSRL------ 1585
Cdd:PRK11281 152 vsLQTQPERAQAALyanSQRLQQ--IRNLLKGGKVGG--KALRPSQRVLLQAEQALLNAQNdlQRKSLEGNTQLqdllqk 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1586 -RIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLrrqVQDESQRKRQ 1649
Cdd:PRK11281 228 qRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPL---VAQELEINLQ 289
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1536-1743 |
1.44e-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: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1536 EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR------QAEAAERSRLRIEEEIRVvrLQLEATERQRGGAE 1609
Cdd:COG3206 97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNvieisyTSPDPELAAAVANALAEA--YLEQNLELRREEAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1610 GELQALRAQAEEAEAQKRQAQEEAERLRRQvqdesqrkrqaeaELALRVKAEAEAAREKQRALQA-LEELRLQAEEAERR 1688
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQK-------------NGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEAR 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1689 LRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1743
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1509-1671 |
1.46e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1509 QRQLAEAHAQAK---AQAEREAKELQQRM----QEEVVR-REEAAVDAQQQKRSIQEELQQLRQSSEAEiqakARQAEAA 1580
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAIKKEAlleaKEEIHKlRNEFEKELRERRNELQKLEKRLLQKEENL----DRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1581 ERSrlriEEEIRVVRLQLEATERqrggaegELQALRAQAEEAEAQKRQA--------QEEA-ERLRRQVQDEsqrkrqAE 1651
Cdd:PRK12704 106 EKR----EEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEE------AR 168
|
170 180
....*....|....*....|..
gi 1820553714 1652 AELALRVKAEAEAARE--KQRA 1671
Cdd:PRK12704 169 HEAAVLIKEIEEEAKEeaDKKA 190
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1824-2257 |
1.49e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1824 RELAEQELEKQRQLAEGTAQQ--RLAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAE 1900
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQqaRLDELEALIDQWlAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1901 MEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIS 1980
Cdd:COG5278 165 LAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALAL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1981 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQV 2060
Cdd:COG5278 245 LLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2061 EEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQ 2140
Cdd:COG5278 325 LAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAA 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2141 RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEA 2220
Cdd:COG5278 405 EAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAAL 484
|
410 420 430
....*....|....*....|....*....|....*..
gi 1820553714 2221 EVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQL 2257
Cdd:COG5278 485 AEAEAAAALAAAAALSLALALAALLLAAAEAALAAAL 521
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2403-2566 |
1.50e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2403 LQEEAEKMKQVAEEAARL-SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2481
Cdd:pfam05262 186 LREDNEKGVNFRRDMTDLkERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPAD 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2482 --------RLQEDKEQMAQQLAEETQgfQRTLEAERQRQlemsAEAERLKLRMAEMSRAQARAEEDAQRFRkqaEEIGEK 2553
Cdd:pfam05262 266 tsspkedkQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR---EPVAED 336
|
170
....*....|...
gi 1820553714 2554 LHRTELATQEKVT 2566
Cdd:pfam05262 337 LQKTKPQVEAQPT 349
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2318-2751 |
1.51e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2318 KAQVEQ-ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIE--AENRALILR 2394
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2395 DKDNTQRFLQEEAEKMKQVAEEA------ARLSVAAQEAARLRQlaeEDLAQQRALAEKMLKEKMQAVQEATRlkaEAEL 2468
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERddllaeAGLDDADAEAVEARR---EELEDRDEELRDRLEECRVAAQAHNE---EAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2469 LQQQKELAQEQARRLQEDkeqmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2548
Cdd:PRK02224 347 LREDADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2549 EIGEKLhrTELATQEKvTLVQTLEIQRQ-----------QSDHDAERLrEAIAELEREKEKLQQEAKLLQLKSEEMQTVQ 2617
Cdd:PRK02224 423 ELRERE--AELEATLR-TARERVEEAEAlleagkcpecgQPVEGSPHV-ETIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2618 QEQLLQETQALQQSFLSEKDSLLqrERFIEQEKAKLEqlfqDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARQRQH 2697
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDL--EELIAERRETIE----EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2698 EAEEGVRRKQEELQQLEQQRRQQEELLAEENqrLREQLQRLEEQhRAALAHSEE 2751
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIAD--AEDEIERLREK-REALAELND 623
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2290-2558 |
1.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2290 EQAALRQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQ 2362
Cdd:COG1340 10 LEELEEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2363 VEEELFSVRVQMEEL-------SKLKARIEA-------------ENRALILRDKDntqrfLQEEAEKMKQVAEEAARLSV 2422
Cdd:COG1340 90 LREELDELRKELAELnkaggsiDKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2423 AAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaeetq 2499
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL----- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 2500 gfqrtleaerqRQLEMSAEAERLKLRMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2558
Cdd:COG1340 240 -----------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1863-2073 |
1.56e-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: 43.37 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1863 EQQRQLLEeeLARLQHEAAAATQKRQELEAELAKVRAEMEvllaskaraeeesrstsekskqrleaeagrfrELAEEAAR 1942
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELA--------------------------------ALEARLEA 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1943 LRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAISEATrlktEAEIALKEKEAeNERLRRLAEDEAFQRRRLEEQAA 2022
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNK----EYEALQKEIES-LKRRISDLEDEILELMERIEELE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2023 QHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEK 2073
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2375-2503 |
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 1820553714 2375 EELSKLKARIEAENRALILRDKDNTQrfLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2454
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 2455 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAEETQGFQR 2503
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
175-278 |
1.59e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 175 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 232
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1820553714 233 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 278
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2277-2613 |
1.64e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2277 KDAEQEAVrrAQAEQAALRQKQAADAEMEKHKKFaEQTLRQKAQVEQELttlrlqleetdhQKNLLDEELQRLKAEATEA 2356
Cdd:PRK10929 39 KTPAQAEI--VEALQSALNWLEERKGSLERAKQY-QQVIDNFPKLSAEL------------RQQLNNERDEPRSVPPNMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2357 ArqrSQVEEELFSVRVQMEELSklkarieaenralilrdkdntqRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE 2436
Cdd:PRK10929 104 T---DALEQEILQVSSQLLEKS----------------------RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2437 DLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2512
Cdd:PRK10929 159 RLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQRE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2513 LEMSAE-AERLKLRMAEMSRAQARA----EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQ------SDHD 2581
Cdd:PRK10929 239 AERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQsqwlgvSNAL 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 1820553714 2582 AERLREAIAELErEKEKLQQ------EAKLLQLKSEEM 2613
Cdd:PRK10929 319 GEALRAQVARLP-EMPKPQQldtemaQLRVQRLRYEDL 355
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1518-1733 |
1.71e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1518 QAKAQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQEELQQLRQ------SSEAEIQAK--------ARQAEAA 1580
Cdd:PRK11637 54 QDIAAKEKSVRQQQQQrasLLAQLKKQEEAISQASRKLRETQNTLNQLNKqidelnASIAKLEQQqaaqerllAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1581 ERSR--------LRIEEEIRVVRLQL------EAteRQRggAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQR 1646
Cdd:PRK11637 134 FRQGehtglqliLSGEESQRGERILAyfgylnQA--RQE--TIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1647 KRQAEAElalRVK--AEAEAAREKQRalQALEELRLQaeeaERRLR----QAEVE-RARQVQVALEtAQRSAEAELQSKR 1719
Cdd:PRK11637 210 LEQARNE---RKKtlTGLESSLQKDQ--QQLSELRAN----ESRLRdsiaRAEREaKARAEREARE-AARVRDKQKQAKR 279
|
250
....*....|....
gi 1820553714 1720 ASFAEKTAQLERSL 1733
Cdd:PRK11637 280 KGSTYKPTESERSL 293
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1200-1644 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1200 LRSELELTLGKLEQVRSLSAIYLEKLKTISLVIrsTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKL----RAQ 1275
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEDLQIATKTI--CQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlrteQQR 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1276 AEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWR----------------ERVAQLLE-RWQAVLAQTDVRQRE 1338
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaedeklldekkqfEKIAEELKgKEQELIFLLQAREKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1339 LEQLGRQL-------RYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQ 1411
Cdd:pfam05483 452 IHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1412 YINAIKDYELQLVTYKAQLEPVASPAK------KPKVQSGSESVIQEYVDLRTRYSELTTLTS------QYIKFISETLR 1479
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDKSEENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIE 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1480 RMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQAKA-----QAEREAKEL-QQRMQEEVVRREEAAVDAQQQK 1552
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAYEIKVNKlELELASAKQKFEEiidnyQKEIEDKKIsEEKLLEEVEKAKAIADEAVKLQ 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1553 RSIQEELQQLRQSSEAEIQAKARQAEAAERSRlriEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEE 1632
Cdd:pfam05483 692 KEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
490
....*....|..
gi 1820553714 1633 AERLRRQVQDES 1644
Cdd:pfam05483 769 KEKLKMEAKENT 780
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1854-2107 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1854 RLRAETEQGEQQRQLLEEELARLQHEAAAAtqkrqelEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEAEAgrf 1933
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARA--- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1934 rELAEEAARLRALaeeakrQRQLAEEDAARQRAEAERVLAEKLAAISEAtrlktEAEIAlkekeaeneRLRRLAEDEAFQ 2013
Cdd:COG3206 234 -ELAEAEARLAAL------RAQLGSGPDALPELLQSPVIQQLRAQLAEL-----EAELA---------ELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2014 RRRLEEQaaqhKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAE 2093
Cdd:COG3206 293 VIALRAQ----IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
250
....*....|....
gi 1820553714 2094 DTLRSKEQAELEAA 2107
Cdd:COG3206 369 SLLQRLEEARLAEA 382
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1815-2050 |
1.79e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.67 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQ-RQLLEEELARLqHEAAAATQKRQEleae 1893
Cdd:pfam05911 10 KVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKI-HDVVLKKTKEWE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1894 laKVRAEMEVLLAskaraeeesrstsEKSKQRLEAEagrfrelAEEAARLRALAEEAKRQRQLAEEdaaRQRAEAE-RVL 1972
Cdd:pfam05911 85 --KIKAELEAKLV-------------ETEQELLRAA-------AENDALSRSLQERENLLMKLSEE---KSQAEAEiEAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820553714 1973 AEKLAAIS-EATRLKTEAEIALKEKEAENErlrrlaEDEaFQRRRLEEQAAQHKADIeERLAQLrkasDSELERQKGLV 2050
Cdd:pfam05911 140 KSRLESCEkEINSLKYELHVLSKELEIRNE------EKN-MSRRSADAAHKQHLESV-KKIAKL----EAECQRLRGLV 206
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2378-2612 |
1.83e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2378 SKLKARIEAENRALILRdkdntQRFlqeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQ 2457
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAK-----ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2458 EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQR-------QLEMSAEAE-----RLKLR 2525
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaQQAANAEAEeevdpKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2526 MAEMSRAQAR---AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREK-EKLQQ 2601
Cdd:PRK05035 583 AAAIARAKAKkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKaRKAAQ 662
|
250
....*....|.
gi 1820553714 2602 EAKLLQLKSEE 2612
Cdd:PRK05035 663 QQANAEPEEAE 673
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2001-2182 |
1.85e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2001 ERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAE 2080
Cdd:COG1579 7 RALLDLQELDS-ELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEI-------EEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2081 LELELGRIRSNAE-DTLrskeQAELEAARQRQlaaeeeqrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2159
Cdd:COG1579 78 YEEQLGNVRNNKEyEAL----QKEIESLKRRI---------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
170 180
....*....|....*....|...
gi 1820553714 2160 RLRERAEQESARQLQLAQEAAQK 2182
Cdd:COG1579 145 AELDEELAELEAELEELEAEREE 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2373-2759 |
1.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2373 QMEELSKLKARieaeNRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQlAEEDLAQQRALAEKmLKEK 2452
Cdd:COG4717 54 EADELFKPQGR----KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-ELEELREELEKLEK-LLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2453 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRA 2532
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2533 QARAEEDAQRFRKQAEEIGEKLHRTElatqekvtlvqtleiQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2612
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLE---------------NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2613 MQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 2692
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2693 RQRQHEAEEGVRRKQEELQQLEQQRR---------QQEELLAEENQRLREQL----QRLEEQHRAALAHSEEVTALQVAA 2759
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEagvedeeelRAALEQAEEYQELKEELeeleEQLEELLGELEELLEALDEEELEE 432
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1506-1670 |
1.96e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1506 LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrl 1585
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1586 rieeeirvvrlqLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDE---SQRKRQAEAELALRVKAEA 1662
Cdd:PRK12705 100 ------------LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKlllKLLDAELEEEKAQRVKKIE 167
|
....*...
gi 1820553714 1663 EAAREKQR 1670
Cdd:PRK12705 168 EEADLEAE 175
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1496-1701 |
2.07e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.51 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1496 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEelqQLRQSSEAEIQAKAR 1575
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAE---AASAPEAAQARERRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1576 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqaLRAQAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAE-AEL 1654
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEE-----EERDERRRRGDREDRQAEAERGERG--RREERGRDGDdRDR 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1820553714 1655 ALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQ 1701
Cdd:PRK12678 206 RDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| PRK01294 |
PRK01294 |
lipase secretion chaperone; |
1530-1703 |
2.07e-03 |
|
lipase secretion chaperone;
Pssm-ID: 234937 [Multi-domain] Cd Length: 336 Bit Score: 43.90 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1530 LQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaersrlrieeeirvvrLQLEATERQRGGAE 1609
Cdd:PRK01294 187 YQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQAL----------------LQQLAQLQASGASP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1610 GELQALRAQAEEAEAqkrqaqeeAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1689
Cdd:PRK01294 251 QELRLMRAQLVGPEA--------AQRLEQLDQQRAAWQQRYDDYLAQRAQILNAAGLSPQDRQAQIAQLRQQRFSPQEAL 322
|
170
....*....|....
gi 1820553714 1690 RQAEVERARQVQVA 1703
Cdd:PRK01294 323 RLAALERIHDAGQT 336
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2462-2763 |
2.09e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2462 LKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAEETQGFQRTLEAERqrqlEMSAEAERLKLRMAEmsraqaraeedaq 2541
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAA------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2542 rfRKQaeEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvqqeql 2621
Cdd:pfam01576 69 --RKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEE------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2622 lqetqalQQSFLSEKDSLLQRER-FIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvASMEEARQRQheae 2700
Cdd:pfam01576 139 -------DILLLEDQNSKLSKERkLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERL-KKEEKGRQEL---- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2701 EGVRRKQEELQQLEQQRRQQEELLAEEnqrLREQLQRLEEQHRAALAHSEEVTALQVAATKTL 2763
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAE---LRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1482-1735 |
2.25e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 44.28 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1482 EEEERLAEQQRAEERERLAEVEA--ALEKQRQLAEAHAQAKAQAEREAKelQQRMQEEVVRREEAAVDAqqqkrsiqeEL 1559
Cdd:pfam04747 72 KSEKKKAQKQIAKDHEAEQKVNAkkAAEKEARRAEAEAKKRAAQEEEHK--QWKAEQERIQKEQEKKEA---------DL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1560 QQLRQSSEAEIQAKARQAEAAERSR-----LRIEEEIRVVRLqleATERQRGGAEGELQALRAQAEEAEaqkrQAQEEAE 1634
Cdd:pfam04747 141 KKLQAEKKKEKAVKAEKAEKAEKTKkastpAPVEEEIVVKKV---ANDRSAAPAPEPKTPTNTPAEPAE----QVQEITG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1635 RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1714
Cdd:pfam04747 214 KKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQ 293
|
250 260
....*....|....*....|.
gi 1820553714 1715 LQSKRasfAEKTAQLERSLQE 1735
Cdd:pfam04747 294 KKNKK---DKKKSESEKVVEE 311
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1858-2080 |
2.30e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1858 ETEQGEQQRQLLEEELARLQ-----------HEAAAATQKRQELEAELAKVRAEMEV-----LLASKARAEEESRSTSEK 1921
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAAAAkakaaALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1922 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--AARQRAEAERVLAEKLAAISEATRLKTEAEIAL---KEK 1996
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkaAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKakaKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1997 EAENERLRRLAEDEAFQRRRLEEQAAQH-KADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEE-ILALKASFEKA 2074
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKAKAAAA 250
|
....*.
gi 1820553714 2075 AAGKAE 2080
Cdd:PRK07735 251 ARAKTK 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2021-2197 |
2.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2021 AAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE 2100
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2101 QAELEAARQRQLAAEEEQRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2166
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 1820553714 2167 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2197
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
176-284 |
2.43e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.13 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 176 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 246
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1820553714 247 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 284
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1860-2010 |
2.48e-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: 44.15 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1860 EQGEQQRQLLEEELARLQHeaAAATQKRQELEAELAKVRAEM--EVLLASKARAEEesrstseKSKQRLEAEAGRFR--- 1934
Cdd:pfam04147 128 DSEEEEDGQLDLKRVRRAH--FGGGEDDEEEEPERKKSKKEVmeEVIAKSKLHKYE-------RQKAKEEDEELREEldk 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1935 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE-----RVLA-EKLAAISEatRLKTEAEIALKEKE----AENERLR 2004
Cdd:pfam04147 199 ELKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydklvRELAfDKRAKPSD--RTKTEEELAEEEKErlekLEEERLR 276
|
....*.
gi 1820553714 2005 RLAEDE 2010
Cdd:pfam04147 277 RMRGEE 282
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1940-2084 |
2.50e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1940 AARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAISEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 2019
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 2020 QAAQ------HKADIEERLAQLRKASDSELERQKGLVEDTLRQR--RQVEEEILALKASFEKAAAGKAELELE 2084
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
187-277 |
2.65e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.75 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 187 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 259
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1820553714 260 DDIADGNPKLTLGLIWTI 277
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1449-1716 |
2.65e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 43.49 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1449 VIQEYVDLRtRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEererLAEVEAALEKQRQLAEAHAQAKAQAEREAK 1528
Cdd:COG1538 78 VAQAYFDLL-AAQEQLALAEENLALAEELLELARARYEAGLASRLD----VLQAEAQLAQARAQLAQAEAQLAQARNALA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1529 ELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeAEIQAKARQAEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1608
Cdd:COG1538 153 LLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERR-PDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1609 EGELQ-------------------ALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ 1669
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1670 RALQALEEL-------RLQAEEAERRLRQAEVERarqvqVALETAQRSAEAELQ 1716
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1479-1568 |
2.69e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.14 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1479 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAH-------AQAKAQAEREAKE-LQQRMQEEVVRREEAAVDAQ 1549
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARkqaqaviAEAEAEADKLAAEaLAEAQAEAQASKEKARREIE 111
|
90
....*....|....*....
gi 1820553714 1550 QQKrsiQEELQQLRQSSEA 1568
Cdd:PRK07353 112 QQK---QAALAQLEQQVDA 127
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1479-1723 |
2.72e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1479 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1558
Cdd:COG3064 60 AKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1559 LQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRR 1638
Cdd:COG3064 140 ERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLAL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1639 QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK 1718
Cdd:COG3064 220 AVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDD 299
|
....*
gi 1820553714 1719 RASFA 1723
Cdd:COG3064 300 SAALA 304
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1818-1961 |
2.72e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1818 EQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1897
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820553714 1898 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1961
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1501-1890 |
2.79e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1501 EVEAALEKqrqlaeahaqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeaeiqAKARQAEAA 1580
Cdd:pfam02029 4 EEEAARER---------------RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1581 ERSRLRIEEEIRVVRLQlEATERQRggaEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1660
Cdd:pfam02029 64 FLDRTAKREERRQKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1661 EAEAAREKqralqalEELRLQAEEAERRLRQAEVERA-RQVQVALETAQRSAEAELQSKRASfaEKTAQLERSLQEEHVA 1739
Cdd:pfam02029 140 YQENKWST-------EVRQAEEEGEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYES--KVFLDQKRGHPEVKSQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1740 VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrlrlqaeevaqqkslaqaeaekqkeeaerearrrgkaEEQ 1819
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKL-------------------------------------EEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1820 AVRHRELAEQELEKQRQlaegtAQQRLAAEQELI--------RLRAETEQG----EQQRQLLEEELARLQHEA-----AA 1882
Cdd:pfam02029 254 RRRRQEKESEEFEKLRQ-----KQQEAELELEELkkkreerrKLLEEEEQRrkqeEAERKLREEEEKRRMKEEierrrAE 328
|
....*...
gi 1820553714 1883 ATQKRQEL 1890
Cdd:pfam02029 329 AAEKRQKL 336
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1588-1820 |
2.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1588 EEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAARE 1667
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1668 KQRA---LQALEELrLQAEEAERRLRQAEVERArqvqvaLETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLR 1744
Cdd:COG3883 95 LYRSggsVSYLDVL-LGSESFSDFLDRLSALSK------IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1745 EEAERRAQQQAEAERAREEAERelerwQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQA 1820
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSA-----EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1842-2084 |
2.90e-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: 43.98 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1842 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAatQKRQELEA---ELAKVRAEMEVLLASK-----ARAEE 1913
Cdd:pfam09731 217 APETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERI--VFQQELVSifpDIIPVLKEDNLLSNDDlnsliAHAHR 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1914 ESRSTSEK-SKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLAEklaaISEATRLKTEAEI 1991
Cdd:pfam09731 295 EIDQLSKKlAELKKREEKHIERALEKQKEELDKLAEElSARLEEVRAADEAQLRLEFEREREE----IRESYEEKLRTEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1992 ALKEKEAEnERLR-RLAEDEAFQRRR--------LEEQAAQHKADIEE---RLAQLRKASDSELErqkglVEDTLRQRRQ 2059
Cdd:pfam09731 371 ERQAEAHE-EHLKdVLVEQEIELQREflqdikekVEEERAGRLLKLNEllaNLKGLEKATSSHSE-----VEDENRKAQQ 444
|
250 260
....*....|....*....|....*
gi 1820553714 2060 VEEEILALKASFEKAAAGKAELELE 2084
Cdd:pfam09731 445 LWLAVEALRSTLEDGSADSRPRPLV 469
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2242-2499 |
2.93e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2242 AQSRRQVEEAERLKQLAEeqaqaraqaqaaaeklrkDAEQEaVRRAQAEQAALRQKQAADAEmekhKKFAEQTLRqkaQV 2321
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLA------------------QAPAK-LRQAQAELEALKDDNDEETR----ETLSTLSLR---QL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2322 EQELTTLRLQLEETdhQKNLldeelqrlkAEA-TEAARQRSQVEE---ELFSVRVQMEELSKLKARIEAENRALI--LRD 2395
Cdd:PRK11281 127 ESRLAQTLDQLQNA--QNDL---------AEYnSQLVSLQTQPERaqaALYANSQRLQQIRNLLKGGKVGGKALRpsQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2396 KDNT-QRFLQEEAEKMKQVAEEAARLSVAAQE-----AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAElL 2469
Cdd:PRK11281 196 LLQAeQALLNAQNDLQRKSLEGNTQLQDLLQKqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAAR-I 274
|
250 260 270
....*....|....*....|....*....|
gi 1820553714 2470 QQQKELAQEQARRLqedkeQMAQQLAEETQ 2499
Cdd:PRK11281 275 QANPLVAQELEINL-----QLSQRLLKATE 299
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2316-2663 |
3.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2316 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENRALilrd 2395
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR---EELEQLEEELEQARSEL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2396 kdntqrflQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKEL 2475
Cdd:COG4372 76 --------EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2476 AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIG--EK 2553
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAkdSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2554 LHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFL 2633
Cdd:COG4372 228 EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
330 340 350
....*....|....*....|....*....|
gi 1820553714 2634 SEKDSLLQRERFIEQEKAKLEQLFQDEVAK 2663
Cdd:COG4372 308 SLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1817-2078 |
3.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1817 EEQAVRHRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQheaaaatQKRQELEAE 1893
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELneeLKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK-------EERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1894 LAKVRAEMEVLLASKARAEEESRSTSEKSKqRLEAEAGRF----------RELAEEAARLRALAEEAKRQRQLAEE-DAA 1962
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRK-EIERLEWRQqtevlspeeeKELVEKIKELEKELEKAKKALEKNEKlKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1963 RQRAEAERVLAE----KLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 2038
Cdd:COG1340 166 RAELKELRKEAEeihkKIKELAEEAQELHEEMIELYKEA---DELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1820553714 2039 SDSElerqKGLVEDTLRQRRQVEEEILALKAS--FEKAAAGK 2078
Cdd:COG1340 243 RKEL----KKLRKKQRALKREKEKEELEEKAEeiFEKLKKGE 280
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1481-1561 |
3.06e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1481 MEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAH-------AQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQ 1551
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEyEEKLAEARaeaqeiiEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQE 107
|
90
....*....|
gi 1820553714 1552 KRSIQEELQQ 1561
Cdd:cd06503 108 KEKALAELRK 117
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2293-2614 |
3.08e-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: 43.74 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2293 ALRQKQAADAEMEKHKKFAEQTLRQKAQVEQEL----TTLRLQLE----ETDHQKNLLDEEL---QRLKAEATEAARQRS 2361
Cdd:pfam15964 315 ALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEAnfekTKALIQCEqlksELERQKERLEKELasqQEKRAQEKEALRKEM 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2362 QVEEE-----LFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQLAEE 2436
Cdd:pfam15964 395 KKEREelgatMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMK----KDEAEK 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2437 DLAQQRALAEKMLKEKMQAVQeatRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMS 2516
Cdd:pfam15964 471 EHREYRTKTGRQLEIKDQEIE---KLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFS 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2517 AEAERLKLRmaemsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLE----IQRQQSDHDAERLREAIAEL 2592
Cdd:pfam15964 548 NEAKAQALQ------AQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKeeccTLAKKLEEITQKSRSEVEQL 621
|
330 340
....*....|....*....|..
gi 1820553714 2593 EREKEKLQQEAKLLQLKSEEMQ 2614
Cdd:pfam15964 622 SQEKEYLQDRLEKLQKRNEELE 643
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1874-2001 |
3.14e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 42.86 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1874 ARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsekskqrlEAEAGRFRELAEEAARLRALAEEA-KR 1952
Cdd:PRK06991 146 AWSQAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAA--------EASAAAAPAADDAEAKKRAIIAAAlER 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1953 QRQLAEEDAARQRA--EAERVLAEKLAAI--SEATRLKTEAEIALKEKEAENE 2001
Cdd:PRK06991 218 ARKKKEELAAQGAGpkNTEGVSAAVQAQIdaAEARRKRLAEQRDAPDDANADG 270
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2315-2612 |
3.21e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2315 LRQKAQVEQ-ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFsvrvQMEELSKLKARIEAEnraliL 2393
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2394 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2473
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2474 ELAQEQARRLQEDKEQMAQQLAEET--QGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIG 2551
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2552 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2599
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 1820553714 2600 QQEAKllQLKSEE 2612
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1476-1742 |
3.23e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKrsi 1555
Cdd:COG3064 45 AELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEK--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1556 qeeLQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAER 1635
Cdd:COG3064 122 ---AEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1636 LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1715
Cdd:COG3064 199 AAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGL 278
|
250 260
....*....|....*....|....*..
gi 1820553714 1716 QSKRASFAEKTAQLERSLQEEHVAVAQ 1742
Cdd:COG3064 279 VVVAAALAGLAAAAAGLVLDDSAALAA 305
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2143-2320 |
3.25e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2143 AALEEVERLKAKVEEARR---LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEqsvLDRLRSE 2219
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRaeeQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAA---LKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2220 AEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAE---QAALRQ 2296
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEakkKAAAEA 215
|
170 180
....*....|....*....|....
gi 1820553714 2297 KQAADAEMEKHKKFAEQTLRQKAQ 2320
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAKAAAE 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2392-2554 |
3.51e-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: 42.22 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2392 ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQ---EATRLKAEAEL 2468
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2469 LQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleaerqrqlEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2548
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEA--------------ELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*.
gi 1820553714 2549 EIGEKL 2554
Cdd:COG1579 167 ELAAKI 172
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1826-2111 |
3.65e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1826 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL 1905
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1906 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAISEAtRL 1985
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1986 KTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrqveeeil 2065
Cdd:PRK11637 170 ETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT--------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 2066 ALKASFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-------ARQRQ 2111
Cdd:PRK11637 223 GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2470-2604 |
3.83e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2470 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRMAEMSR------AQARAEEDAQRF 2543
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 2544 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLQQEAK 2604
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1815-2064 |
3.99e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVRHRELAEQ--ELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELE 1891
Cdd:pfam13868 67 RKEERKRYRQELEEQieEREQKRQEEyEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1892 AELAKvRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE-----------EAARLRALAEEAKRQRQLAEED 1960
Cdd:pfam13868 147 KEEER-EEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQqekaqdekaerDELRAKLYQEEQERKERQKERE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1961 AARQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAEN--ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLA---QL 2035
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEereEQ 305
|
250 260
....*....|....*....|....*....
gi 1820553714 2036 RKASDSELERQKGLVEDTLRQRRQVEEEI 2064
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERRERIEEE 334
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2424-2606 |
4.09e-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: 42.22 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2424 AQEAARLRQLAEED--LAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETqgf 2501
Cdd:COG1579 3 PEDLRALLDLQELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2502 qrtleaERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTElatqekvtlvQTLEIQRQQSDHD 2581
Cdd:COG1579 80 ------EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEK 143
|
170 180
....*....|....*....|....*
gi 1820553714 2582 AERLREAIAELEREKEKLQQEAKLL 2606
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREEL 168
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1494-1627 |
4.24e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1494 EERERLAEVEAALEKQRQLAEAHaqakaQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSiQEELQQLRQSSEAEIQAK 1573
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEE-----EERLRKEELRRRAEEERARREEEARRLEEERRR-EEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1574 ARQAEAAERSRLRIEEEIRVvrlqLEATERQRggAEGELQALRAQAEEAEAQKR 1627
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKA----REEAERQR--QEREKIMQQEEQERLERKKR 138
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1257-1700 |
4.31e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1257 ATLPELEATKASLKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQ 1336
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1337 RELEQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAI 1416
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1417 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEER 1496
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1497 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQ 1576
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1577 AEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL 1656
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1820553714 1657 RVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1700
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1360-1530 |
4.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1360 LQDARQRQEQIqampLADSQAVREQLRQEKALLEEIERHGEKvEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspAKK 1439
Cdd:PRK12704 33 IKEAEEEAKRI----LEEAKKEAEAIKKEALLEAKEEIHKLR-NEFEKELRERRNELQKLEKRLLQKEENLD-----RKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1440 PKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEeeeRLAEQQRAEERERL---AEVEAALEKQRQLAEAH 1516
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE---RISGLTAEEAKEILlekVEEEARHEAAVLIKEIE 179
|
170
....*....|....
gi 1820553714 1517 AQAKAQAEREAKEL 1530
Cdd:PRK12704 180 EEAKEEADKKAKEI 193
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1620-1737 |
4.35e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1620 EEAeaqKRQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1699
Cdd:PRK00409 505 EEA---KKLIGEDKEKLNELIASLEELERELEQKA-------EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110
....*....|....*....|....*....|....*....
gi 1820553714 1700 VQVALETAQRSAEAELQSKRASFAEKTAQL-ERSLQEEH 1737
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVkAHELIEAR 613
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1318-1595 |
4.36e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1318 VAQLLERWQAVLAQTDVRQRELEQLGRQLryyrESADplgawlQDARQRQEQIQAMPLADSQAVREQLrqEKALLEEIER 1397
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1398 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFISET 1477
Cdd:PRK11281 129 ---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1478 LR-RMEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAEREAKELQQRM-QEEVVRREEAAVDAQQQK 1552
Cdd:PRK11281 193 QRvLLQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQEAInSKRLTLSEKTVQEAQSQD 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820553714 1553 RS--------IQEELQQLRQSSEAEIQAKAR-------------QAEAAERSRLRIEEEIRVVR 1595
Cdd:PRK11281 270 EAariqanplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1482-1665 |
4.42e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1482 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAV-DAQQQKRSIQEELQ 1560
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIaRAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1561 QLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelqALRAQAEEAEAQKRQAQEEAErlrRQV 1640
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA--------AVAAAIARAKARKAAQQQANA---EPE 670
|
170 180
....*....|....*....|....*
gi 1820553714 1641 QDESQRKRQAEAELAlRVKAEAEAA 1665
Cdd:PRK05035 671 EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1611-1730 |
4.42e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1611 ELQALRAQAEEAEAQKRQAQEEAERLRRQVQdesqrkrqaE-AELALRVKAEAEAAREKQRaLQALEELRLQAEEAERRL 1689
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLE---------ElEAAALQPGEEEELEEERRR-LSNAEKLREALQEALEAL 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1820553714 1690 RQAE---VERARQVQVALETAQRsAEAELQSKRASFAEKTAQLE 1730
Cdd:COG0497 236 SGGEggaLDLLGQALRALERLAE-YDPSLAELAERLESALIELE 278
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1815-2111 |
4.43e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1815 KAEEQAVrhrELAEQELEKQRQLAEGTAQqrlaaeqelIRLRAETEQGEQQRQLLEE--ELARLQHEAAAATQKRQ-ELE 1891
Cdd:COG5185 279 RLNENAN---NLIKQFENTKEKIAEYTKS---------IDIKKATESLEEQLAAAEAeqELEESKRETETGIQNLTaEIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1892 AELAKVRAEMEVLLASKARAEEESRstSEKSKQRLEAEAGRFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERV 1971
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVE--LSKSSEELDSFKDTIESTKES---LDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1972 LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA-----QHKADIEERLAQLRKASDS---EL 2043
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrsvrSKKEDLNEELTQIESRVSTlkaTL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2044 ERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA--EDTLRSKEQAELEAARQRQ 2111
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELiqASNAKTDGQAANLRTAVID 571
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1476-1725 |
4.61e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1555
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1556 QEELQQLRQSSE--AEIQAKARQAEAAERSRLRIEEEI----------------------RVVRL--QLEATERQRGGAE 1609
Cdd:COG1340 81 DELNEKLNELREelDELRKELAELNKAGGSIDKLRKEIerlewrqqtevlspeeekelveKIKELekELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1610 ------GELQALRAQAEEAEAQKRQAQEEAERLRRQVQdesQRKRQAEaelalRVKAEAEAAREK-QRALQALEELRLQA 1682
Cdd:COG1340 161 klkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMI---ELYKEAD-----ELRKEADELHKEiVEAQEKADELHEEI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1820553714 1683 EEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEK 1725
Cdd:COG1340 233 IELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1487-1881 |
4.66e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1487 LAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQE-ELQQLRQ 1564
Cdd:pfam15709 149 RAREGKTEPRLFNQETPASIsHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKsELISKGK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1565 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE---RQRGGAEGELQALRAQAEEAE--AQKRQAQEEAERLRRQ 1639
Cdd:pfam15709 229 KTGAKRKRTQKERNLEVAAELSGPDVINSKETEDASERgafSSDSVVEDPWLSSKYDAEESQvsIDGRSSPTQTFVVTGN 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1640 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQA----LE-ELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1714
Cdd:pfam15709 309 MESEEERSEEDPSKALLEKREQEKASRDRLRAERAemrrLEvERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1715 LQSKRASFAEktaqlERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSL 1794
Cdd:pfam15709 389 IRLRKQRLEE-----ERQRQEEEERKQRLQLQAAQ-------------------ERARQQQEEFRRKLQELQRKKQQEEA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1795 AqaeaekqkeeaerearrrgKAEEQAVRHRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1874
Cdd:pfam15709 445 E-------------------RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
....*..
gi 1820553714 1875 RLQHEAA 1881
Cdd:pfam15709 506 RLALEEA 512
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1526-1664 |
4.68e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1526 EAKELQQRMQEevVRREEAAVDAQQQKRSiQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1605
Cdd:COG0542 412 ELDELERRLEQ--LEIEKEALKKEQDEAS-FERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1606 GGAEGELQALRAQAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEAELALRVKAEAEA 1664
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2826-2863 |
4.71e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 4.71e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1820553714 2826 RHYLQGRSSIAGLLLKPTSEKLSVYAALQRQLLSPGTA 2863
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1667-2064 |
4.81e-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: 42.72 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1667 EKQRALQALEELRLQAEEAERRLRQA-------EVERARQVQVALETAQRsaEAELQSKRASFAEKTAQLERSLQEEHVA 1739
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQRMRELQQQaalaweeLRRRDQKRQETLERERR--LLLQQSQEQWQAEKEQRKARLGREERRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1740 VAQLREEAERRAqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQkslaqaeaekqkeeaerearrrgkaeeq 1819
Cdd:pfam15558 82 ADRREKQVIEKE-----------------SRWREQAEDQENQRQEKLERARQ---------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1820 avrhrelaEQELEKQRQlaegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRA 1899
Cdd:pfam15558 117 --------EAEQRKQCQ------EQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1900 eMEVLLASKARAEEESRSTS-EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAARQRAEAERVLAEK-- 1975
Cdd:pfam15558 183 -RKVLVDCQAKAEELLRRLSlEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRaKWRAEEKEEERQEHKEALAELad 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1976 ---LAAISEATRLKTEAEIALKEKEAENERLRRL----AEDEAFQRRRLEEQAAQHKadiEERLAQLRKASDSELERQKG 2048
Cdd:pfam15558 262 rkiQQARQVAHKTVQDKAQRARELNLEREKNHHIlklkVEKEEKCHREGIKEAIKKK---EQRSEQISREKEATLEEARK 338
|
410
....*....|....*.
gi 1820553714 2049 LVEDTLRQRRQVEEEI 2064
Cdd:pfam15558 339 TARASFHMREKVREET 354
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1363-1691 |
5.13e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1363 ARQRQEQIQAMpLADSQAVREQLRQE-KALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVaspakkpk 1441
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDEL-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1442 vqsgsESVIQEYVDLRTRYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1520
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1521 AQ--------AEREAKELQQRMQEEVVRREEAAVD-AQQQKRSIQEELQQLRQSSEAEIQAKA----------RQAEAAE 1581
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKKyveknlpeieDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1582 RSRLRIEEEIRVV----RLQLEATERQRgGAEGELQALRAQAEEAE---AQKRQA----QEEAERLRRQVQD-ESQRKRQ 1649
Cdd:pfam06160 305 EQNKELKEELERVqqsyTLNENELERVR-GLEKQLEELEKRYDEIVerlEEKEVAyselQEELEEILEQLEEiEEEQEEF 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1820553714 1650 AEAELALRvkaeaeaaREKQRALQALEELRLQAEEAERRLRQ 1691
Cdd:pfam06160 384 KESLQSLR--------KDELEAREKLDEFKLELREIKRLVEK 417
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1628-1707 |
5.45e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 42.09 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1628 QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETA 1707
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAAAAPAADDAEAKKRAIIAAALERARKKKEELAAQ 228
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2079-2498 |
5.56e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.97 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2079 AELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2158
Cdd:COG5278 110 DELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2159 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVARRAAEEAEEARVQAE 2238
Cdd:COG5278 190 ELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2239 REAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQK 2318
Cdd:COG5278 270 LAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2319 AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDN 2398
Cdd:COG5278 350 LLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2399 TQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2478
Cdd:COG5278 430 EALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALL 509
|
410 420
....*....|....*....|
gi 1820553714 2479 QARRLQEDKEQMAQQLAEET 2498
Cdd:COG5278 510 LAAAEAALAAALAAALASAE 529
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1825-1916 |
5.65e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.90 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1825 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVL 1904
Cdd:pfam20492 23 KKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARL 95
|
90
....*....|..
gi 1820553714 1905 LASKARAEEESR 1916
Cdd:pfam20492 96 EEEVERKEEEAR 107
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1528-1743 |
5.65e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1528 KELQQRMQEEvvrreEAAVDAQQQKRSiqEELQQLrQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGG 1607
Cdd:PRK11637 50 KSIQQDIAAK-----EKSVRQQQQQRA--SLLAQL-KKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1608 AEGELqalraqAEEAEAQKRQAQEEAERLRRQVQdESQRKRQAEAELALRVKAEAEAAREKQralQALEELRLQaeeaer 1687
Cdd:PRK11637 122 QERLL------AAQLDAAFRQGEHTGLQLILSGE-ESQRGERILAYFGYLNQARQETIAELK---QTREELAAQ------ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1688 rlrQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1743
Cdd:PRK11637 186 ---KAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSEL 238
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2128-2322 |
5.70e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2128 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQqtlq 2207
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2208 qeqsvldRLRSEAEVARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKL-RKDAEQEAVRR 2286
Cdd:PRK09510 146 -------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEaKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1820553714 2287 AQAEQAALRQKQAAD----AEMEKHKKFAEQTLRQKAQVE 2322
Cdd:PRK09510 219 AAAEAKAAAAKAAAEakaaAEKAAAAKAAEKAAAAKAAAE 258
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1556-1669 |
5.76e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.90 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1556 QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQEEAER 1635
Cdd:pfam20492 8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAE 87
|
90 100 110
....*....|....*....|....*....|....
gi 1820553714 1636 LRRQVQDESQRKRQAEAElALRVKAEAEAAREKQ 1669
Cdd:pfam20492 88 AQEEIARLEEEVERKEEE-ARRLQEELEEAREEE 120
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1482-1669 |
5.81e-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: 43.06 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1482 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER----------EAKELQQRMQEEVVRRE-----EAAV 1546
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegeiEAKEADHKGETEAEEVEhegetEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1547 DAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRAQAEEAE 1623
Cdd:TIGR00927 726 TEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1820553714 1624 AQKRQAQEEAERlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ 1669
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1851-2467 |
5.91e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1851 ELIRLRAETEQGEQQ--RQLLEEELARLQHEAAAATQKRQeLEAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR 1925
Cdd:pfam05557 3 ELIESKARLSQLQNEkkQMELEHKRARIELEKKASALKRQ-LDRESDRNQElqkRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1926 LEAEAGRFRELAEEAARLRALAE----------EAKRQRQLAEEDAARQRAEAERV---LAEKLAAISEATRLKTEAEIA 1992
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREvisclknelsELRRQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1993 LKEKEAENERLRRLAedeafQRRRLEEQAAQHKADIEERLAQLRKAsDSELERQKGLVE---DTLRQRRQVEEEILALKA 2069
Cdd:pfam05557 162 QSSLAEAEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPEL-EKELERLREHNKhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2070 S---FEKAAAGKAELELELgrirsnaedtlrSKEQAELEAARQrqlaaeeEQRRREAEERVQKSLAAEEEAARQRKAALe 2146
Cdd:pfam05557 236 KlerEEKYREEAATLELEK------------EKLEQELQSWVK-------LAQDTGLNLRSPEDLSRRIEQLQQREIVL- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2147 everlkakVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEkahafavqqkeqeLQQTLQQEQSVLDRLRSEAEVARRA 2226
Cdd:pfam05557 296 --------KEENSSLTSSARQLEKARRELEQELAQYLKKIED-------------LNKKLKRHKALVRRLQRRVLLLTKE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2227 AEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAqaraqaqaaaeKLRKDAEQEAVRRAQAEQAALRQKQAADA-EME 2305
Cdd:pfam05557 355 RDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQ-----------KMQAHNEEMEAQLSVAEEELGGYKQQAQTlERE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2306 KHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEAteaARQRSQVEEELFSVRV-QMEELSKLKARi 2384
Cdd:pfam05557 424 LQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMEL---ERRCLQGDYDPKKTKVlHLSMNPAAEAY- 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2385 eaenralilRDKDNTQRFLQEEAEKMKqvaeeaarlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKekmQAVQEATRLKA 2464
Cdd:pfam05557 500 ---------QQRKNQLEKLQAEIERLK-----------------RLLKKLEDDLEQVLRLPETTST---MNFKEVLDLRK 550
|
...
gi 1820553714 2465 EAE 2467
Cdd:pfam05557 551 ELE 553
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1598-1675 |
5.98e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.53 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1598 LEATERqrggAEGELQALRAQAEEAEAQ-KRQAQ---EEAERLRRQVQDESQRKRQAEAElALRVKAEAEAAREKQRALQ 1673
Cdd:PRK05759 44 LAAAER----AKKELELAQAKYEAQLAEaRAEAAeiiEQAKKRAAQIIEEAKAEAEAEAA-RIKAQAQAEIEQERKRARE 118
|
..
gi 1820553714 1674 AL 1675
Cdd:PRK05759 119 EL 120
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1617-1691 |
6.09e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1617 AQAEEAEAQKRQAQEEAERLRRQVQDESQR-----KRQAEAELA-LRVKAEAEAAREKQralQALEELRLQAEEAERRLR 1690
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEiieeaRKEAEKIKEeILAEAKEEAERILE---QAKAEIEQEKEKALAELR 116
|
.
gi 1820553714 1691 Q 1691
Cdd:cd06503 117 K 117
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2241-2418 |
6.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2241 AAQSRRQVEEAERLKQlaeeqaqaraQAQAAAEKLRKDAEQEAVRRAQAEQAAlrQKQAADAEMEKHKKFAEQTLRQKAQ 2320
Cdd:PRK12705 25 LKKRQRLAKEAERILQ----------EAQKEAEEKLEAALLEAKELLLRERNQ--QRQEARREREELQREEERLVQKEEQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2321 VEQELttlrlqlEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEE------LSKLKARIEAENRALILR 2394
Cdd:PRK12705 93 LDARA-------EKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQRVKK 165
|
170 180
....*....|....*....|....*....
gi 1820553714 2395 DKDNTQRFLQEEAEK-----MKQVAEEAA 2418
Cdd:PRK12705 166 IEEEADLEAERKAQNilaqaMQRIASETA 194
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1581-1734 |
6.18e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.71 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1581 ERSRLRIEEEIRvvrlqlEATERQRggaegelqalRAQAEEAEAQKR--QAQEEAERLRRQVQDESQRKRQAEAElalrv 1658
Cdd:PRK07352 49 EERREAILQALK------EAEERLR----------QAAQALAEAQQKlaQAQQEAERIRADAKARAEAIRAEIEK----- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1659 KAEAEAAREKQRALQALEelrlqaEEAERRLRQAeveRARQVQVALEtaqrSAEAELQSKRASFAEKTAqLERSLQ 1734
Cdd:PRK07352 108 QAIEDMARLKQTAAADLS------AEQERVIAQL---RREAAELAIA----KAESQLPGRLDEDAQQRL-IDRSIA 169
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1476-1643 |
6.30e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRA---EERERLAEVEAALEKQRQLAEAHAQ----AKAQAEREAKELqqrmqeevvrreeaavda 1548
Cdd:PRK00409 492 EIAKRLGLPENIIEEAKKligEDKEKLNELIASLEELERELEQKAEeaeaLLKEAEKLKEEL------------------ 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1549 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAersrlrIEEEIRVVRL--QLEATERQRGGAEGELQALRAQAEEAEAQK 1626
Cdd:PRK00409 554 EEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE------ADEIIKELRQlqKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
170
....*....|....*..
gi 1820553714 1627 RQAQEEAERLrrQVQDE 1643
Cdd:PRK00409 628 KKQKEKQEEL--KVGDE 642
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1310-1603 |
6.33e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1310 EVERWRERVAQLLERWQAVLAQTDVRQREL------EQLGRQLRYYRESADPLGAWLQDARQRQEQIQAMPLADSQAVRE 1383
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFdptiadEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1384 QLRQ-----EKALLEEIERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEPVaspaKKPKVQSGSESVIQEyVDLRT 1458
Cdd:pfam02029 140 YQENkwsteVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVK----YESKVFLDQKRGHPE-VKSQN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1459 RYSELTTLTSQYIKFISETLRRMEEEErlaeqqraeERERLAEVEAALEKQRQlaeahaQAKAQAEREAKELQQRMQEEV 1538
Cdd:pfam02029 212 GEEEVTKLKVTTKRRQGGLSQSQEREE---------EAEVFLEAEQKLEELRR------RRQEKESEEFEKLRQKQQEAE 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1539 VRREEAAVDAQQQKRSIQEELQQLRQsseAEIQAKARQAEaaERSRLRieEEIRvvRLQLEATER 1603
Cdd:pfam02029 277 LELEELKKKREERRKLLEEEEQRRKQ---EEAERKLREEE--EKRRMK--EEIE--RRRAEAAEK 332
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1447-1693 |
6.33e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1447 ESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAKAQ 1522
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1523 AEREAKELQQRMQEEVVRREEAAVDAQQQKR--SIQEELQQLRQSSEAEIQAKARQAEAAERSRLR-IEEEIRVVRLQLE 1599
Cdd:COG1340 98 RKELAELNKAGGSIDKLRKEIERLEWRQQTEvlSPEEEKELVEKIKELEKELEKAKKALEKNEKLKeLRAELKELRKEAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1600 ---------ATERQRGGAE-----GELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1665
Cdd:COG1340 178 eihkkikelAEEAQELHEEmielyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
250 260
....*....|....*....|....*...
gi 1820553714 1666 REKQRalqalEELRLQAEEAERRLRQAE 1693
Cdd:COG1340 258 REKEK-----EELEEKAEEIFEKLKKGE 280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1772-1978 |
6.49e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1772 QLKANEALRLRLQAEEVAQQKSLAQAEAE-----KQKEEAEREARRRGKAEEQAvrHRELAEQELEKQRQLAegTAQQRL 1846
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRiraleQELAALEAELAELEKEIAEL--RAELEAQKEELAELLR--ALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1847 AAEQELIRLRAET-EQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1925
Cdd:COG4942 118 RQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820553714 1926 LEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1978
Cdd:COG4942 198 QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2322-2549 |
6.55e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2322 EQELTTLRLQLEETDHQKNLLD-------EELQRLKAEATEAARQRSQVEEELFSVRVQMEELSklKARIEAENRAlilr 2394
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQleldnlrLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEAT--LARVDLEAKI---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2395 dkdntqRFLQEEAEKMKQVAEEaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK- 2473
Cdd:pfam00038 127 ------ESLKEELAFLKKNHEE--EVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKl 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 2474 ELAQEQARRLQEDKEQMAQQLAEETQGFQRtLEAERQRQLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEE 2549
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTIQS-LEIELQSLKKQKASLER---QLAETEERYELQLADYQELISELEA 270
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1825-2021 |
6.85e-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: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1825 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEV 1903
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1904 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAERVLAE----K 1975
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKLRNQltskS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1820553714 1976 LAAISEA---TRLKTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQA 2021
Cdd:pfam09787 160 QSSSSQSeleNRLHQLTE-TLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
185-395 |
6.98e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 42.62 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 185 FTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQIALDYLRHRQVKL 254
Cdd:COG5069 384 FTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGFSL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 255 VNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMVEGY---QGLRCDNFTSSW 324
Cdd:COG5069 462 VGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGLKGdkeEGIRSFGDPAGS 533
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 325 RDGRLFNAIIHRHKPMLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSIITYVSSL 395
Cdd:COG5069 534 VSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVLTFIESL 609
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1921-2068 |
7.15e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1921 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAisEATRLKTE 1988
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1989 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALK 2068
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1608-1699 |
7.25e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.60 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1608 AEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQaeaelALRVKAEAEAAREKQralQALEELRLQAEEAER 1687
Cdd:pfam00430 42 AEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKE-----EIVAAAEAEAERIIE---QAAAEIEQEKDRALA 113
|
90
....*....|..
gi 1820553714 1688 RLRQAEVERARQ 1699
Cdd:pfam00430 114 ELRQQVVALAVQ 125
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1476-1577 |
7.46e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1476 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAKELQQrmqeevvRREEAAVDAQQQKRSI 1555
Cdd:PRK11448 152 LTLKQQLELQAREKAQSQALAEAQQQELVALEG---LAAELEEKQQELEAQLEQLQE-------KAAETSQERKQKRKEI 221
|
90 100
....*....|....*....|....*.
gi 1820553714 1556 QEELQQLRQSSEAE----IQAKARQA 1577
Cdd:PRK11448 222 TDQAAKRLELSEEEtrilIDQQLRKA 247
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1492-1718 |
7.90e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.67 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1492 RAEERERLAE--VEAALEK---QRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsiQEELQQLRQss 1566
Cdd:pfam13779 486 DAERRLRAAQerLSEALERgasDEEIAKLMQELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMT--QQDLQRMLD-- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1567 eaEIQAKARQAEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRAQAEEAEAQKRQAQ--EEAERLRRQVQDES 1644
Cdd:pfam13779 562 --RIEELARSGRRAEAQQML--SQLQQMLENLQAGQPQQQQQQGQSEMQQAMDELGDLLREQQQllDETFRQLQQQGGQQ 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1645 QRKRQAEAELALRV---------------KAEAEAA---REKQRAL-QALEELR-----LQAEEAERRLRQAE--VERAR 1698
Cdd:pfam13779 638 QGQPGQQGQQGQGQqpgqggqqpgaqmppQGGAEALgdlAERQQALrRRLEELQdelkeLGGKEPGQALGDAGraMRDAE 717
|
250 260
....*....|....*....|
gi 1820553714 1699 QvqvALETAQRSAEAELQSK 1718
Cdd:pfam13779 718 E---ALGQGDLAGAVDAQGR 734
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1856-1993 |
7.91e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.17 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1856 RAETEQGEQqrqlleEELARLQHEA--AAATQKRqeleaELAKVRAEMEVLLASKARAEEESRST--------SEKSKQR 1925
Cdd:PRK12472 191 RAETLAREA------EDAARAADEAktAAAAAAR-----EAAPLKASLRKLERAKARADAELKRAdkalaaakTDEAKAR 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 1926 LEAeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKlaaiSEATRLKTEAEIAL 1993
Cdd:PRK12472 260 AEE---RQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKK----AETAKAATDAKLAL 320
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
180-282 |
7.99e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 39.59 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 180 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 255
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1820553714 256 NIRNDDIADGNPKLTLGLIWTIILHFQ 282
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2246-2659 |
8.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2246 RQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADA-EMEKHKKFAEQTLRQKAQVEQE 2324
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2325 LTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFS-----VRVQMEELSKLKARIEAENRALILRDKDNT 2399
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdlaeeLEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2400 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2479
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2480 ARRLQEDKEQMAQQLAEetQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTEL 2559
Cdd:COG4717 311 PALEELEEEELEELLAA--LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-------LEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2560 ATQEkvTLVQTLEIQRQQSDhDAERLREAIAELERE------------KEKLQQEAKLLQLKSEEMQTVQQEQLLQETQA 2627
Cdd:COG4717 382 EDEE--ELRAALEQAEEYQE-LKEELEELEEQLEELlgeleellealdEEELEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430
....*....|....*....|....*....|...
gi 1820553714 2628 LQQ-SFLSEKDSLLQRERFIEQEKAKLEQLFQD 2659
Cdd:COG4717 459 EAElEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
1474-1577 |
8.23e-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: 41.07 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1474 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKA----QAEREAKELQQRMQEEVVRREEAA---- 1545
Cdd:pfam06391 63 VEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRkeekQEEEEEKEKKEKAKQELIDELMTSnkda 142
|
90 100 110
....*....|....*....|....*....|....
gi 1820553714 1546 --VDAQQQKRSIQEELQQLRQSSEAEIQAKARQA 1577
Cdd:pfam06391 143 eeIIAQHKKTAKKRKSERRRKLEELNRVLEQKPT 176
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1245-1743 |
8.34e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1245 HEEQLKEAQAVPATLPELEatkaslkklrAQAEAQQPMFDAlRDElrGAQEVGERLQQRHGERDVEVERWrERVAQLLEr 1324
Cdd:pfam10174 125 HERQAKELFLLRKTLEEME----------LRIETQKQTLGA-RDE--SIKKLLEMLQSKGLPKKSGEEDW-ERTRRIAE- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1325 WQAVLAQTDVrqrELEQLGRQLRYYRESAdplgawlqdarQRQEQIQAMPlADSQAVREQLRQEKALLEEIERHGEKVEE 1404
Cdd:pfam10174 190 AEMQLGHLEV---LLDQKEKENIHLREEL-----------HRRNQLQPDP-AKTKALQTVIEMKDTKISSLERNIRDLED 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1405 CQRFAKQyiNAIKDYELQLVTYKaQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSELTTLTS------QYIKFISE 1476
Cdd:pfam10174 255 EVQMLKT--NGLLHTEDREEEIK-QMEVYKSHSKfmKNKIDQLKQELSKKESELLALQTKLETLTNqnsdckQHIEVLKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1477 TLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQA-------------EREAKELQQRMQ--EEVVR 1540
Cdd:pfam10174 332 SLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEKSTLAgeirdlkdmldvkERKINVLQKKIEnlQEQLR 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1541 reeaavDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEA-------AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ 1613
Cdd:pfam10174 412 ------DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAlsekeriIERLKEQREREDRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1614 ALRAQAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALEELRLQAEEAER-RLRQA 1692
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQ 565
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820553714 1693 EV----ERARQVQVALE---TAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1743
Cdd:pfam10174 566 EVarykEESGKAQAEVErllGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI 623
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2430-2605 |
8.41e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2430 LRQLAEEDLAQQRALAEKMLKEkmqavqeatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAER 2509
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2510 QRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAI 2589
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEA 171
|
170
....*....|....*.
gi 1820553714 2590 AELEREKEklqQEAKL 2605
Cdd:PRK12704 172 AVLIKEIE---EEAKE 184
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1665-1719 |
8.56e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820553714 1665 AREKQRALQaleelRLQAEEAERRlRQAEVERARQVQVALETAQRS-AEAELQSKR 1719
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| FliH |
COG1317 |
Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular ... |
1481-1608 |
8.78e-03 |
|
Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440928 [Multi-domain] Cd Length: 172 Bit Score: 40.29 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1481 MEEEERLAEQQRAEERE------RLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVR----------REEA 1544
Cdd:COG1317 1 MEELEALREEAREEGYAegyeegLEEGRAEAEAEIAEALEQLQALLEQLQAPLEELDEELEEELVElalaiarkviGREL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820553714 1545 AVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlRIEEEIRVVRLQLEATER-QRGGA 1608
Cdd:COG1317 81 ALDPEAILALVREALAALREAEEVTIRVNPDDLELVRE---ALDELLGEGGWRLVADPSlARGGC 142
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
659-753 |
9.12e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 38.85 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 659 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQL---SPATRGAYRDCLGRLD 735
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1820553714 736 LQYAKLLNSSKARLRSLE 753
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1906-2334 |
9.31e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1906 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAISEAtR 1984
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERlAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKK-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1985 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEI 2064
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2065 LALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEEQRRREAEERVQKSLAAEEEAArqRKAA 2144
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA--LAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2145 LEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDRLRSEAEVAR 2224
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 2225 RAAEEAEEARVQAEREAAQSRRQVEEAERLKQLAEEQAQARAQAQAAAEKLRKDAEQEAVRRAQAEQAALRQKQAADAEM 2304
Cdd:COG3064 318 LAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGG 397
|
410 420 430
....*....|....*....|....*....|
gi 1820553714 2305 EKHKKFAEQTLRQKAQVEQELTTLRLQLEE 2334
Cdd:COG3064 398 GGLLGLRLDLGAALLEAASAVELRVLLALA 427
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1606-1735 |
9.39e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820553714 1606 GGAEGELQALRAQAEEAEAQKRQAQEEAERLRRQVQDESQrkrqaeaelalrvkAEAEAAREKQRALQALEELRLQAEEa 1685
Cdd:PRK12705 19 GVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK--------------ELLLRERNQQRQEARREREELQREE- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1820553714 1686 ERRLRQAEVERARQVQVALETAQRS-AEAELQSKRASFAEKTAQLERSLQE 1735
Cdd:PRK12705 84 ERLVQKEEQLDARAEKLDNLENQLEeREKALSARELELEELEKQLDNELYR 134
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4418-4448 |
9.88e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.88e-03
10 20 30
....*....|....*....|....*....|.
gi 1820553714 4418 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4448
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| |
