|
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 ... |
1149-1256 |
3.72e-74 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 243.08 E-value: 3.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1149 DRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKL 1228
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIK---ARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKL 77
|
90 100
....*....|....*....|....*...
gi 1838104091 1229 VNIRNDDIADGNPKLTLGLIWTIILHFQ 1256
Cdd:cd21188 78 VNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1146-1267 |
8.01e-70 |
|
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: 231.07 E-value: 8.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1146 DERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 1225
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK---AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1838104091 1226 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGLSE 1267
Cdd:cd21235 78 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1146-1264 |
7.27e-68 |
|
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: 226.02 E-value: 7.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1146 DERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 1225
Cdd:cd21236 12 DERDKVQKKTFTKWINQHLMK---VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQ 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 1838104091 1226 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQING 1264
Cdd:cd21236 89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTG 127
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1269-1374 |
4.09e-63 |
|
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: 211.42 E-value: 4.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1269 MTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLD 1348
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1838104091 1349 PEDVDVPHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
1270-1374 |
4.13e-62 |
|
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: 208.40 E-value: 4.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDP 1349
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1838104091 1350 EDVDVPHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1146-1266 |
2.75e-59 |
|
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: 201.03 E-value: 2.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1146 DERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 1225
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK---VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1838104091 1226 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGLS 1266
Cdd:cd21237 78 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1270-1374 |
2.05e-55 |
|
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: 189.43 E-value: 2.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERdLGVTRLLDP 1349
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1838104091 1350 EDVDVPHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1268-1374 |
1.83e-49 |
|
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: 172.53 E-value: 1.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1268 DMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERdLGVTRLL 1347
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1838104091 1348 DPEDVDVPHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1151-1257 |
2.60e-49 |
|
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: 171.80 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1151 VQKKTFTKWVNKHLIKraESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLVN 1230
Cdd:cd21186 2 VQKKTFTKWINSQLSK--ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVN 79
|
90 100
....*....|....*....|....*..
gi 1838104091 1231 IRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21186 80 ISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-100 |
1.18e-47 |
|
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.
Pssm-ID: 427337 Cd Length: 92 Bit Score: 166.54 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 7 MPLKDLRAIYELLFKDGVMVAKKDkRPQIKHPEIEsVSNLQVMRAMVSLKSRGYVKETFSWRHFYWYLTNEGIVYLRDYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPELN-VPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|....
gi 1838104091 87 RLPSEIVPASLQRT 100
Cdd:pfam03501 79 HLPAEIVPATLKRS 92
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1270-1370 |
5.54e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.20 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDP 1349
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1838104091 1350 EDVDVPHPDEKSIITYVSSLY 1370
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1146-1253 |
7.22e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 162.54 E-value: 7.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1146 DERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHR 1224
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHL---ARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQ 87
|
90 100
....*....|....*....|....*....
gi 1838104091 1225 QVKLVNIRNDDIADGNPKLTLGLIWTIIL 1253
Cdd:cd21246 88 RVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1270-1370 |
5.58e-45 |
|
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: 159.48 E-value: 5.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDP 1349
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1838104091 1350 EDVDVPHPDEKSIITYVSSLY 1370
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
1147-1257 |
8.08e-45 |
|
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: 159.46 E-value: 8.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1147 ERDRVQKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHKLQNVQIALDFLRHR 1224
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPPMK-VEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESK 79
|
90 100 110
....*....|....*....|....*....|...
gi 1838104091 1225 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21241 80 KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
1147-1257 |
1.35e-42 |
|
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: 153.11 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1147 ERDRVQKKTFTKWVNKHLIKRAeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHKLQNVQIALDFLRHR 1224
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLS-QPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKR 79
|
90 100 110
....*....|....*....|....*....|...
gi 1838104091 1225 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21190 80 CIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1144-1253 |
8.60e-42 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 150.91 E-value: 8.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1144 IEDERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLr 1222
Cdd:cd21193 9 LQEERINIQKKTFTKWINSFLEK---ANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL- 84
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1223 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1253
Cdd:cd21193 85 KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1145-1370 |
9.23e-42 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 165.88 E-value: 9.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1145 EDERDRVQKKTFTKWVNKHLIKRAESQhhVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLR 1222
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGGQKE--FGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1223 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQingLSEDMTAKEKLLCWSQRMTDGYQN-IRCDNFTTSWRDG 1301
Cdd:COG5069 81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 1302 KLFNAVIHKHHPRLIDMGRV-YQQSNQE-NLEQAFNVAERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 1370
Cdd:COG5069 158 LAFSALIHDSRPDTLDPNVLdLQKKNKAlNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
1266-1376 |
5.93e-41 |
|
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: 148.23 E-value: 5.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1266 SEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTR 1345
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1346 LLDPEDVDVPHPDEKSIITYVSSLYDVMPRM 1376
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKM 111
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1123-1253 |
6.31e-40 |
|
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: 146.35 E-value: 6.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1123 SSDEEWDHSLDEPE--EKTWPHFIEDERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLP 1200
Cdd:cd21317 1 LADDDWDNDNSSARlfERSRIKALADEREAVQKKTFTKWVNSHL---ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 1201 R-EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1253
Cdd:cd21317 78 KpTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1144-1253 |
3.31e-39 |
|
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: 144.40 E-value: 3.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1144 IEDERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLR 1222
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHL---ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1223 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1253
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1269-1370 |
1.35e-38 |
|
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: 141.54 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1269 MTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLD 1348
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1838104091 1349 PEDVDVPHPDEKSIITYVSSLY 1370
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1266-1376 |
1.50e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 141.73 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1266 SEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTR 1345
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1346 LLDPEDVDVPHPDEKSIITYVSSLYDVMPRM 1376
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKM 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
1269-1374 |
2.53e-38 |
|
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: 140.53 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1269 MTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLD 1348
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1838104091 1349 PEDVDVPHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
1257-1370 |
2.78e-38 |
|
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: 140.58 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1257 ISDIQInglsEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNV 1336
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1838104091 1337 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
1147-1257 |
4.70e-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: 139.97 E-value: 4.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1147 ERDRVQKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQV 1226
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV-VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSI 79
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21242 80 KLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
2007-2084 |
1.59e-37 |
|
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: 136.96 E-value: 1.59e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 2007 LSWQYLMRDFKLIRSWNIIMLKSMKPEEYRLMMRNLELHYQDYMRESQDSQLFGPDDRMQVEGDFTNSTQHFDSLLRS 2084
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1273-1374 |
5.53e-37 |
|
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: 136.79 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1273 EK-LLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED 1351
Cdd:cd21187 2 EKtLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1838104091 1352 VDVPHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1151-1255 |
8.29e-37 |
|
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: 136.38 E-value: 8.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1151 VQKKTFTKWVNKHLIKRAESqhhVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLRHRQVKL 1228
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLS---ITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKL 80
|
90 100
....*....|....*....|....*..
gi 1838104091 1229 VNIRNDDIADGNPKLTLGLIWTIILHF 1255
Cdd:cd21215 81 TNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-133 |
1.06e-36 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 136.69 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 5 MLMPLKDLRAIYELLFKDGVMVAKKDkRPQIKHPEIEsVSNLQVMRAMVSLKSRGYVKETFSWRHFYWYLTNEGIVYLRD 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKD-PKGPWHPELN-VPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1838104091 85 YLRLPSEIVPAslqrtrkpaatmTFAQQAARVQTVEGPTSYVPKPGRRG 133
Cdd:PTZ00034 80 YLHLPPDVFPA------------THKKKSVNFERKTEEEGSRGGRGGRG 116
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
1149-1253 |
1.99e-36 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 135.21 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1149 DRVQKKTFTKWVNKHLIKRAESqhhVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 1227
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQ---IENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVK 79
|
90 100
....*....|....*....|....*.
gi 1838104091 1228 LVNIRNDDIADGNPKLTLGLIWTIIL 1253
Cdd:cd21214 80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1270-1376 |
9.88e-36 |
|
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: 133.30 E-value: 9.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDP 1349
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|....*..
gi 1838104091 1350 EDVDVPHPDEKSIITYVSSLYDVMPRM 1376
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYYHYFSKM 108
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1254-1376 |
1.93e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 133.26 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1254 HFQISDIQINGLSEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQA 1333
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1838104091 1334 FNVAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDVMPRM 1376
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKM 123
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2472-3714 |
2.50e-35 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 149.98 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2472 AKILKAEEQKKMADLQAELDK-QKKLAEAHAKAIAKAEKEADELKHQMKQEVSKRevaaldaenqKKNIELELHE----- 2545
Cdd:NF041483 85 ADQLRADAERELRDARAQTQRiLQEHAEHQARLQAELHTEAVQRRQQLDQELAER----------RQTVESHVNEnvawa 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2546 --LKKLSEQQindKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETElkqlrEKAAEAERLRKLAQEEAEKLHKQ 2623
Cdd:NF041483 155 eqLRARTESQ---ARRLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAE-----SARAEAEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2624 VIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQaeEAERKVKQAQIEKEKQIQIAHVAAEKS-ATAELQST 2702
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAAKQlASAESANE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2703 QRSfveKTSKLEeslkqehgtVLQLQQEAAhlkkqqEDALKAREEAEKELDKWRQkanEALRLRLQAEEEAhkKSLAQEE 2782
Cdd:NF041483 305 QRT---RTAKEE---------IARLVGEAT------KEAEALKAEAEQALADARA---EAEKLVAEAAEKA--RTVAAED 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2783 AEKQKEEAEREAKK-RAKAEESALKQKEMAEKELERQRKvadstaqqklTAEQELIRLRAE-FDNAEQQRSLLEDELYRL 2860
Cdd:NF041483 362 TAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRR----------EAEAEADRLRGEaADQAEQLKGAAKDDTKEY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2861 KNEVIAAQQQRKQLEDELAKMRSE-MEILIQLKSRAEKETMSNTEkskmlldaEASKmrdVAEEA-GKLRAIAEEAkyqR 2938
Cdd:NF041483 432 RAKTVELQEEARRLRGEAEQLRAEaVAEGERIRGEARREAVQQIE--------EAAR---TAEELlTKAKADADEL---R 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2939 QIAEEEAARQRAEAerilkeklaaISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQ 3018
Cdd:NF041483 498 STATAESERVRTEA----------IERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIA 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3019 LKKS----------------------------SQAEMQRQKAmVDDTLKQRRVVEEEIRILKLNFEK------------A 3058
Cdd:NF041483 568 ARQAeaaeeltrlhteaeerltaaeealadarAEAERIRREA-AEETERLRTEAAERIRTLQAQAEQeaerlrteaaadA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3059 SSGKLDLELELNKLKN-IAEETQQSKLRAEEEAEKQRklAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELD---- 3133
Cdd:NF041483 647 SAARAEGENVAVRLRSeAAAEAERLKSEAQESADRVR--AEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGsara 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3134 -------RLKKKAEE----ARKQKDKADSEAEKQIVAASQAALKCRTAEQQVqsvlAQQKEDSM--MHKKLQQEYEKakk 3200
Cdd:NF041483 725 eadqereRAREQSEEllasARKRVEEAQAEAQRLVEEADRRATELVSAAEQT----AQQVRDSVagLQEQAEEEIAG--- 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3201 lakeaeaakekaekeavlLRKQAEEAesqkaaaekEAAIQAKAQEDAERLRKEAEfeaAKRAQAENAALEQKKKADAEMA 3280
Cdd:NF041483 798 ------------------LRSAAEHA---------AERTRTEAQEEADRVRSDAY---AERERASEDANRLRREAQEETE 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3281 KHKKLAEQTLKQKFQvEQEltkvKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVK----VQMEELLKvk 3356
Cdd:NF041483 848 AAKALAERTVSEAIA-EAE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIG-- 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3357 lKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAA-----ILSVESQEASRLRQIAEEDLVQQRALAEKMLKekmqai 3431
Cdd:NF041483 921 -EATSEAERLTAEARAEAERLRDEARAEAERVRADAAaqaeqLIAEATGEAERLRAEAAETVGSAQQHAERIRT------ 993
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3432 qEASRLKAEAEL-LQRQKDLAQEQAQRLL-EDKELMQKRLDEETEEYQKSLEaerkrqlEIVAEAEKLklqvsqLSVAQA 3509
Cdd:NF041483 994 -EAERVKAEAAAeAERLRTEAREEADRTLdEARKDANKRRSEAAEQADTLIT-------EAAAEADQL------TAKAQE 1059
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3510 KAEEEAKRFKKQADNI--AARlLETEIATKDkSTVMQQLEVERRNNskEADDL-----RNAIANLE-TE--KARLKKDAE 3579
Cdd:NF041483 1060 EALRTTTEAEAQADTMvgAAR-KEAERIVAE-ATVEGNSLVEKART--DADELlvgarRDATAIRErAEelRDRITGEIE 1135
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3580 ELQNKSKEMADAQMKQI-EHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKK 3658
Cdd:NF041483 1136 ELHERARRESAEQMKSAgERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAE 1215
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3659 KLHAtmdEAlskQKEAEREMLNKQKEMQELEKKRleqEKVLAEENkKLRDQLQQLE 3714
Cdd:NF041483 1216 KIKA---EA---EAEAKRTVEEGKRELDVLVRRR---EDINAEIS-RVQDVLEALE 1261
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1146-1257 |
3.40e-35 |
|
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: 131.97 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1146 DERDRVQKKTFTKWVNKHLIKRAesQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 1225
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFG--KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNN 78
|
90 100 110
....*....|....*....|....*....|..
gi 1838104091 1226 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21231 79 VDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2593-3165 |
1.29e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.54 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREKAAEAERLRKLaQEEAEKLHKQVIeeTQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLkmQAEEAERK 2672
Cdd:COG1196 199 ERQLEPLERQAEKAERYREL-KEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAEL--EAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2673 VKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKEL 2752
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2753 DKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTA 2832
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2833 EQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEmeiliQLKSRAEKETMSNTEKSKMLLDA 2912
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE-----LAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2913 EASKMRDVAEEAGKLRAIAE----EAKYQRQIAEEEAAR--------QRAEAERILKEKLAAISEATRLkteAEIALKEK 2980
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVligvEAAYEAALEAALAAAlqnivvedDEVAAAAIEYLKAAKAGRATFL---PLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2981 EAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASS 3060
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3061 GKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRklameeekrrreaeetvkkitAAEKEAGRQRKIAQDELDRLKKKAE 3140
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEAL---------------------LAEEEEERELAEAEEERLEEELEEE 724
|
570 580
....*....|....*....|....*
gi 1838104091 3141 EARKQKDKADSEAEKQIVAASQAAL 3165
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLE 749
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2355-3114 |
5.43e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 142.59 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2355 QAVSITDSKTLKEQLSQEKKLLEEIENN--KENVDECQKYAKAYINSIKDYElqlvaynakadphaSPLKKNKMDSASDN 2432
Cdd:PTZ00121 1022 QNFNIEKIEELTEYGNNDDVLKEKDIIDedIDGNHEGKAEAKAHVGQDEGLK--------------PSYKDFDFDAKEDN 1087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2433 IIQEyvtlrtRYSELMTLTSQYIKFITEtqrRLEDEEKAAKILK-------AEEQKKMADLQaELDKQKKLAEAHAKAIA 2505
Cdd:PTZ00121 1088 RADE------ATEEAFGKAEEAKKTETG---KAEEARKAEEAKKkaedarkAEEARKAEDAR-KAEEARKAEDAKRVEIA 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2506 KAEKEADELKHQMKQEVSKREVAALDAENQKKNIEL-------------------ELHELKKLSEQQINDKSQLVDDALQ 2566
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELrkaedarkaeaarkaeeerKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2567 SRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTaeEELKRKSEAEK 2646
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAK 1315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2647 EAAKQKQKALED---LENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQ--RSFVEKTSKLEESLKQEh 2721
Cdd:PTZ00121 1316 KADEAKKKAEEAkkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEakKKADAAKKKAEEKKKAD- 1394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2722 gtvlQLQQEAAHLKKQQEDaLKAREEAEKELDKWRQKANE---ALRLRLQAEE-----EAHKKS-----LAQEEAEKQKE 2788
Cdd:PTZ00121 1395 ----EAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEakkadEAKKKAeeakkAEEAKKKAEEA 1469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2789 EAEREAKKRA-----------KAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQ----ELIRLRAEFDNAEQQR--- 2850
Cdd:PTZ00121 1470 KKADEAKKKAeeakkadeakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkaEEAKKADEAKKAEEKKkad 1549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2851 SLLEDELYRLKNEVIAAQQQRKQLEDELAKMRsEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAI 2930
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2931 AEEAKYQRQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEialkEKEAENERLRRAAEDEayqRKAleDEANQHKK 3010
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDE---KKA--AEALKKEA 1698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3011 EIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDlELELNKLKNIA--EETQQSKLRAEE 3088
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKkeEEKKAEEIRKEK 1777
|
810 820
....*....|....*....|....*.
gi 1838104091 3089 EAEKQRKLAMEEEKRRREAEETVKKI 3114
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2460-3095 |
2.13e-32 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 139.69 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2460 ETQRRLEDEEkaAKILKAEeqkkmaDLQAELDKQ-KKLA-EAhakaiAKAEKeADELKHQMKQevSKREVAALDAENQKK 2537
Cdd:COG1196 176 EAERKLEATE--ENLERLE------DILGELERQlEPLErQA-----EKAER-YRELKEELKE--LEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2538 NIELELHELKKLSEQqindksqlvddalqsrtkieeeihiiriqLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEA 2617
Cdd:COG1196 240 ELEELEAELEELEAE-----------------------------LEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2618 EKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLkmQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATA 2697
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL--EEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2698 ELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKS 2777
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2778 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQR------- 2850
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavav 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2851 -SLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRA 2929
Cdd:COG1196 529 lIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2930 IAEEAKYQRQIAE-----------EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQR 2998
Cdd:COG1196 609 READARYYVLGDTllgrtlvaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2999 KALEDEANQHKKEIEEKIVQLKKsSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKAssgkLDLELELNKLKNIAEE 3078
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAE-AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL----LEEEALEELPEPPDLE 763
|
650
....*....|....*..
gi 1838104091 3079 TQQSKLraeEEAEKQRK 3095
Cdd:COG1196 764 ELEREL---ERLEREIE 777
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1126-1253 |
6.89e-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: 124.00 E-value: 6.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1126 EEWDHSLDEPE--EKTWPHFIEDERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-E 1202
Cdd:cd21316 26 DEWDNENSSARlfERSRIKALADEREAVQKKTFTKWVNSHL---ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpT 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 1203 KGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1253
Cdd:cd21316 103 KGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
1269-1367 |
1.01e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 121.76 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1269 MTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLD 1348
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1838104091 1349 PEDVDVPHPDEKSIITYVS 1367
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1275-1375 |
1.13e-31 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 121.57 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1275 LLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRV-YQQSNQENLEQAFNVAERDLGVTRLLDPEDVD 1353
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVvSQQSATERLDHAFNIARQHLGIEKLLDPEDVA 84
|
90 100
....*....|....*....|..
gi 1838104091 1354 VPHPDEKSIITYVSSLYDVMPR 1375
Cdd:cd21233 85 TAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1151-1257 |
1.24e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 121.63 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1151 VQKKTFTKWVNKHLIKRAESqhhVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLRHRQVKL 1228
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMS---VEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKL 80
|
90 100
....*....|....*....|....*....
gi 1838104091 1229 VNIRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21227 81 VNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
1269-1367 |
5.68e-31 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 119.55 E-value: 5.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1269 MTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLD 1348
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1838104091 1349 PEDVDVPHPDEKSIITYVS 1367
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1151-1257 |
6.03e-31 |
|
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: 119.34 E-value: 6.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1151 VQKKTFTKWVNKHLIKRAESQhhVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLVN 1230
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKPP--IKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVN 79
|
90 100
....*....|....*....|....*..
gi 1838104091 1231 IRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21232 80 IGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1147-1259 |
8.74e-31 |
|
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: 119.22 E-value: 8.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1147 ERDRVQKKTFTKWVNKHLiKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHKLQNVQIALDFLRHR 1224
Cdd:cd21191 1 ERENVQKRTFTRWINLHL-EKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDS 79
|
90 100 110
....*....|....*....|....*....|....*
gi 1838104091 1225 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 1259
Cdd:cd21191 80 NVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1257-1370 |
3.67e-30 |
|
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: 117.63 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1257 ISDIQinglSEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNV 1336
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1838104091 1337 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 1370
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2745-3352 |
7.35e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.60 E-value: 7.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQkaNEAlRLR-LQAEEEAHKKSLaqeeaekqkeeaEREAKK----RAKAEESALKQKEMAEKELERQR 2819
Cdd:COG1196 174 KEEAERKLEATEE--NLE-RLEdILGELERQLEPL------------ERQAEKaeryRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2820 KVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKET 2899
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2900 MSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKyQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKE 2979
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELE-EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2980 KEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAmvdDTLKQRRVVEEEIRILKLNFEKAS 3059
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE---EAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3060 SGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKI--------TAAEKEAGRQRKIAQDE 3131
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigveaayeAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3132 LDRLKKKAEEARKQKDKADSE----AEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEA 3207
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3208 AKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAE 3287
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 3288 QTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 3352
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2892-3734 |
8.22e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 132.19 E-value: 8.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2892 KSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKlraiAEEAKYQRQIAEEEAARQRAEAERILKEKLAaisEATRLKT 2971
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDARKAEEARK----AEDAKRVEIARKAEDARKAEEARKAEDAKKA---EAARKAE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2972 EAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEE--KIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIR 3049
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3050 ILKLNFEKASSGKLDLELELNKLKNIAEETQQSK-LRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRqrkia 3128
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEeKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE----- 1340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3129 qdeldrlKKKAEEARKQKDKAdseaekqivaasqAALKCRTAEQQVQsvlAQQKEDSMMHKKLQQeyekakklakeaeaa 3208
Cdd:PTZ00121 1341 -------AKKAAEAAKAEAEA-------------AADEAEAAEEKAE---AAEKKKEEAKKKADA--------------- 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3209 kekaekeavlLRKQAEEaesqkaaaekeaaiqakaQEDAERLRKEAEfEAAKRAQAENAALEQKKKADaemaKHKKLAEQ 3288
Cdd:PTZ00121 1383 ----------AKKKAEE------------------KKKADEAKKKAE-EDKKKADELKKAAAAKKKAD----EAKKKAEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3289 TLKQkfqveqeltkvklklddtdkqkdlldDELQRLKDEVDDAVKQRGQVEEelfkvKVQMEELLKVKLKIEKENQLLIK 3368
Cdd:PTZ00121 1430 KKKA--------------------------DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKKKAEEAKKADEAKKK 1478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3369 KDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLK----EKMQAIQEASRLKAEAELL 3444
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELK 1558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3445 QRQKDLAQEQAQRLLEDKELMQKRLDEeteeyqkSLEAERKRqleiVAEAEKLKLQVSQLSVAQAKAEEEAKrfkkqadn 3524
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEE-------AKKAEEAR----IEEVMKLYEEEKKMKAEEAKKAEEAK-------- 1619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3525 IAARLLETEIATKDKSTVMQQLEVERRnnsKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQ 3604
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3605 QTFLTEKEMLLKKERLiEDEKKRLESQYEEEAKKAKAltdeqERQRKLMEEEKKKlhatMDEALSKQKEAEREMLNKQKE 3684
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEA-EEKKKAEELKKAEEENKIKA-----EEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEE 1766
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3685 MQELEKKRLEQEKVLAEENKKlRDQLQQLEEAQKEKNTQVISAATVETTK 3734
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDE-EDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1275-1374 |
1.62e-29 |
|
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: 115.44 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1275 LLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPEDVDV 1354
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVAV 84
|
90 100
....*....|....*....|
gi 1838104091 1355 PHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21234 85 QLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1150-1258 |
2.83e-29 |
|
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: 115.24 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1150 RVQKKTFTKWVNKHLIKRAEsqhHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHKLQNVQIALDFLRHRQ-V 1226
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANK---HIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgI 90
|
90 100 110
....*....|....*....|....*....|..
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1258
Cdd:cd21311 91 KIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2650-3691 |
4.79e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 129.49 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2650 KQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQStqrsfvEKTSKLEESLKQEHGTVLQlQQ 2729
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATE------EAFGKAEEAKKTETGKAEE-AR 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2730 EAAHLKKQQEDALKAREEaekeldkwrQKANEALRLrlqaeEEAHKkslaqeeaekQKEEAEREAKKRA----KAEESal 2805
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEA---------RKAEDARKA-----EEARK----------AEDAKRVEIARKAedarKAEEA-- 1169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2806 KQKEMAEKELERQRKVADSTAQQKLTAEQelIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEM 2885
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRKAED--ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2886 EILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAiAEEAKYQRQIAEEEAARQRAEAERILKEklaAISE 2965
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK-ADEAKKAEEKKKADEAKKKAEEAKKADE---AKKK 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2966 ATRLKTEAEiALKEKEAENERLRRAAEDEAyQRKALEDEANQHKKEIEEKivqlkkssQAEMQRQKAmvdDTLKQRrvvE 3045
Cdd:PTZ00121 1324 AEEAKKKAD-AAKKKAEEAKKAAEAAKAEA-EAAADEAEAAEEKAEAAEK--------KKEEAKKKA---DAAKKK---A 1387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3046 EEIRilklnfekassgkldlelELNKLKNIAEEtqqSKLRAEEeaekqrklameeekrrreaeetVKKITAAEKEAGRQR 3125
Cdd:PTZ00121 1388 EEKK------------------KADEAKKKAEE---DKKKADE----------------------LKKAAAAKKKADEAK 1424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3126 KIAQD--ELDRLKKKAEEARKQKD-KADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSmmhkklqqeyekakkla 3202
Cdd:PTZ00121 1425 KKAEEkkKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE----------------- 1487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3203 keaeaakekaekeavlLRKQAEEAESQKAAAEKEAAIQAKAQE--DAERLRKEAEF---EAAKRAQAENAALEQKKKADA 3277
Cdd:PTZ00121 1488 ----------------AKKKAEEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAkkaEEAKKADEAKKAEEKKKADEL 1551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3278 EMAKHKKLAEQTLK--QKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEElfkVKVQMEELLKV 3355
Cdd:PTZ00121 1552 KKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE---AKIKAEELKKA 1628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3356 KLKIEKENQLLIK--KDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQiAEEDlvqQRALAEKMLKEKMQAIQE 3433
Cdd:PTZ00121 1629 EEEKKKVEQLKKKeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK-AEED---EKKAAEALKKEAEEAKKA 1704
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3434 ASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQkrldEETEEYQKSLEAErkrqleiVAEAEKLKlqvsqlsVAQAKAEE 3513
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKK----EAEEDKKKAEEAK-------KDEEEKKK-------IAHLKKEE 1766
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3514 EAKRFKKQADNIAarLLETEIATKDKSTVMqqlEVERRNNSKEaDDLRNAIANLETEKARLKKDAEELQNKSKEMADAQM 3593
Cdd:PTZ00121 1767 EKKAEEIRKEKEA--VIEEELDEEDEKRRM---EVDKKIKDIF-DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKN 1840
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3594 KQIEHEKTMLQQTFLTEKEMLL--KKERLIEDEKKRLESQYEE--EAKKAKALTDEQERQRKLMEEEKKKLHATMDEALS 3669
Cdd:PTZ00121 1841 MQLEEADAFEKHKFNKNNENGEdgNKEADFNKEKDLKEDDEEEieEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLD 1920
|
1050 1060
....*....|....*....|..
gi 1838104091 3670 KQKEAEREMLNKQKEMQELEKK 3691
Cdd:PTZ00121 1921 KDEYIKRDAEETREEIIKISKK 1942
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1275-1370 |
1.51e-28 |
|
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: 112.44 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1275 LLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED-VD 1353
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1838104091 1354 VPHPDEKSIITYVSSLY 1370
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1150-1255 |
2.06e-28 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 112.19 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1150 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 1226
Cdd:cd21183 3 RIQANTFTRWCNEHL---KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHI 79
|
90 100
....*....|....*....|....*....
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHF 1255
Cdd:cd21183 80 KLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2424-3187 |
2.37e-28 |
|
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: 126.71 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2424 NKMDSASDNIIQEYVTLRTRYSELMTLTSQYIKfiTETQRRLEDEEKAAKIL-----KAEEQKKMADLQAELDKQKKLAE 2498
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEK--AERYKELKAELRELELAllvlrLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2499 AHAKAIAKAEKEADELKHQMkQEVSKrEVAALDAENQKKNIELEL--HELKKLSEQQINDKSQLV------DDALQSRTK 2570
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEV-SELEE-EIEELQKELYALANEISRleQQKQILRERLANLERQLEeleaqlEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2571 IEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAK 2650
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2651 QKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHgtvlQLQQE 2730
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA----QLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2731 AAHLKKQQEDALKAREEAEKELD--------------------KWRQKANEALRLRLQAeeeahkkslaqeeaekqkeeA 2790
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKnqsglsgilgvlselisvdeGYEAAIEAALGGRLQA--------------------V 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2791 EREAKKRAKAEESALKQKE-----MAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLK--NE 2863
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNElgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2864 VIAAQQQRKQLEDELAKMRSEMEIL----IQLKSRAEKEtMSNTEKSKMLLDAEAsKMRDVAEEAGKLRAIAEEAKYQRQ 2939
Cdd:TIGR02168 631 LDNALELAKKLRPGYRIVTLDGDLVrpggVITGGSAKTN-SSILERRREIEELEE-KIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2940 IAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEdEANQHKKEIEEKIVQL 3019
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3020 kkssQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAME 3099
Cdd:TIGR02168 788 ----EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3100 EEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLA 3179
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
....*...
gi 1838104091 3180 QQKEDSMM 3187
Cdd:TIGR02168 944 RLSEEYSL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2604-3504 |
4.65e-28 |
|
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: 125.94 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2604 AEAERLRKLAQEEA--EKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQkqkaledLENLKMQAEEAERKvkQAQIEKE 2681
Cdd:TIGR02168 152 AKPEERRAIFEEAAgiSKYKERRKETERKLERTRENLDRLEDILNELERQ-------LKSLERQAEKAERY--KELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2682 KQIQIAHVAAEKsataelqstqRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANE 2761
Cdd:TIGR02168 223 RELELALLVLRL----------EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2762 ALRL--RLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRakaeesalkQKEMAEKELERQRKVADSTAQQKLTAEQELIRL 2839
Cdd:TIGR02168 293 LANEisRLEQQKQILRERLANLERQLEELEAQLEELES---------KLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2840 RAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEiliQLKSRAEKETmsnTEKSKMLLDAEASKMRD 2919
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQ---QEIEELLKKLEEAELKE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2920 VAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAlkekeaenERLRRAAEDEAYQRK 2999
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL--------ERLQENLEGFSEGVK 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3000 ALEDEANQ---HKKEIEEKIVQLKKSSQA-----EMQRQKAMVDDTLKQRRVVE--EEIRILKLNF--EKASSGKLDLEL 3067
Cdd:TIGR02168 510 ALLKNQSGlsgILGVLSELISVDEGYEAAieaalGGRLQAVVVENLNAAKKAIAflKQNELGRVTFlpLDSIKGTEIQGN 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3068 ELNKLKNIaeETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKK---------K 3138
Cdd:TIGR02168 590 DREILKNI--EGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPggvitggsaK 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3139 AEEARKQKDKADSEAEKQIvaaSQAALKCRTAEQQVQSVLAQQKEdsmmhkkLQQEyekakklakeaeaakekaekeAVL 3218
Cdd:TIGR02168 668 TNSSILERRREIEELEEKI---EELEEKIAELEKALAELRKELEE-------LEEE---------------------LEQ 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3219 LRKQAEEAESQKAAaekeaaiqakAQEDAERLRKEAEFEAAKRAQAE---NAALEQKKKADAEMAKHKKLAEQTLKQKFQ 3295
Cdd:TIGR02168 717 LRKELEELSRQISA----------LRKDLARLEAEVEQLEERIAQLSkelTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3296 VEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKvklKIEKENQLLIkkdkdKAQ 3375
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE---QIEELSEDIE-----SLA 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3376 QLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQA 3455
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1838104091 3456 QRLLEdkelmqkRLdeeTEEYQKSLEAERKRQLEIVAEAEKLKLQVSQL 3504
Cdd:TIGR02168 939 DNLQE-------RL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2459-3183 |
8.67e-28 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 124.94 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2459 TETQRRLEDEEKAAKILKAEEQKKMADLQAELDK---------QKKLAEAHAKAIAKAEKEADELKHQMKQEV-SKREVA 2528
Cdd:NF041483 312 EEIARLVGEATKEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAkATTRAA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2529 ALDAENQKKNIELELHELKKLSEQQIND-KSQLVDDALQSRTKIEEEIHIIRIQL--ETTLNQKSTAETE---------- 2595
Cdd:NF041483 392 AEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRgeAEQLRAEAVAEGErirgearrea 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2596 LKQLREKA-----------AEAERLRKLAQEEAEKLHKQVIEE-TQKKRTAEEELKRkseAEKEAAKQKQKALEDLENLK 2663
Cdd:NF041483 472 VQQIEEAArtaeelltkakADADELRSTATAESERVRTEAIERaTTLRRQAEETLER---TRAEAERLRAEAEEQAEEVR 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2664 MQAE--------EAERKVKQAQIEKEKQIQIAHVAAE----------KSATAELQSTQRSFVEKTSKLEESLKQEHGTV- 2724
Cdd:NF041483 549 AAAEraarelreETERAIAARQAEAAEELTRLHTEAEerltaaeealADARAEAERIRREAAEETERLRTEAAERIRTLq 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2725 LQLQQEAAHLKKQQ-EDALKAREEAEKELDKWRQKA-NEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAkkRAKAEE 2802
Cdd:NF041483 629 AQAEQEAERLRTEAaADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEA--LAAAQE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2803 SALKQKEMAEKELERQRKVADSTAQQKLTAEQELI---RLRAEFDNAEQQRsLLEDELYRLKNEVIAAQQQRKQLEDELA 2879
Cdd:NF041483 707 EAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVA 785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2880 KMRSEMEILIQ-LKSRAEK-----ETMSNTEKSKMLLDAEASKMRdVAEEAGKLRAIA-EEAKYQRQIAEEEAARQRAEA 2952
Cdd:NF041483 786 GLQEQAEEEIAgLRSAAEHaaertRTEAQEEADRVRSDAYAERER-ASEDANRLRREAqEETEAAKALAERTVSEAIAEA 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2953 ERILKEklaAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKAleDEANQHKKEIEEkivqlkKSSQAEMQRQKA 3032
Cdd:NF041483 865 ERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRS--DAAAQADRLIGE------ATSEAERLTAEA 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3033 MVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEET----QQSKLRAEEEAEKQRklameeekrrreae 3108
Cdd:NF041483 934 RAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETvgsaQQHAERIRTEAERVK-------------- 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3109 etvkkiTAAEKEAGRQRKIAQDELDRL--------KKKAEEARKQKDK----ADSEAEKQIVAASQAALKCRT-AEQQVQ 3175
Cdd:NF041483 1000 ------AEAAAEAERLRTEAREEADRTldearkdaNKRRSEAAEQADTliteAAAEADQLTAKAQEEALRTTTeAEAQAD 1073
|
....*....
gi 1838104091 3176 S-VLAQQKE 3183
Cdd:NF041483 1074 TmVGAARKE 1082
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-105 |
1.31e-27 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 110.02 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 5 MLMPLKDLRAIYELLFKDGVMVAKKDKRpQIKHPEIEsVSNLQVMRAMVSLKSRGYVKETFSWRHFYWYLTNEGIVYLRD 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHRELE-IPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|.
gi 1838104091 85 YLRLPSEIVPASLQRTRKPAA 105
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2921-3578 |
6.07e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.97 E-value: 6.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2921 AEEAGKLRAIAEEAKyQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKA 3000
Cdd:COG1196 209 AEKAERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3001 LEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAmvdDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQ 3080
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3081 QSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLkkkaEEARKQKDKADSEAEKQIVAA 3160
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3161 SQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQ 3240
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3241 AKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKhkklAEQTLKQKfqveqELTKVKLKLDDTDKQKDLLDDE 3320
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA----AIEYLKAA-----KAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3321 LQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVklkiekenqlLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQ 3400
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRT----------LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3401 EASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSL 3480
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3481 EAERKRQLEIVAEAEKLKLQVSQLsvaqakaEEEAKRFKKQAD-----NIAArLLETEIATKDKSTVMQQLE-VErrnns 3554
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEEL-------ERELERLEREIEalgpvNLLA-IEEYEELEERYDFLSEQREdLE----- 808
|
650 660
....*....|....*....|....
gi 1838104091 3555 KEADDLRNAIANLETEKARLKKDA 3578
Cdd:COG1196 809 EARETLEEAIEEIDRETRERFLET 832
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2462-3335 |
1.46e-26 |
|
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: 120.85 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2462 QRRLEDEEKAA-----KILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAENQK 2536
Cdd:pfam02463 153 ERRLEIEEEAAgsrlkRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2537 KNIELELHELKKL--SEQQINDKSQlvddalQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQ 2614
Cdd:pfam02463 233 KLNEERIDLLQELlrDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2615 EEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKqkaleDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKS 2694
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-----KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2695 ATAELQSTQRSFVEKTSKLEESLKQehgtvlqlQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAH 2774
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKE--------AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2775 KKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIR----LRAEFDNAEQQR 2850
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKdgvgGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2851 SLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAI 2930
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2931 AEEAKYQRQIAEEEAARQRAEAERILKEKLAAISE-ATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHK 3009
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLrKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3010 KEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRI--------LKLNFEKASSGKLDLELELNKLKNIAEETQQ 3081
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIneelkllkQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3082 SKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAAS 3161
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3162 QAAL----KCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEA 3237
Cdd:pfam02463 854 EELErleeEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKY 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3238 AIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMaKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLL 3317
Cdd:pfam02463 934 EEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV-NLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAII 1012
|
890
....*....|....*...
gi 1838104091 3318 DDELQRLKDEVDDAVKQR 3335
Cdd:pfam02463 1013 EETCQRLKEFLELFVSIN 1030
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1132-1257 |
1.63e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 107.54 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1132 LDEPEEKTWPHFIEDERDRVQKKTFTKWVNkHLIKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHK 1210
Cdd:cd21247 1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMN-NVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1838104091 1211 LQNVQIALDFLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21247 80 LENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2600-3520 |
2.14e-26 |
|
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: 120.46 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2600 REKAAEAERLRKLAQEEAEKLHKQVIEEtqkkrtaEEELKRKSEAEKEAAKQKqkaledLENLKMQAEEAERKVKQAQIE 2679
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLE-------ELKLQELKLKEQAKKALE------YYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2680 KEKQIQIahvaaeksatAELQSTQRSFVEKTSKLEESLKQEhgtvlqlQQEAAHLKKQQEDALKAREEAEKELDKWRQKA 2759
Cdd:pfam02463 233 KLNEERI----------DLLQELLRDEQEEIESSKQEIEKE-------EEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2760 NEALRLRLQAEEEAHKKSlaqeeaekqkeeaereakkraKAEESALKQKEMAEKELERQRKVADSTAQQKltaeQELIRL 2839
Cdd:pfam02463 296 EELKSELLKLERRKVDDE---------------------EKLKESEKEKKKAEKELKKEKEEIEELEKEL----KELEIK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2840 RAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKmrsEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMrd 2919
Cdd:pfam02463 351 REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK---LKEEELELKSEEEKEAQLLLELARQLEDLLKEEK-- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2920 vAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRK 2999
Cdd:pfam02463 426 -KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3000 ALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEET 3079
Cdd:pfam02463 505 ARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLI 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3080 QQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAA-EKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIV 3158
Cdd:pfam02463 585 PKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAkVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3159 AASQAALKCRTAEQQVQSVLAQQKEDSmMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAA 3238
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAK-EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3239 IQAKAQEDAERLRKEAEFEAAKRAQAEnaaLEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDdtDKQKDLLD 3318
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELS---LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL--KEEAELLE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3319 DELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVE 3398
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3399 SQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLK-------AEAELLQRQKDLAQEQAQRLLEDKELMQKRLDE 3471
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEellleeaDEKEKEENNKEEEEERNKRLLLAKEELGKVNLM 978
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1838104091 3472 ETEEYQKSLEAERKRqleivaEAEKLKLQVSQLSVAQAKAEEEAKRFKK 3520
Cdd:pfam02463 979 AIEEFEEKEERYNKD------ELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
1255-1370 |
3.08e-26 |
|
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: 106.71 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1255 FQISDIQInglsEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAF 1334
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1838104091 1335 NVAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2730-3715 |
3.16e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2730 EAA---HLKKQQEDALK--------------AREEAEKELDKWRQKANEALRLR-LQAEEEAHKKSLaqeeaekqkeeae 2791
Cdd:TIGR02168 163 EAAgisKYKERRKETERklertrenldrledILNELERQLKSLERQAEKAERYKeLKAELRELELAL------------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2792 reAKKRAKAEESALKQKEMAEKELERQRKVADSTAQqklTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEvIAAQQQR 2871
Cdd:TIGR02168 230 --LVLRLEELREELEELQEELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2872 KQLEDElakmrsemeiliqlksraeketmsntekskmlldaeasKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAE 2951
Cdd:TIGR02168 304 KQILRE--------------------------------------RLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2952 AERILKEK---LAAISEATRLKTEAEIALKEKEAENERLRRAaedeayqRKALEDEANQHKKEIEEkIVQLKKSSQAEMQ 3028
Cdd:TIGR02168 346 LEELKEELeslEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEIER-LEARLERLEDRRE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3029 RQKAmvddtlkqrrvveeeiRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAE 3108
Cdd:TIGR02168 418 RLQQ----------------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3109 ETVKKItAAEKEAGRQRKIAQDELDRLKKKAEEARKQKD----------KADSEAEKQIVAASQAALK---CRTAEQQVQ 3175
Cdd:TIGR02168 482 RELAQL-QARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvlseliSVDEGYEAAIEAALGGRLQavvVENLNAAKK 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3176 SVLAQQKEDS---MMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAE---SQKAAAEKEAAIQAKAQEDAER 3249
Cdd:TIGR02168 561 AIAFLKQNELgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalSYLLGGVLVVDDLDNALELAKK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3250 LRKEAEF-------------EAAKRAQAENAALEQKKkadaEMAKHkklaeqtlkqkfqvEQELTKVKLKLDDTDKQKDL 3316
Cdd:TIGR02168 641 LRPGYRIvtldgdlvrpggvITGGSAKTNSSILERRR----EIEEL--------------EEKIEELEEKIAELEKALAE 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3317 LDDELQRLKDEVDDAVKQRGQVEEELfkvkvqmEELLKVKLKIEKENQllikkdkdKAQQLLAEEAENMKRLAKEAAILS 3396
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQI-------SALRKDLARLEAEVE--------QLEERIAQLSKELTELEAEIEELE 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3397 VESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEeteey 3476
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----- 842
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3477 qksLEAERKRQLEivaEAEKLKLQVSQLSVAQAKAEEEAKRFKKQadniaarlleteiatkdkstvMQQLEVERRNNSKE 3556
Cdd:TIGR02168 843 ---LEEQIEELSE---DIESLAAEIEELEELIEELESELEALLNE---------------------RASLEEALALLRSE 895
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3557 ADDLRNAIANLETEKARLKKDAEELQNKskeMADAQMKQIEhektmLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEA 3636
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREK---LAQLELRLEG-----LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3637 KKAkaltdeqERQRKLMEEEKKKLH----ATMDEAlsKQKEAEREMLNKQKEMQELEKKRLEQ--EKVLAEENKKLRDQL 3710
Cdd:TIGR02168 968 EEA-------RRRLKRLENKIKELGpvnlAAIEEY--EELKERYDFLTAQKEDLTEAKETLEEaiEEIDREARERFKDTF 1038
|
....*
gi 1838104091 3711 QQLEE 3715
Cdd:TIGR02168 1039 DQVNE 1043
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
1257-1370 |
4.36e-26 |
|
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: 106.32 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1257 ISDIQInglsEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNV 1336
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1838104091 1337 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2793-3720 |
1.09e-25 |
|
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: 118.15 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2793 EAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRaEFDNAEQQRSLLEDELYRLKNEVIaaQQQRK 2872
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE-YYQLKEKLELEEEYLLYLDYLKLN--EERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2873 QLEDELAKMRSEMEILIQLksrAEKETMSNTEKSKmLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEA 2952
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQE---IEKEEEKLAQVLK-ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2953 ERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKa 3032
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3033 mvddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVK 3112
Cdd:pfam02463 395 ------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3113 KITAAEKEagrqrkiaqdeldrlKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQ 3192
Cdd:pfam02463 469 KSEDLLKE---------------TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3193 QEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEaakRAQAENAALEQK 3272
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE---IDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3273 KKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 3352
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3353 LKVKLKIEKENQLLIKKDKDKaQQLLAEEAENMKrlakeAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQ 3432
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEE-LKKLKLEAEELL-----ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3433 EASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKlqvsQLSVAQAKAE 3512
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI----KEEELEELAL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3513 EEAKRFKKQADNIAARLLETEIATKDKSTvmQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQ 3592
Cdd:pfam02463 841 ELKEEQKLEKLAEEELERLEEEITKEELL--QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3593 MKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQ--RKLMEEEKKKLHATMDEALSK 3670
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVnlMAIEEFEEKEERYNKDELEKE 998
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3671 QKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:pfam02463 999 RLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
1273-1372 |
1.35e-25 |
|
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: 104.29 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1273 EKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED- 1351
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1838104091 1352 VDVPHPDEKSIITYVSSLYDV 1372
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2942-3726 |
3.97e-25 |
|
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: 116.22 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2942 EEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEK-IVQLK 3020
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKeKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3021 KSSQAEMQRQKAmvddtLKQRRVVEEEIRILKLNFEKASSGKLDLELELNK--LKNIAEETQQSKLRAEEEAEKQRKLAM 3098
Cdd:pfam02463 223 EEYLLYLDYLKL-----NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAqvLKENKEEEKEKKLQEEELKLLAKEEEE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3099 EEEKRRREAEETVKKITAAEKEAGRQRKiAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVL 3178
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLKESEKEKKK-AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3179 AQQKEDSmmhKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDaerlrKEAEFEA 3258
Cdd:pfam02463 377 AKKKLES---ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL-----KQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3259 AKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLldDELQRLKDEVDDAVKQRGQV 3338
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR--SGLKVLLALIKDGVGGRIIS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3339 EEELFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRA 3418
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3419 LAEKMLKEKMQAIQEASR--LKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLdeETEEYQKSLEAERKRQLEIVAEAEK 3496
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVveGILKDTELTKLKESAKAKESGLRKGVSLEEGLA--EKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3497 LKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKK 3576
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3577 DAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKK-ERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEE 3655
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAlEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3656 EKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVIS 3726
Cdd:pfam02463 845 EQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK 915
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2927-3720 |
1.11e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.77 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2927 LRAIAEEA------KYQRQIAEEEAARQRAEAER---ILKEKLAAISeatRLKTEAEIALKEKEAENERlrraaedEAYQ 2997
Cdd:TIGR02168 157 RRAIFEEAagiskyKERRKETERKLERTRENLDRledILNELERQLK---SLERQAEKAERYKELKAEL-------RELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2998 RKALEDEANQHKKEIEEKivqlkKSSQAEMQRQkamVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE 3077
Cdd:TIGR02168 227 LALLVLRLEELREELEEL-----QEELKEAEEE---LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3078 ETQQSKLRAEEEAEkqrklameeekrrrEAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKD---KADSEAE 3154
Cdd:TIGR02168 299 RLEQQKQILRERLA--------------NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsleAELEELE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3155 KQIVAASQAALKCRTAEQQVQSVLAQqkedsmmhkKLQQEYekakklakeaeaakekaekeavLLRKQAEEAESQKAAAE 3234
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQ---------LELQIA----------------------SLNNEIERLEARLERLE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3235 KEAAIQAKAQEDAERLRKEAEFEAAKRAQAE-NAALEQKKKADAEMAKHKKLAEQTLKQKfqvEQELTKVKLKLDDTDKQ 3313
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEElEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQAR 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3314 KDLLDDELQRLKDEvDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKE---------NQLLIKKDKD--KAQQLLAE-- 3380
Cdd:TIGR02168 491 LDSLERLQENLEGF-SEGVKALLKNQSGLSGILGVLSELISVDEGYEAAieaalggrlQAVVVENLNAakKAIAFLKQne 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3381 -----------------EAENMKRLAKEAAILSVesqeASRLRQIAE----------------EDLVQQRALAEKMLKEK 3427
Cdd:TIGR02168 570 lgrvtflpldsikgteiQGNDREILKNIEGFLGV----AKDLVKFDPklrkalsyllggvlvvDDLDNALELAKKLRPGY 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3428 M------------------QAIQEASRLKAEAEL--LQRQKDLAQEQAQRL---LEDKELMQKRLDEETEEYQKSLEAER 3484
Cdd:TIGR02168 646 RivtldgdlvrpggvitggSAKTNSSILERRREIeeLEEKIEELEEKIAELekaLAELRKELEELEEELEQLRKELEELS 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3485 KRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAI 3564
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3565 ANLETEKARLKKDAEELQNKsKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLEsQYEEEAKKAKALTD 3644
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERA 883
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3645 EQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1270-1370 |
1.35e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 101.35 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERdLGVTRLLDP 1349
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1838104091 1350 EDV---DVphPDEKSIITYVSSLY 1370
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1150-1255 |
1.44e-24 |
|
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: 101.41 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1150 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 1226
Cdd:cd21228 3 KIQQNTFTRWCNEHL---KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESI 79
|
90 100
....*....|....*....|....*....
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHF 1255
Cdd:cd21228 80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1154-1254 |
2.47e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 100.47 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1154 KTFTKWVNKHLIKRAESqhHVTDLYEDLRDGHNLISLLEVLSGDTLPREK---GRMRFHKLQNVQIALDFLRHRQVKLVN 1230
Cdd:smart00033 1 KTLLRWVNSLLAEYDKP--PVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVL 78
|
90 100
....*....|....*....|....
gi 1838104091 1231 IRNDDIADGnPKLTLGLIWTIILH 1254
Cdd:smart00033 79 FEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
1150-1258 |
3.00e-24 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 101.26 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1150 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHKLQNVQIALDFLRHRQV 1226
Cdd:cd21310 15 KIQQNTFTRWCNEHL---KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHI 91
|
90 100 110
....*....|....*....|....*....|..
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1258
Cdd:cd21310 92 KLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
1257-1370 |
4.83e-24 |
|
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: 100.57 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1257 ISDIQInglsEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNV 1336
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1838104091 1337 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1270-1374 |
1.24e-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: 98.71 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYqNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDP 1349
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1838104091 1350 EDVDVPHPDEKSIITYVSSLYDVMP 1374
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1275-1370 |
1.30e-23 |
|
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: 98.38 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1275 LLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED-VD 1353
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1838104091 1354 VPHPDEKSIITYVSSLY 1370
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1151-1257 |
1.92e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 98.13 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1151 VQKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTLP-REKGRMRFHKLQNVQIALDFLRHRQ-VKL 1228
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGVR-VTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPK 80
|
90 100
....*....|....*....|....*....
gi 1838104091 1229 VNIRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:pfam00307 81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1269-1375 |
2.94e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 97.74 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1269 MTAKEKLLCWSQRMTDGY-QNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQ--ENLEQAFNVAERDLGVTR 1345
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1346 -LLDPEDVDvpHPDEKSIITYVSSLYDVMPR 1375
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3205-3716 |
4.33e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.26 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3205 AEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKK 3284
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3285 LAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKE-- 3362
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEll 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3363 ----NQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLK 3438
Cdd:COG1196 390 ealrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3439 AEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQL-----------------EIVAEAEKLKLQV 3501
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayEAALEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3502 SQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNA-----------------I 3564
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAdaryyvlgdtllgrtlvA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3565 ANLETEKARLKKDAEELQNKSKEMADAQMKQiehektMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTD 3644
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGG------SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3645 EQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEA 3716
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
1257-1370 |
1.45e-22 |
|
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: 96.30 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1257 ISDIQInglsEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNV 1336
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1838104091 1337 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1273-1373 |
1.82e-22 |
|
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: 95.22 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1273 EKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPEDV 1352
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1838104091 1353 DVPHPDEKSIITYVSSLYDVM 1373
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3119-3719 |
6.31e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 6.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3119 KEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKA 3198
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3199 KKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAE 3278
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3279 MAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLK 3358
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3359 IEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLK 3438
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3439 AEAELLQRQKDLAQEQAQRLLEdkelmqkrldeeteeyqksLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRF 3518
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATF-------------------LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3519 KKQADNIAARLLETEIAtKDKSTVMQQLEVERRNNSKEADDLrnAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEH 3598
Cdd:COG1196 616 YVLGDTLLGRTLVAARL-EAALRRAVTLAGRLREVTLEGEGG--SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3599 EKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREM 3678
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1838104091 3679 lnkQKEMQELEK---KRLEQEKVLAEENKKLRDQLQQLEEAQKE 3719
Cdd:COG1196 773 ---EREIEALGPvnlLAIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
1270-1369 |
8.81e-22 |
|
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: 93.31 E-value: 8.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERdLGVTRLLDP 1349
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1838104091 1350 ED-VDVPHPDEKSIITYVSSL 1369
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1906-1972 |
1.25e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.17 E-value: 1.25e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 1906 QLKPRNptTSIKGKLPIQAVCDFKQQEITVHKGDECALLNNSQPFKWKVLNHSGNEAVVPSVCFMVP 1972
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
1271-1370 |
2.14e-21 |
|
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: 92.24 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1271 AKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPE 1350
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1838104091 1351 D-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3368-3723 |
4.82e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3368 KKDKDKAQQLLAEEAENMKRLAkeaAILS-VESQeasrLRQIAEedlvqQRALAEKMlkekmQAIQEASRLKaEAELLQR 3446
Cdd:COG1196 171 KERKEEAERKLEATEENLERLE---DILGeLERQ----LEPLER-----QAEKAERY-----RELKEELKEL-EAELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3447 QKDLAQEQAQRLLEDKELMQKRLDEETEEYQ---KSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQAD 3523
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3524 NIAARLleteiatkdkstvmQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEmADAQMKQIEHEKTML 3603
Cdd:COG1196 313 ELEERL--------------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3604 QQTFLTEKEMLLKKERLIEDEKKRLEsQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQK 3683
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1838104091 3684 EMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQ 3723
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2353-3022 |
5.30e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 102.83 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2353 KIQAVSITDSKTLKEQLSQEKK--LLEEIENNKENVDECQKYAKAYINSIKDYELQLVAYNAKADPHAspLKKNKMDSAS 2430
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2431 DNIIQEYVTLRTRYSELmtltSQYIKFITETQRRLEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKE 2510
Cdd:TIGR02168 284 EELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2511 ADELKHQMKQEVSKREVAALDAENQKKNIELELHELKKLSEQQINDKSQLVDdaLQSRtkieeeihIIRIQLETTLNQKS 2590
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDR--------RERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2591 TAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELkRKSEAEKEAAKQKQKALEDLENLKMQAEEAE 2670
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2671 RKVKQAQIEK-----------------EKQIQIA------HVAAEKSATA------------------------------ 2697
Cdd:TIGR02168 509 KALLKNQSGLsgilgvlselisvdegyEAAIEAAlggrlqAVVVENLNAAkkaiaflkqnelgrvtflpldsikgteiqg 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2698 ---ELQSTQRSFVEKTSKLEESLKQ------------------------------------------------------E 2720
Cdd:TIGR02168 589 ndrEILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsakT 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2721 HGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKA 2800
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2801 EESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEV----IAAQQQRKQLED 2876
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2877 ELAKMRSEMEILIQLKSRAEK--ETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAER 2954
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEElsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 2955 ILKEKLAAISEATRLKTEAEIALKEKEAE----NERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKS 3022
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1270-1370 |
6.84e-21 |
|
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: 90.87 E-value: 6.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDP 1349
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1838104091 1350 EDVDV--PHPDEKSIITYVSSLY 1370
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2442-3678 |
1.07e-20 |
|
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: 101.79 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2442 TRYSELMTLTSQYIKFITETQRRLEDE----EKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKaEKEADELKHQ 2517
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESElkelEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR-KQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2518 MKQEVSKREVAALDAENQKKNIELELHELkklsEQQIND------KSQLVDDALQSRTKIEEEihiiriQLETTLNQKST 2591
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQHIQDL----EEQLDEeeaarqKLQLEKVTTEAKIKKLEE------DILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2592 AETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLK-----MQA 2666
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQeqiaeLQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2667 EEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEdALKAre 2746
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE-ALKT-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2747 EAEKELDKwrQKANEALRLRLQAEEEAHKKSLAqeeaekqkeeaerEAKKRAKAEESALKQK------EMAEkELERQRK 2820
Cdd:pfam01576 307 ELEDTLDT--TAAQQELRSKREQEVTELKKALE-------------EETRSHEAQLQEMRQKhtqaleELTE-QLEQAKR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2821 VADSTAQQKLTAEQELIRLRAEF-------DNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKS 2893
Cdd:pfam01576 371 NKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLN 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2894 RAEKETMsnteKSKMLLDAEASKMRDVAEE-----------AGKLRAIAEE-AKYQRQIAEEEAARQRAEaerilkekla 2961
Cdd:pfam01576 451 EAEGKNI----KLSKDVSSLESQLQDTQELlqeetrqklnlSTRLRQLEDErNSLQEQLEEEEEAKRNVE---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2962 aiseatRLKTEAEIALKEkeaenerLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQA--EMQRQKAMVDDTLK 3039
Cdd:pfam01576 517 ------RQLSTLQAQLSD-------MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAydKLEKTKNRLQQELD 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3040 QRRVVEEEIRILKLNFEKASSgKLDLELElnKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRrreaeetVKKITAAEK 3119
Cdd:pfam01576 584 DLLVDLDHQRQLVSNLEKKQK-KFDQMLA--EEKAISARYAEERDRAEAEAREKETRALSLARA-------LEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3120 EAGRQRKIAQDELDRLKKKAEEARKQKdkadSEAEKQIvaasqaalkcRTAEQQVQSvlaqqkedsmmhkklqqeyekak 3199
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGKNV----HELERSK----------RALEQQVEE----------------------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3200 klakeaeaakekaekeavlLRKQAEEAESQKaaaekeaaiqaKAQEDAeRLRKEAEFEAAKraqaenAALEQKKKADAEM 3279
Cdd:pfam01576 697 -------------------MKTQLEELEDEL-----------QATEDA-KLRLEVNMQALK------AQFERDLQARDEQ 739
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3280 AKHKKlaEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKvklki 3359
Cdd:pfam01576 740 GEEKR--RQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR----- 812
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3360 EKENQLLIKKDkdkaqqLLAEEAENMKRLakeaailsvESQEASRLRqiAEEDLvqqrALAEKMlkeKMQAIQEASRLKA 3439
Cdd:pfam01576 813 ELEEARASRDE------ILAQSKESEKKL---------KNLEAELLQ--LQEDL----AASERA---RRQAQQERDELAD 868
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3440 EAELLQRQKDLAQEQAQRLledkELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFK 3519
Cdd:pfam01576 869 EIASGASGKSALQDEKRRL----EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLE 944
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3520 KQADNIAARLLETEIATKDKstvmqqleverrnnskeaddLRNAIANLETEKARLKkdaEELQNKSKEMADAQMKQIEHE 3599
Cdd:pfam01576 945 RQNKELKAKLQEMEGTVKSK--------------------FKSSIAALEAKIAQLE---EQLEQESRERQAANKLVRRTE 1001
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3600 KTMlqqtflteKEMLLKkerlIEDEKKRLEsQYEEEAKKAKALTDEQERQRKLMEEE-------KKKLHATMDEALSKQK 3672
Cdd:pfam01576 1002 KKL--------KEVLLQ----VEDERRHAD-QYKDQAEKGNSRMKQLKRQLEEAEEEasranaaRRKLQRELDDATESNE 1068
|
....*.
gi 1838104091 3673 EAEREM 3678
Cdd:pfam01576 1069 SMNREV 1074
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2789-3728 |
1.34e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.44 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2789 EAEREAKKrAKAEESALKQkEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDN--------AEQQRSLLEDELYRL 2860
Cdd:NF041483 91 DAERELRD-ARAQTQRILQ-EHAEHQARLQAELHTEAVQRRQQLDQELAERRQTVEShvnenvawAEQLRARTESQARRL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2861 KNEVIA----------------AQQQRKQLEDELAKMRSEMEILIqLKSRAEKETmsntekskmLLDAEASKMRDVAEEA 2924
Cdd:NF041483 169 LDESRAeaeqalaaaraeaerlAEEARQRLGSEAESARAEAEAIL-RRARKDAER---------LLNAASTQAQEATDHA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2925 GKLRAiaeeakyqRQIAEEEAARQRA-EAERILKEKLAaiseatrlktEAEIALKEKEAENERLRRAAEDEAYQRKALED 3003
Cdd:NF041483 239 EQLRS--------STAAESDQARRQAaELSRAAEQRMQ----------EAEEALREARAEAEKVVAEAKEAAAKQLASAE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3004 EAN-QHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEeiRILKLNFEKA-SSGKLDLELELNKLKNIAEE--- 3078
Cdd:NF041483 301 SANeQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAE--KLVAEAAEKArTVAAEDTAAQLAKAARTAEEvlt 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3079 -----TQQSKLRAEEEAEKQRKlameeekrrreaeetvkkitAAEKEAGRQRKIAQDELDRLKKKA-------------- 3139
Cdd:NF041483 379 kasedAKATTRAAAEEAERIRR--------------------EAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvel 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3140 -EEARK-----QKDKADSEAEKQIV---AASQAALKCRTAEQQVQSVLAQQKEDSmmhKKLQQeyekakKLAKEAEAAKE 3210
Cdd:NF041483 439 qEEARRlrgeaEQLRAEAVAEGERIrgeARREAVQQIEEAARTAEELLTKAKADA---DELRS------TATAESERVRT 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3211 KAEKEAVLLRKQAEEAesqkaaaekeaaiQAKAQEDAERLRKEAEFEAAK-RAQAENAALEQKKKAD-AEMAKHKKLAEQ 3288
Cdd:NF041483 510 EAIERATTLRRQAEET-------------LERTRAEAERLRAEAEEQAEEvRAAAERAARELREETErAIAARQAEAAEE 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3289 TLKQKFQVEQELTKVKLKLDDTDKQKDLL----DDELQRLKDEVDDAVKQ-RGQVEEELFKVKVQME----------ELL 3353
Cdd:NF041483 577 LTRLHTEAEERLTAAEEALADARAEAERIrreaAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAadasaaraegENV 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3354 KVKLKIE--KENQLLIKKDKDKAQQLLAEEAENMKRLAKEAA-ILSVESQEASRLRQIAEEDLVQQRALAEkmlKEKMQA 3430
Cdd:NF041483 657 AVRLRSEaaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAeALAAAQEEAARRRREAEETLGSARAEAD---QERERA 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3431 IQEASRLKAEAellQRQKDLAQEQAQRLLEdkelmqkrldeeteeyqkslEAERkRQLEIVAEAEKLKLQVSQlSVA--Q 3508
Cdd:NF041483 734 REQSEELLASA---RKRVEEAQAEAQRLVE--------------------EADR-RATELVSAAEQTAQQVRD-SVAglQ 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3509 AKAEEE-----------AKRFKKQADNIAARL-----LETEIATKDKSTVMQQLEVE----------------------R 3550
Cdd:NF041483 789 EQAEEEiaglrsaaehaAERTRTEAQEEADRVrsdayAERERASEDANRLRREAQEEteaakalaertvseaiaeaerlR 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3551 RNNSKEADDLR----NAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMlqqtfltekemllKKERLIEDEKK 3626
Cdd:NF041483 869 SDASEYAQRVRteasDTLASAEQDAARTRADAREDANRIRSDAAAQADRLIGEATS-------------EAERLTAEARA 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3627 RLESQYEEEAKKA-KALTDEQERQRKLMEE---EKKKLHATMDEAL-SKQKEAERemlnkqkemqelekKRLEQEKVLAE 3701
Cdd:NF041483 936 EAERLRDEARAEAeRVRADAAAQAEQLIAEatgEAERLRAEAAETVgSAQQHAER--------------IRTEAERVKAE 1001
|
1050 1060 1070
....*....|....*....|....*....|....*
gi 1838104091 3702 ---ENKKLRDQLQQ-----LEEAQKEKNTQVISAA 3728
Cdd:NF041483 1002 aaaEAERLRTEAREeadrtLDEARKDANKRRSEAA 1036
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
1274-1372 |
1.61e-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: 89.72 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1274 KLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLD-PEDV 1352
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1838104091 1353 DVPHPDEKSIITYVSSLYDV 1372
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2455-2972 |
2.31e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2455 IKFITETQRRLEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAEN 2534
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2535 QKKNIELELHELKKLSEQQINDKSQLvddalqsrtkieeeihiirIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQ 2614
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERL-------------------ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2615 EEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKS 2694
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2695 ATAELqstqrsfvektskleeslkqEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAH 2774
Cdd:COG1196 532 VEAAY--------------------EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2775 KKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLE 2854
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2855 DELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEA 2934
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1838104091 2935 KYQRQIAEEEAARQRAEAERiLKEK--------LAAISEATRLKTE 2972
Cdd:COG1196 752 ALEELPEPPDLEELERELER-LEREiealgpvnLLAIEEYEELEER 796
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2443-3155 |
2.71e-20 |
|
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: 100.43 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2443 RYSELMTLTSQYIKFITETQRRLEDEEKAAKIL---KAEEQKKMADLQA----ELDKQKKLAEAHAKAIAKAE-KEADEL 2514
Cdd:TIGR00618 89 RVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILaakKSETEEVIHDLLKldykTFTRVVLLPQGEFAQFLKAKsKEKKEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2515 KHQMkQEVSKREVAALDAENQKKNIELELHELKKLSEQQINDKSQLVddalQSRTKIEEEIHIIRIQLETTLNQKSTAET 2594
Cdd:TIGR00618 169 LMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMP----DTYHERKQVLEKELKHLREALQQTQQSHA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAAEAERLRKLAQEEAEKLHKQvieETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENlKMQAEEAERKVK 2674
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEEL---RAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQSK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2675 QAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVE----------KTSKLEESLKQEHGT--VLQLQQEAAHLKkQQEDAL 2742
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihirdahevATSIREISCQQHTLTqhIHTLQQQKTTLT-QKLQSL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2743 KA------REEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEA--------EKQKEEAEREAKKRAKAEESALKQK 2808
Cdd:TIGR00618 399 CKeldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaitctaqcEKLEKIHLQESAQSLKEREQQLQTK 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2809 EMAEKELERQRKVADSTAQ-----------------QKLTA--------------EQELIRLRAEFDNAEQQRSLLEDEL 2857
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLelqeepcplcgscihpnPARQDidnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQR 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2858 YRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQ 2937
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2938 RQIAEEEAARQRaEAERILKEKlaaISEATRLKTEAEialKEKEAENERLRRAAEDEAYQRKALEDEANQHK---KEIEE 3014
Cdd:TIGR00618 639 QELALKLTALHA-LQLTLTQER---VREHALSIRVLP---KELLASRQLALQKMQSEKEQLTYWKEMLAQCQtllRELET 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3015 KIVQLKK----------SSQAEMQRQKAMVDDTLKQ-RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQ-QS 3082
Cdd:TIGR00618 712 HIEEYDRefneienassSLGSDLAAREDALNQSLKElMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQfFN 791
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3083 KLRAEEEAE-KQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIA-----QDELDRLKKKAEEARKQKDKADSEAEK 3155
Cdd:TIGR00618 792 RLREEDTHLlKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEeksatLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2980-3666 |
5.75e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2980 KEAENeRLRRAAEDEAyqRkaLEDEANqhkkEIEEKIVQLKKssqaemQRQKAmvddtlKQRRVVEEEIRILklnfekas 3059
Cdd:COG1196 175 EEAER-KLEATEENLE--R--LEDILG----ELERQLEPLER------QAEKA------ERYRELKEELKEL-------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3060 sgklDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAmeeeKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKA 3139
Cdd:COG1196 226 ----EAELLLLKLRELEAELEELEAELEELEAELEELE----AELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3140 EEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLL 3219
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3220 RKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQE 3299
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3300 LTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVkqrgQVEEELFKVKVQMEELLKVklkiekenqllIKKDKDKAQQLLA 3379
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAA----ARLLLLLEAEADYEGFLEG-----------VKAALLLAGLRGL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3380 EEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKM--QAIQEASRLKAEAELLQRQKDLAQEQAQR 3457
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3458 LLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATK 3537
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3538 DKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKK 3617
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3618 ERL---IEDEKKRLES----------QYEEEAKKAKALTDeqerQRKLMEEEKKKLHATMDE 3666
Cdd:COG1196 763 EELereLERLEREIEAlgpvnllaieEYEELEERYDFLSE----QREDLEEARETLEEAIEE 820
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
1150-1258 |
1.47e-19 |
|
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: 87.83 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1150 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 1226
Cdd:cd21309 16 KIQQNTFTRWCNEHL---KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESI 92
|
90 100 110
....*....|....*....|....*....|..
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1258
Cdd:cd21309 93 KLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
1266-1373 |
2.03e-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: 86.93 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1266 SEDMTAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTR 1345
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1838104091 1346 LLDPEDV-DVPHPDEKSIITYVSSLYDVM 1373
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
1150-1258 |
2.60e-19 |
|
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: 87.06 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1150 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 1226
Cdd:cd21308 19 KIQQNTFTRWCNEHL---KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESI 95
|
90 100 110
....*....|....*....|....*....|..
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1258
Cdd:cd21308 96 KLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2915-3757 |
3.48e-19 |
|
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: 96.68 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2915 SKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARqrAEAERILKEklaaISEATRLKTEAEIALKEKEAENERLRRAAEDE 2994
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALE--RQKEAIERQ----LASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2995 AYQRKAL-EDEANQHKKEIEE---KIVQLKKSSQAEMQRQKamvdDTLKQRRVVEEEIRILKLNFEkassgKLDLELELN 3070
Cdd:TIGR02169 278 NKKIKDLgEEEQLRVKEKIGEleaEIASLERSIAEKERELE----DAEERLAKLEAEIDKLLAEIE-----ELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3071 KLKNIAEETQQSKLRAEEEAEKQR--KLAMEEEKRRREAEETVKKITAAEKEAG---RQRKIAQDELDRLKKKAEEARKQ 3145
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAEleEVDKEFAETRDELKDYREKLEKLKREINelkRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3146 KDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEaeaakekaekeavlLRKQAEE 3225
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK--------------LQRELAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3226 AESQKAAAEKEAAIQAKAQED------------------AERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAE 3287
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVlkasiqgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGR 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3288 QTL--KQKFQVEQELTKVKLKLDDTDKQKDLLDDElqrlkDEVDDAVKQRGQ---VEEELFKVKVQMEELLKVKLKIE-- 3360
Cdd:TIGR02169 575 ATFlpLNKMRDERRDLSILSEDGVIGFAVDLVEFD-----PKYEPAFKYVFGdtlVVEDIEAARRLMGKYRMVTLEGElf 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3361 -------------KENQLLIKKDKDKAQQlLAEEAENMKRLakeaailsvesqeasrlrqiaEEDLVQQRALAEKMLKEK 3427
Cdd:TIGR02169 650 eksgamtggsrapRGGILFSRSEPAELQR-LRERLEGLKRE---------------------LSSLQSELRRIENRLDEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3428 MQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQL--S 3505
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaR 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3506 VAQAKAEE---EAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQ 3582
Cdd:TIGR02169 788 LSHSRIPEiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3583 NKSKEmADAQMKQIEHEKTMLQQtfltEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALT---DEQERQRKLMEEEKKK 3659
Cdd:TIGR02169 868 EELEE-LEAALRDLESRLGDLKK----ERDELEAQLRELERKIEELEAQIEKKRKRLSELKaklEALEEELSEIEDPKGE 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3660 LHATMDEALSKQKEAErEMLNKQKEMQELE-------------KKRL----EQEKVLAEENKKLRDQLQQLEEAQKEKNT 3722
Cdd:TIGR02169 943 DEEIPEEELSLEDVQA-ELQRVEEEIRALEpvnmlaiqeyeevLKRLdelkEKRAKLEEERKAILERIEEYEKKKREVFM 1021
|
890 900 910
....*....|....*....|....*....|....*
gi 1838104091 3723 QVISAATvETTKNVYNGQNAGDVVDSVENKPDPLS 3757
Cdd:TIGR02169 1022 EAFEAIN-ENFNEIFAELSGGTGELILENPDDPFA 1055
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2746-3587 |
5.45e-19 |
|
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: 96.29 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2746 EEAEKELDKWRQKANEALRLR-LQAEEEahkkslaqeeaekqkeeaEREAKKRAKAEESALKQKEMAEKELERQRKVADS 2824
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQaLLKEKR------------------EYEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2825 TAQQKLTAEQELIRLRAEFDNAEQQ-RSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILiqlksrAEKETMSNT 2903
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA------EERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2904 EKSKMLLDAEASKmRDVAEEAGKLRAIAEEakYQRQIAEEEAARQRAEAE----RILKEKLAA----ISEATRLKTEAEI 2975
Cdd:TIGR02169 330 EIDKLLAEIEELE-REIEEERKRRDKLTEE--YAELKEELEDLRAELEEVdkefAETRDELKDyrekLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2976 ALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQaEMQRQKAMVDDTLKQRRVVEEEIRILKlnf 3055
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-KLEQLAADLSKYEQELYDLKEEYDRVE--- 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3056 EKASSGKLDLElELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEEtvKKITAAEKEAGRQRKIAQDELDRL 3135
Cdd:TIGR02169 483 KELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGE--RYATAIEVAAGNRLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3136 KKKAEEARKQKDK-----------ADSEAEKQIVAASQA---ALKCRTAEQQVQSVLAQQKEDSMMHKKLqqEYEKAKKL 3201
Cdd:TIGR02169 560 AKEAIELLKRRKAgratflplnkmRDERRDLSILSEDGVigfAVDLVEFDPKYEPAFKYVFGDTLVVEDI--EAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3202 AKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAK 3281
Cdd:TIGR02169 638 KYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3282 HKKLAeqtlKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKvklkieK 3361
Cdd:TIGR02169 718 IGEIE----KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA------R 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3362 ENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEkmlkekmqaiQEASRLKAEA 3441
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE----------QIKSIEKEIE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3442 ELLQRQKDLAQEQAQRLLEDKELMQKR--LDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFK 3519
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3520 KQ-------------ADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSK 3586
Cdd:TIGR02169 938 DPkgedeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
.
gi 1838104091 3587 E 3587
Cdd:TIGR02169 1018 E 1018
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
1152-1255 |
8.68e-19 |
|
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: 84.56 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1152 QKKTFTKWVNKHLiKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHKLQNVQIALDFLRHRQVKLV 1229
Cdd:cd21212 1 EIEIYTDWANHYL-EKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQ 79
|
90 100
....*....|....*....|....*.
gi 1838104091 1230 NIRNDDIADGNPKLTLGLIWTIILHF 1255
Cdd:cd21212 80 GITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1153-1253 |
3.19e-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: 83.16 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1153 KKTFTKWVNKHLIKRaeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHKLQNVQIALDFLRHRQV-KLV 1229
Cdd:cd00014 1 EEELLKWINEVLGEE--LPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELD 78
|
90 100
....*....|....*....|....*
gi 1838104091 1230 NIRNDDI-ADGNPKLTLGLIWTIIL 1253
Cdd:cd00014 79 LFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1272-1370 |
3.37e-18 |
|
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: 83.50 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1272 KEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED 1351
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1838104091 1352 -VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
1270-1369 |
4.37e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 82.98 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERdLGVTRLLDP 1349
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1838104091 1350 ED-VDVPHPDEKSIITYVSSL 1369
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1270-1368 |
7.16e-18 |
|
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: 81.90 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYqniRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQ-ENLEQAFNVAERDLGVTRLLD 1348
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPlENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1838104091 1349 PEDVDVPHPDEKSIITYVSS 1368
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
1272-1371 |
1.31e-17 |
|
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: 81.55 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1272 KEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED 1351
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1838104091 1352 VDV--PHPDEKSIITYVSSLYD 1371
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2243-2988 |
1.99e-17 |
|
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: 90.89 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2243 AKEVESYRAKLKKMRAEAEGEQPVFDSLEEELQKATT-VSEKMSRvHSERDIELDHFRQNVSGLQDRWKAVFTQMEIRHR 2321
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEkLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2322 ELEQLGRQLGYYHESYDWLIHWITDAKERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIK 2401
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2402 DYELQLVAYNAK---ADPHASPLKKNKMDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAE 2478
Cdd:TIGR02168 390 QLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2479 EQKK----------MADLQAELDKQKKLAEAH---AKAIAKAEKEADELKHQMKQEVSKREV---------AAL------ 2530
Cdd:TIGR02168 470 LEEAeqaldaaereLAQLQARLDSLERLQENLegfSEGVKALLKNQSGLSGILGVLSELISVdegyeaaieAALggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2531 ----DAENQKKNIE-LELHELKKLS---EQQINDKSQLVDDAlqSRTKIEEEIHIIRIQLETTLNQKSTA-ETELKQLR- 2600
Cdd:TIGR02168 550 vvveNLNAAKKAIAfLKQNELGRVTflpLDSIKGTEIQGNDR--EILKNIEGFLGVAKDLVKFDPKLRKAlSYLLGGVLv 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2601 -EKAAEAERLRKLAQEEAeklhkQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIE 2679
Cdd:TIGR02168 628 vDDLDNALELAKKLRPGY-----RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2680 KEKQIQIAHVAAEKSATAELQSTQRSfvektSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKA 2759
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2760 NEALRLRLQAEEEAhkkslaqeEAEKQKEEAEREAKKRAKAEESALKQK--------EMAEKELERQRKVADSTAQQKLT 2831
Cdd:TIGR02168 778 AEAEAEIEELEAQI--------EQLKEELKALREALDELRAELTLLNEEaanlrerlESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2832 AEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMS-NTEKSKMLL 2910
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElREKLAQLEL 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2911 DAEASKMRdVAEEAGKLRA----IAEEAKYQRQIAEEEAARQRAEAERiLKEKLAAISEATRLkteaeiALKEKEAENER 2986
Cdd:TIGR02168 930 RLEGLEVR-IDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKER 1001
|
..
gi 1838104091 2987 LR 2988
Cdd:TIGR02168 1002 YD 1003
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
1272-1378 |
2.49e-17 |
|
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: 80.86 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1272 KEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED 1351
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*....
gi 1838104091 1352 VDV--PHPDEKSIITYVSSLYDVMPRMDV 1378
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRRHEM 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3111-3731 |
2.67e-17 |
|
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: 90.50 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3111 VKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEK-QIVAASQAALkcRTAEQQVQSVLAQQKEDSMmhK 3189
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaERYKELKAEL--RELELALLVLRLEELREEL--E 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3190 KLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAA------KRAQ 3263
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqlEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3264 AENAALEQKKKADAE-MAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEEL 3342
Cdd:TIGR02168 323 AQLEELESKLDELAEeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3343 FKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAilsvesQEASRLRQIAEEDLVQQRALAEK 3422
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ------EELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3423 MLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKR-----LDEETEEYQKSLEA--------------- 3482
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlseLISVDEGYEAAIEAalggrlqavvvenln 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3483 ERKRQLEIVAEAEKLKLQVSQLSVAQAKA----------------------EEEAKRFKK----------------QADN 3524
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTFLPLDSIKGTEiqgndreilkniegflgvakdlVKFDPKLRKalsyllggvlvvddldNALE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3525 IAARLLETE-IATKD----------------KSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKsKE 3587
Cdd:TIGR02168 637 LAKKLRPGYrIVTLDgdlvrpggvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE-LE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3588 MADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQErQRKLMEEEKKKLHATMDEA 3667
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIEELEAQIEQL 794
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3668 LSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEA--QKEKNTQVISAATVE 3731
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLeeQIEELSEDIESLAAE 860
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1273-1369 |
6.73e-17 |
|
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: 79.28 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1273 EKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRV----YQQSNQENLEQAFNVAERDLGVTRLLD 1348
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVaaslSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1838104091 1349 PEDVDVPHPDEKSIITYVSSL 1369
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
1274-1372 |
8.22e-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: 79.15 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1274 KLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLD-PEDV 1352
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1838104091 1353 DVPHPDEKSIITYVSSLYDV 1372
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3252-3801 |
1.21e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3252 KEAEFEAAKRAQAENAALEQKKKADAemakhkklAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLlddelqRLKDEVDDA 3331
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEE--------AKKTETGKAEEARKAEEAKKKAEDARKAEEA------RKAEDARKA 1142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3332 VKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEE---AENMKRLakEAAILSVESQEASRLRQI 3408
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElrkAEDARKA--EAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3409 AEEDLVQQRALAEKMLKEKMQAiQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDE--ETEEYQKSLEAERKR 3486
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkKAEEKKKADEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3487 QLEIVAEAEKLKLQVSQLSVAQAKAEEEakrfKKQADNIAARLLETEIA--TKDKSTVMQQLEVERRNNSKEADDLRNAI 3564
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEA----KKKADAAKKKAEEAKKAaeAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3565 ANLETEKAR-----------LKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKErliEDEKKRLESQYE 3633
Cdd:PTZ00121 1376 AKKKADAAKkkaeekkkadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA---EEAKKADEAKKK 1452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3634 -EEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKK----RLEQEKVLAEENKKLRD 3708
Cdd:PTZ00121 1453 aEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKKAEE 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3709 QLQQLEEAQKEKNTQVISAATVETTKNVYNGQNAGDVVDSVENKPDPLSFDGIRDKVPASRLRDVGLLSKKEfdklKKGK 3788
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE----KKMK 1608
|
570
....*....|...
gi 1838104091 3789 ATVQQLGETEKLK 3801
Cdd:PTZ00121 1609 AEEAKKAEEAKIK 1621
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2242-2886 |
2.56e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2242 DAKEVESYRAKLKKMRAEAEGEQPVFDSLEEELQKATTVSEkmsrvhsERDIELDHFRQNVSGLQDRWKAVFTQMEIRHR 2321
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA-------ELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2322 ELEQLGRQLGYYHESydwlihwITDAKERQEKIQAvsitdskTLKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIK 2401
Cdd:COG1196 296 ELARLEQDIARLEER-------RRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2402 DYELQLVAYNAKADPhasplkknkmdsasdnIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQK 2481
Cdd:COG1196 362 EAEEALLEAEAELAE----------------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2482 KMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAEnqkkNIELELHELKKLSEQQINDKSQLV 2561
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA----ALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2562 DDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRK 2641
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2642 SEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTskleeslkQEH 2721
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT--------LEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2722 GTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAE 2801
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2802 ESALKQKEMAEKELERQRKVADSTAQQKL-TAEQELIRLRA--------------EFDNAEQQRSLLEDElyrlKNEVIA 2866
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLeELERELERLEReiealgpvnllaieEYEELEERYDFLSEQ----REDLEE 809
|
650 660
....*....|....*....|
gi 1838104091 2867 AqqqRKQLEDELAKMRSEME 2886
Cdd:COG1196 810 A---RETLEEAIEEIDRETR 826
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
1272-1370 |
3.93e-16 |
|
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: 77.43 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1272 KEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED 1351
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1838104091 1352 -VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2927-3731 |
5.03e-16 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 86.42 E-value: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2927 LRAIAEEAKYQRQIAEEEAARQRAEAERILKEKlaaISEATRLKTEAeialkEKEAeNERLRRAAEDEAYQRKALEDEAN 3006
Cdd:NF041483 78 LRNAQIQADQLRADAERELRDARAQTQRILQEH---AEHQARLQAEL-----HTEA-VQRRQQLDQELAERRQTVESHVN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3007 -------QHKKEIEEKIVQLKKSSQAEMqrQKAMVDDTLKQRRVVEEEIRILKLNFEKASSgkldlelelnklkniaeET 3079
Cdd:NF041483 149 envawaeQLRARTESQARRLLDESRAEA--EQALAAARAEAERLAEEARQRLGSEAESARA-----------------EA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3080 QQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQR---------KIAQDELDRLKKKAEEARKQKDKAD 3150
Cdd:NF041483 210 EAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQaaelsraaeQRMQEAEEALREARAEAEKVVAEAK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3151 SEAEKQIVAA-SQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVL-------LRKQ 3222
Cdd:NF041483 290 EAAAKQLASAeSANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAaedtaaqLAKA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3223 AEEAESQKAAAEKEAAIQAK-AQEDAERLRKEAEFEAAK-RAQAENAALEQKKKADAEM----AKHKKLAEQTLKQKFQV 3296
Cdd:NF041483 370 ARTAEEVLTKASEDAKATTRaAAEEAERIRREAEAEADRlRGEAADQAEQLKGAAKDDTkeyrAKTVELQEEARRLRGEA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3297 EQeltkvkLKLDDTDKQKDLLDDELQRLKDEVDDAVKqrgQVEEELFKVKVQMEELlkvKLKIEKENQLLIKKDKDKAQQ 3376
Cdd:NF041483 450 EQ------LRAEAVAEGERIRGEARREAVQQIEEAAR---TAEELLTKAKADADEL---RSTATAESERVRTEAIERATT 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3377 LLAEEAENMKRLAKEAAILSVESQE-ASRLRQIAEEDLVQQRALAEK-MLKEKMQAIQEASRLKAEAEllqrQKDLAQEQ 3454
Cdd:NF041483 518 LRRQAEETLERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAE----ERLTAAEE 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3455 AQR-LLEDKELMQKRLDEETEEyQKSLEAERKRQLEIVAEAEKLKLQ---VSQLSVAQAKAEEEAKRFKKQADNIAARLL 3530
Cdd:NF041483 594 ALAdARAEAERIRREAAEETER-LRTEAAERIRTLQAQAEQEAERLRteaAADASAARAEGENVAVRLRSEAAAEAERLK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3531 ETEIATKDKSTVMQQLEVERRnnskeADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQI-EHEKTMLQQTFLT 3609
Cdd:NF041483 673 SEAQESADRVRAEAAAAAERV-----GTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERArEQSEELLASARKR 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3610 EKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEAlskqkeAEREMLNKQKEMQELE 3689
Cdd:NF041483 748 VEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHA------AERTRTEAQEEADRVR 821
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1838104091 3690 KKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVE 3731
Cdd:NF041483 822 SDAYAERERASEDANRLRREAQEETEAAKALAERTVSEAIAE 863
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5145-5183 |
5.26e-16 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 74.67 E-value: 5.26e-16
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 5145 LLEAQIATGGIIDPEKSHRLPVEVAYKRGFFDEEMNEIL 5183
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2346-3140 |
6.83e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.79 E-value: 6.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2346 DAKERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQLVAYNAKADPHASPLKKN- 2424
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLq 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2425 -KMDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQKKMADLQAeldkqKKLAEAHAKA 2503
Cdd:pfam02463 285 eEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI-----KREAEEEEEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2504 IAKAEKEADELKHQMKQEVSKREVAALDAENQKKNIELELHELKKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLE 2583
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2584 TTL----NQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDL 2659
Cdd:pfam02463 440 ELKqgklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2660 ENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVE----------------KTSKLEESLKQEHGT 2723
Cdd:pfam02463 520 VGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRaltelplgarklrlliPKLKLPLKSIAVLEI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2724 VLQLQQEAAHLKKQQEDALKARE------EAEKELDKWRQKANEALRLRLQAEEEAHK-----------KSLAQEEAEKQ 2786
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAkvvegiLKDTELTKLKESAKAKESGLRKGVSLEEGlaeksevkaslSELTKELLEIQ 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2787 KEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRA--EFDNAEQQRSLLEDELYRLKNEV 2864
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIneELKLLKQKIDEEEEEEEKSRLKK 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2865 IAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKEtmsntEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEE 2944
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE-----EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2945 AARQRAEAERILKEKLAAISEATRLktEAEIALKEKEAENERLRRAAEDEayqrKALEDEANQHKKEIEEKIVQLKKSSQ 3024
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERL--EEEITKEELLQELLLKEEELEEQ----KLKDELESKEEKEKEEKKELEEESQK 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3025 AEMQRQKamvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELE-LNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKR 3103
Cdd:pfam02463 909 LNLLEEK---ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEE 985
|
810 820 830
....*....|....*....|....*....|....*..
gi 1838104091 3104 RREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAE 3140
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2630-3501 |
8.50e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2630 KKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERkVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEK 2709
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2710 TSKLEeslkqehgtvlQLQQEAAHLKKQQEDALKAREEAEKELDKwrQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEE 2789
Cdd:TIGR02169 250 EEELE-----------KLTEEISELEKRLEEIEQLLEELNKKIKD--LGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2790 AEREAKKRAKAEE---SALKQKEMAEKELERQRKvadstaqqkltaeqELIRLRAEFDNAEQQRSLLEDELYRLKNEVIA 2866
Cdd:TIGR02169 317 LEDAEERLAKLEAeidKLLAEIEELEREIEEERK--------------RRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2867 AQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAA 2946
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2947 RQRAEAERI--LKEKLAAISEatRLkTEAEIALKEKEAEnerlRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKK--- 3021
Cdd:TIGR02169 463 DLSKYEQELydLKEEYDRVEK--EL-SKLQRELAEAEAQ----ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSvge 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3022 ------SSQAEMQRQKAMVDDTLkqrrVVEEEIRILKLnfEKASSGKLdleLELNKLKniAEETQQSKLRAEE------- 3088
Cdd:TIGR02169 536 ryataiEVAAGNRLNNVVVEDDA----VAKEAIELLKR--RKAGRATF---LPLNKMR--DERRDLSILSEDGvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3089 --EAEKQRKLAMEEEKRRREaeeTVKKITAAEKEAGRQRKIAQD--------------------ELDRLKKKAEEARKQK 3146
Cdd:TIGR02169 605 lvEFDPKYEPAFKYVFGDTL---VVEDIEAARRLMGKYRMVTLEgelfeksgamtggsraprggILFSRSEPAELQRLRE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3147 DKADSEAEKQIVAASQaalkcRTAEQQVQSVLAQQKEDSMMHKKLQQEyekakklakeaeaakekaekeavLLRKQAEEA 3226
Cdd:TIGR02169 682 RLEGLKRELSSLQSEL-----RRIENRLDELSQELSDASRKIGEIEKE-----------------------IEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3227 ESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLK 3306
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEAR 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3307 LDDTDK-------QKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKDKDkaqqlLA 3379
Cdd:TIGR02169 814 LREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LK 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3380 EEAENMKRLAKEAAIlSVESQEAS--RLRQIAEEDLVQQRALAE--KMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQA 3455
Cdd:TIGR02169 889 KERDELEAQLRELER-KIEELEAQieKKRKRLSELKAKLEALEEelSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3456 QRL-------LEDKELMQKRLDEETEEYQKsLEAERKRQLEIVAEAEKLKLQV 3501
Cdd:TIGR02169 968 RALepvnmlaIQEYEEVLKRLDELKEKRAK-LEEERKAILERIEEYEKKKREV 1019
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1149-1251 |
8.80e-16 |
|
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: 76.42 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1149 DRVQKKTFTKWVNKHLIKRAESQhhVTDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHKLQNVQIALDFLRHR- 1224
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDl 79
|
90 100
....*....|....*....|....*..
gi 1838104091 1225 QVKLVNIRNDDIADGNPKLTLGLIWTI 1251
Cdd:cd21225 80 KIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3436-3727 |
1.09e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3436 RLKAEAELLQRQKDLAQEQAQRLledkelmqKRLDEE---TEEYQK-SLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKA 3511
Cdd:COG1196 180 KLEATEENLERLEDILGELERQL--------EPLERQaekAERYRElKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3512 EEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQ--------- 3582
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEeelaeleee 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3583 ----NKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKL--MEEE 3656
Cdd:COG1196 332 leelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELeeAEEA 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3657 KKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISA 3727
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
1275-1370 |
1.52e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.86 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1275 LLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAErDLGVTRLLDPED-VD 1353
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1838104091 1354 VPHPDEKSIITYVSSLY 1370
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2954-3731 |
1.85e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2954 RILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQH------KKEIEEKIVQLKKSSQAEM 3027
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3028 QRQKAMVDdtlKQRRVVEEEIrilklnfEKASSGKLDLELELNKLKNIAEE--TQQSKLRAEEEAEKQRKLAmeeeKRRR 3105
Cdd:TIGR02169 236 ERQKEAIE---RQLASLEEEL-------EKLTEEISELEKRLEEIEQLLEElnKKIKDLGEEEQLRVKEKIG----ELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3106 EAEETVKKITAAE---KEAGRQRKIAQDELDRLKKKAEEARKQ--KDKADSEAEKQIVAASQAALkcRTAEQQVQSVLAQ 3180
Cdd:TIGR02169 302 EIASLERSIAEKErelEDAEERLAKLEAEIDKLLAEIEELEREieEERKRRDKLTEEYAELKEEL--EDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3181 QKEDSMMHKKLQQEyekakklakeaeaakekaekeavlLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRkeaefEAAK 3260
Cdd:TIGR02169 380 FAETRDELKDYREK------------------------LEKLKREINELKRELDRLQEELQRLSEELADLN-----AAIA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3261 RAQAENAALEQKKK-ADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDtdkqkdlLDDELQRLKDEVDDAVKQRGQVE 3339
Cdd:TIGR02169 431 GIEAKINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3340 EELFKvkvqmeellkvklkiEKENQLLIKKDKDKAQQLLAEEAEnmkrlAKEAAILSVESQEASRLRQIA-EEDLVQQRA 3418
Cdd:TIGR02169 504 ERVRG---------------GRAVEEVLKASIQGVHGTVAQLGS-----VGERYATAIEVAAGNRLNNVVvEDDAVAKEA 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3419 LaeKMLKE------------KMQAIQEASRLKAEAELLQRQKDLAQ----------------------EQAQRLL----- 3459
Cdd:TIGR02169 564 I--ELLKRrkagratflplnKMRDERRDLSILSEDGVIGFAVDLVEfdpkyepafkyvfgdtlvvediEAARRLMgkyrm 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3460 ---------------------EDKELMQKRLDEETEEYQKSLEaERKRQLEIV-AEAEKLKLQVSQLSVAQAKAEEEAKR 3517
Cdd:TIGR02169 642 vtlegelfeksgamtggsrapRGGILFSRSEPAELQRLRERLE-GLKRELSSLqSELRRIENRLDELSQELSDASRKIGE 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3518 FKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQnksKEMADAQMKQIE 3597
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQ 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3598 HEKTMLqqtfltEKEMLLKKERLIEDE----KKRLESQYEEEAKK-AKALTDEQERQRKLMEEEKKKLHATMDEALSKQK 3672
Cdd:TIGR02169 798 AELSKL------EEEVSRIEARLREIEqklnRLTLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3673 EAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVE 3731
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2586-3475 |
2.65e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2586 LNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALE-DLENLKM 2664
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2665 QAEEAERKVKQAQiEKEKQIQiahvaaeksatAELQSTQrsfvEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKA 2744
Cdd:TIGR02169 309 SIAEKERELEDAE-ERLAKLE-----------AEIDKLL----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQKANEaLRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEesaLKQKEMAEKELERQRKVADS 2824
Cdd:TIGR02169 373 LEEVDKEFAETRDELKD-YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2825 TAQQkltAEQELIRLRAefdnaeqQRSLLEDELYRLKNEViaaqqqrKQLEDELAKMRSEMEILIQLKSRAEKETMSNTE 2904
Cdd:TIGR02169 449 EIKK---QEWKLEQLAA-------DLSKYEQELYDLKEEY-------DRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2905 KSKMLLDAEASKMRDVAEeagklrAIAEEAKYqrQIAEEEAARQR------------AEAERILKEKlaAISEATRL--- 2969
Cdd:TIGR02169 512 VEEVLKASIQGVHGTVAQ------LGSVGERY--ATAIEVAAGNRlnnvvveddavaKEAIELLKRR--KAGRATFLpln 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2970 KTEAEIALKEKEAENERLRRAAEDEAYQRKAledeanqhkkeieEKIVqlkkssqaemqrqKAMVDDTLkqrrVVE--EE 3047
Cdd:TIGR02169 582 KMRDERRDLSILSEDGVIGFAVDLVEFDPKY-------------EPAF-------------KYVFGDTL----VVEdiEA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3048 IRILKLNFEKASsgkLDLELeLNKLKNIAEETQQSKLRAEEEAEKQRKLAMeeekrrreaeetvkkITAAEKEAGRQRKI 3127
Cdd:TIGR02169 632 ARRLMGKYRMVT---LEGEL-FEKSGAMTGGSRAPRGGILFSRSEPAELQR---------------LRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3128 AQDELDRLKKKAEEARkqkdKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSmmhKKLQQEYEKAKKLAKEAEA 3207
Cdd:TIGR02169 693 LQSELRRIENRLDELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL---SSLEQEIENVKSELKELEA 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3208 AKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKraQAENAALEQKKKADAEMAKHKKLAE 3287
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE--QKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3288 QTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlkvKLKIEKENQLLi 3367
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL---EAQIEKKRKRL- 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3368 KKDKDKAQQLLAEEAEnmkrLAKEAAILSVESQEASRLRQIAEEDLVQQRALaEKMLKEKMQAIQEAsrlkaeAELLQRQ 3447
Cdd:TIGR02169 920 SELKAKLEALEEELSE----IEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEY------EEVLKRL 988
|
890 900
....*....|....*....|....*...
gi 1838104091 3448 KDLaQEQAQRLLEDKELMQKRLDEETEE 3475
Cdd:TIGR02169 989 DEL-KEKRAKLEEERKAILERIEEYEKK 1015
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
1270-1370 |
5.18e-15 |
|
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: 74.34 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAErDLGVTRLLDP 1349
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1838104091 1350 ED-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4831-4869 |
7.04e-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: 7.04e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 4831 LLEAQAATGFIVDPVNNETLTVDEAVRKGVVGPELHDKL 4869
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2463-3198 |
7.11e-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: 82.42 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2463 RRLEDEEKAAKILKAEEQKK-----MADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVS------KREVAALD 2531
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEaierqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2532 AE--NQKKNIELELHELKKLSEQQINDKSQlvddalqsRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREkaaEAERL 2609
Cdd:TIGR02169 301 AEiaSLERSIAEKERELEDAEERLAKLEAE--------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKE---ELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2610 RKLAQEEAEKlHKQVIEETQKKRTAEEELKRKSE----AEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKE-KQI 2684
Cdd:TIGR02169 370 RAELEEVDKE-FAETRDELKDYREKLEKLKREINelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdKAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2685 QIahvaaeKSATAELQSTQrsfvEKTSKLEESLkqehgtvLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEAlr 2764
Cdd:TIGR02169 449 EI------KKQEWKLEQLA----ADLSKYEQEL-------YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG-- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2765 lrlQAEEEAHKKSLAQEEAEKQKEEAEREakKRAKAEESAL---------KQKEMAEK--ELERQRKVADST--AQQKLT 2831
Cdd:TIGR02169 510 ---RAVEEVLKASIQGVHGTVAQLGSVGE--RYATAIEVAAgnrlnnvvvEDDAVAKEaiELLKRRKAGRATflPLNKMR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2832 AEQELIRLRAE------------------------------FDNAEQQRSL--------LEDELY------------RLK 2861
Cdd:TIGR02169 585 DERRDLSILSEdgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLmgkyrmvtLEGELFeksgamtggsraPRG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2862 NEVIAAQQQRK--QLEDELAKMRSEMEILIQLKSRAEKEtmsntekskmlLDAEASKMRDVAEEAGKLRAiaeeakyQRQ 2939
Cdd:TIGR02169 665 GILFSRSEPAElqRLRERLEGLKRELSSLQSELRRIENR-----------LDELSQELSDASRKIGEIEK-------EIE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2940 IAEEEAARQRAEAERiLKEKLAAISEAtrlKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHK-KEIEEKIVQ 3018
Cdd:TIGR02169 727 QLEQEEEKLKERLEE-LEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3019 LKKssqaEMQRQKAMVDDtlkqrrvVEEEIRILKLNFEKASSGKLDLELELNKLKNiaeetQQSKLRAEEEAEKQRKLAM 3098
Cdd:TIGR02169 803 LEE----EVSRIEARLRE-------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEEL 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3099 EEEkrrreaeetVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVL 3178
Cdd:TIGR02169 867 EEE---------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1838104091 3179 AQQKEDS-------------MMHKKLQ--------------QEYEKA 3198
Cdd:TIGR02169 938 DPKGEDEeipeeelsledvqAELQRVEeeiralepvnmlaiQEYEEV 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2468-2898 |
7.95e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.74 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2468 EEKAAKILKAEEQKKMADLQA--ELDKQKKLAEAHAKAIAKAEKEADELKHQMKQevSKREVAALDAENQKKNIELELHE 2545
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKElkELEEELKEAEEKEEEYAELQEELEELEEELEE--LEAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2546 L---KKLSEQQINDKSQLVDDALQSRTkieeeihiiriQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHK 2622
Cdd:COG4717 130 LyqeLEALEAELAELPERLEELEERLE-----------ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2623 QVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDlenlKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAEL--- 2699
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLEN----ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLilt 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2700 ----------------QSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQkANEAL 2763
Cdd:COG4717 275 iagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2764 RLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEK--ELERQRKVADSTAQQKLTAEQElIRLRA 2841
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDE-EELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 2842 EFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLE--DELAKMRSEMEILIQLKSRAEKE 2898
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEE 491
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
1152-1255 |
8.38e-15 |
|
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: 73.49 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1152 QKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMRfhklQNVQIALDFLRHRQ 1225
Cdd:cd21213 1 QLQAYVAWVNSQLKKRPGIRP-VQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKR 75
|
90 100 110
....*....|....*....|....*....|
gi 1838104091 1226 VKLVNIRNDDIADGNPKLTLGLIWTIILHF 1255
Cdd:cd21213 76 IRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2582-3097 |
1.25e-14 |
|
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: 81.81 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2582 LETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKqviEETQKKRTAEEELKRKSE-------AEKEAAKQKQK 2654
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA---ELNQLLRTLDDQWKEKRDelngelsAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2655 ALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAeLQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAahL 2734
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK--L 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2735 KKQQEDALKAREEAEKELDK----WRQKANEALRlRLQAEEEAHKKSLAqeeaekqkeeaerEAKKR---AKAEESALKQ 2807
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQAleseLREQLEAGKL-EFNEEEYRLKSRLG-------------ELKLRlnqATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2808 KEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQ------------RKQL- 2874
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEAp 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2875 --EDELAKMRSEmeiliQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEA 2952
Cdd:pfam12128 546 dwEQSIGKVISP-----ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2953 ERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKA 3032
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 3033 MVDDTLKQRRvveeEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLA 3097
Cdd:pfam12128 701 WLEEQKEQKR----EARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLA 761
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1270-1370 |
1.42e-14 |
|
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: 73.14 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAErDLGVTRLLDP 1349
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1838104091 1350 ED-VDVPHPDEKSIITYVSSLY 1370
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2596-3152 |
1.79e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2596 LKQLREKAAEA----ERLRKLAQEEAEKLHKQV--IEET----------QKKRTAEEELKRKSEAEKEAAKQKQKALEDL 2659
Cdd:PRK02224 164 LEEYRERASDArlgvERVLSDQRGSLDQLKAQIeeKEEKdlherlngleSELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2660 ENLKMQAEEAErkVKQAQIEkEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGtVLQLQQEAahLKKQQE 2739
Cdd:PRK02224 244 EEHEERREELE--TLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEA--VEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2740 DALKAREEAEKELDKWRQKA----NEALRLRLQAEEeahkkslaqeeaekqkeEAEREAKKRAKAEEsalkqkemAEKEL 2815
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAqahnEEAESLREDADD-----------------LEERAEELREEAAE--------LESEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2816 ERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEiliqlKSRA 2895
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE-----EAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2896 EKETMSNTEKSKMLLDAE-ASKMRDVAEEAGKLRAIAEEAKYQRQIAEE--EAARQRAEAERILKEKLAAISEATRLKTE 2972
Cdd:PRK02224 448 LLEAGKCPECGQPVEGSPhVETIEEDRERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2973 AEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLkkssqAEMQRQKAMVDDTLKQRRVVEEEirilk 3052
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESLERIRTL----- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3053 lnFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAmeeekrrreaeetvKKITAAEKEAGRQRKI-AQDE 3131
Cdd:PRK02224 598 --LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE--------------AEFDEARIEEAREDKErAEEY 661
|
570 580
....*....|....*....|.
gi 1838104091 3132 LDRLKKKAEEARKQKDKADSE 3152
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAE 682
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2925-3741 |
2.01e-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: 81.17 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2925 GKLRAIAEEAKYQRQIAEEEAARQRAEAERILKeklaaiSEATRLKTEAEIALKEKEAENERLRRAaedeaYQRKALEDE 3004
Cdd:TIGR00618 52 GKLPRRSEVIRSLNSLYAAPSEAAFAELEFSLG------TKIYRVHRTLRCTRSHRKTEQPEQLYL-----EQKKGRGRI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3005 ANQHKKEIEEKIVQLKKSSQAEMQRQKamvddTLKQRRVVeeeiRILKLNFEKASSGKLDLElELNKLKNIAEET--QQS 3082
Cdd:TIGR00618 121 LAAKKSETEEVIHDLLKLDYKTFTRVV-----LLPQGEFA----QFLKAKSKEKKELLMNLF-PLDQYTQLALMEfaKKK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3083 KLRAEEEAEKQR-KLAMEEEKRRREAEETVKKITAAE----KEAGRQRKIAQDELDRLKKKAEEaRKQKDKADSEAEKQI 3157
Cdd:TIGR00618 191 SLHGKAELLTLRsQLLTLCTPCMPDTYHERKQVLEKElkhlREALQQTQQSHAYLTQKREAQEE-QLKKQQLLKQLRARI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3158 VAASqaALKCRTAEQQVQSVLAQQKEDSMMHKKlQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEA 3237
Cdd:TIGR00618 270 EELR--AQEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3238 AIQAKAQEDaeRLRKEAEFEAAKRAQAENA-ALEQKKKADAEMAKHKKLAEQTLKQKFQVEQEL--TKVKLKLDDTDKQK 3314
Cdd:TIGR00618 347 LQTLHSQEI--HIRDAHEVATSIREISCQQhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqaTIDTRTSAFRDLQG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3315 DLLDDELQRLKDEVDDAVKQRG---QVEEELFKVKVQMEELLKVKLKIEKENQL--LIKKDKDKAQ---QLLAEEAENMK 3386
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAitcTAQCEKLEKIHLQESAQSLKEREQQLQTKeqIHLQETRKKAvvlARLLELQEEPC 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3387 RLAKEAAILSVESQ-----EASRLRQIAEEDLVQQRALAEKMLKEKMQAIQE-ASRLKAEAELLQRQKDLAQEQAQRLLE 3460
Cdd:TIGR00618 505 PLCGSCIHPNPARQdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKqRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3461 DKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVA---QAKAEEEAKRfKKQADNIAARLLETEIATK 3537
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlhlQQCSQELALK-LTALHALQLTLTQERVREH 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3538 DKSTVMQQLEVERRNNSKEaDDLRNAIANLETEKARLKKDAEELQN--KSKEMADAQMKQIEHEKTMLQQTFLTEKEMLL 3615
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLAL-QKMQSEKEQLTYWKEMLAQCQTLLREleTHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3616 K-KERLIEDEKKRLESQYEEEAKKAKAL-----TDEQERQRKLMEEEKKKLHATmDEALSKQKEAEREMLNKQKEM---- 3685
Cdd:TIGR00618 743 QsLKELMHQARTVLKARTEAHFNNNEEVtaalqTGAELSHLAAEIQFFNRLREE-DTHLLKTLEAEIGQEIPSDEDilnl 821
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3686 -QELEKKRLEQEKVLAEENKK----LRDQLQQLEEAQKEKNTQVISAATVETTKNVYNGQN 3741
Cdd:TIGR00618 822 qCETLVQEEEQFLSRLEEKSAtlgeITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN 882
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2363-2905 |
2.21e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2363 KTLKEQLSQEKKLL---EEIENNKENVDECQKYAKAYINSIKDYELQLVAYNAKADPHASPLKKNKMDSASDNIiqEYVT 2439
Cdd:PRK03918 172 KEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK--ELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2440 LRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKA--EEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQ 2517
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2518 MKqEVSKREVAALDAENQKKNIELELHELKKlSEQQINDKSQLVDDALQSRTKIEEEIHII-RIQLETTLNQKSTAETEL 2596
Cdd:PRK03918 330 IK-ELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2597 KQLREKAAEAERL---RKLAQEEAEK------LHKQVIEETQKKRTAEE---ELKRKSEAEKEAAKQKQKALEDLENLKM 2664
Cdd:PRK03918 408 SKITARIGELKKEikeLKKAIEELKKakgkcpVCGRELTEEHRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2665 QAEEAERKVKQAQI--------EKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGtvlqLQQEAAHLKK 2736
Cdd:PRK03918 488 VLKKESELIKLKELaeqlkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2737 QQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELE 2816
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2817 RQRKVADSTAQ------------QKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDeLAKMRSE 2884
Cdd:PRK03918 644 ELRKELEELEKkyseeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALER 722
|
570 580
....*....|....*....|....*
gi 1838104091 2885 MEILIQ----LKSRAEKETMSNTEK 2905
Cdd:PRK03918 723 VEELREkvkkYKALLKERALSKVGE 747
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1173-1252 |
3.37e-14 |
|
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: 71.85 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1173 HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM----RFHKLQNVQIALDFLRHRQV----KLVNIRNDDIADGNPKLT 1244
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1838104091 1245 LGLIWTII 1252
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4498-4536 |
3.49e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 3.49e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 4498 LLEAQAATGFLVDPVRNQFLTVDEAVKSGLVGPELHEKL 4536
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3421-3719 |
4.02e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.78 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3421 EKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKElmQKRLDEETEEyqKSLEAERKRQLEivaEAEKLK-L 3499
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKME--QERLRQEKEE--KAREVERRRKLE---EAEKARqA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3500 QVSQLSVAQAKAEEEAKRFKKQADNIA--------ARLLETEIATK-DKSTVMQQLEVERRNnskeaddlRNAIANLETE 3570
Cdd:pfam17380 328 EMDRQAAIYAEQERMAMERERELERIRqeerkrelERIRQEEIAMEiSRMRELERLQMERQQ--------KNERVRQELE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3571 KARLKKDAEELQNKSKEMADAQMKQI--EHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLES-----QYEEEAKKAKALT 3643
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIraEQEEARQREVRRLEEERAREMERVRLEEQERQQQverlrQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3644 DEQERQRKLMEEEKKK-LHATMDEALSKQKEAEREMLNKQKEMQELEKKRL-EQEKVLAEENKKLRDQLQQLEEAQKE 3719
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeEERRREAEEERRKQQEMEERRRIQEQ 557
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3398-3696 |
6.48e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.01 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3398 ESQEASRLRQIAEEDL--VQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEE 3475
Cdd:pfam17380 294 EKMEQERLRQEKEEKAreVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3476 YQKSLEAERkRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKstvMQQLEVERrnnSK 3555
Cdd:pfam17380 374 ISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE---VRRLEEER---AR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3556 EADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKtmlQQTFLTEKEMLLKKERLIEDEKKR--LESQYE 3633
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQAMIEEERKRklLEKEME 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 3634 -------EEAKKAKAltdEQERQRKLMEEEKKKLHATMDEALSKQK-----EAEREMLnkqKEMQELEKKRLEQE 3696
Cdd:pfam17380 524 erqkaiyEEERRREA---EEERRKQQEMEERRRIQEQMRKATEERSrleamEREREMM---RQIVESEKARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2793-3025 |
1.15e-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: 76.34 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2793 EAKKRAKAEESALKQK-EMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQR 2871
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2872 KQLEDELAKMRSEMeiliqlksraekETMSNTEKSKMLLDAEaskmrDVAEEAGKLRAIAEEAKYQRQIAEE------EA 2945
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAPARREQAEElradlaEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2946 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQA 3025
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3319-3737 |
1.36e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.89 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3319 DELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLL-IKKDKDKAQQLLAEEAENMKRL-AKEAAILS 3396
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELeERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3397 VESQEASRLRQIAEEdlvqQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEY 3476
Cdd:COG4717 161 LEEELEELEAELAEL----QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3477 QKSLEAERKRQLEIVAE----------------------AEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEI 3534
Cdd:COG4717 237 EAAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3535 ATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEmadaqmkqiEHEKTMLQQTFLTEKEML 3614
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE---------QEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3615 LKKERL------IEDEKKRLESQYEEEAKKAKALTDEQERQRklMEEEKKKLHATMDEAlskqkEAEREMLNKQKEMQEL 3688
Cdd:COG4717 388 RAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEEL-----EEELEELREELAELEA 460
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1838104091 3689 EKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVETTKNVY 3737
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2453-3189 |
2.83e-13 |
|
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: 77.47 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2453 QYIKFITETQRRLEDEEkaakilKAEEQKKMADLQAELDKQKKLAEahakaiakAEKEADELKHQMKQEVSKREvaalDA 2532
Cdd:pfam15921 82 EYSHQVKDLQRRLNESN------ELHEKQKFYLRQSVIDLQTKLQE--------MQMERDAMADIRRRESQSQE----DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2533 ENQKKNIELELHELKKLSEQQINDKSqlvddalqsrtkieeeihiirIQLETTLNQKSTAETELKQLREKAAEAErlrkl 2612
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSN---------------------TQIEQLRKMMLSHEGVLQEIRSILVDFE----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2613 aQEEAEKLHKQVIEETQKKR---TAEEELKRKSEAEKEAAKQKQKALED-LENLKMQAE---EAERKVKQAQIEK---EK 2682
Cdd:pfam15921 198 -EASGKKIYEHDSMSTMHFRslgSAISKILRELDTEISYLKGRIFPVEDqLEALKSESQnkiELLLQQHQDRIEQlisEH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2683 QIQIAHVaAEKSATAELQS----TQRSFVEKTSKLEESLKQEH-----GTVLQLQQEAAHLKKQQEDALkarEEAEKELD 2753
Cdd:pfam15921 277 EVEITGL-TEKASSARSQAnsiqSQLEIIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYEDKI---EELEKQLV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2754 KWRQKANEALRLRLQAEEEAH------KKSLAQEEAEKQKEEAEREAKKRAKAEESALK------QKEMAEKELERQR-- 2819
Cdd:pfam15921 353 LANSELTEARTERDQFSQESGnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTGNSitidhlRRELDDRNMEVQRle 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2820 ---KVADSTAQQKLtaEQELIRLRAEFDNAEQQRSL---LEDELYRLKNEVIAAQQQRKQLEDElAKMRSEMEILIQLKS 2893
Cdd:pfam15921 433 allKAMKSECQGQM--ERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKE 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2894 RAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQR-QIAEE----EAARQRAEAerilKEKLAAISEATR 2968
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKdkviEILRQQIEN----MTQLVGQHGRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2969 LKTEAEIALKEKEAENERLrraaedEAYQRKALEDEANQHKKEIEEKIVQLK----KSSQAEMQRQKAMVDdtLKQRR-- 3042
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRL------ELQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKD--IKQERdq 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3043 -------------VVEEEIRILKLNFEKAS------SGKLDLEL-----ELNKLKNIAEETQQSKLRAEEEAEKQRKLAM 3098
Cdd:pfam15921 658 llnevktsrnelnSLSEDYEVLKRNFRNKSeemettTNKLKMQLksaqsELEQTRNTLKSMEGSDGHAMKVAMGMQKQIT 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3099 EEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAE---------KQIVAASQAAL-KCR 3168
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEvlrsqerrlKEKVANMEVALdKAS 817
|
810 820
....*....|....*....|.
gi 1838104091 3169 TAEQQVQSVLAQQKEDSMMHK 3189
Cdd:pfam15921 818 LQFAECQDIIQRQEQESVRLK 838
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1145-1254 |
2.87e-13 |
|
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: 69.23 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1145 EDERDrvqKKTFTKWVNKHLIKraesqHHVTDLYEDLRDGhnlISLLEVLsgDTL-P---------REKGRMRFHKLQNV 1214
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLD-----PLINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENC 67
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1838104091 1215 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1254
Cdd:cd21219 68 NYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2726-3719 |
4.25e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 76.75 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2726 QLQQEAAHLKKQQEDALKAREEAeKELDKWRQKANE---ALRLRLQAEEE----AHKKSLAQEEAEKQKEEAEREAKKRA 2798
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESEL-KELEKKHQQLCEeknALQEQLQAETElcaeAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2799 KAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQeliRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDEL 2878
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQ---KLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2879 AKMRSEMeiliqlksrAEKEtmsntEKSKMLLDAEASKMRDVAEEAGKLRaiaEEAKyQRQiaEEEAARQRAEAEriLKE 2958
Cdd:pfam01576 162 SEFTSNL---------AEEE-----EKAKSLSKLKNKHEAMISDLEERLK---KEEK-GRQ--ELEKAKRKLEGE--STD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2959 KLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRkaleDEANQHKKEIEEKIVQLkkssQAEMQRQKAMVDDTL 3038
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQK----NNALKKIRELEAQISEL----QEDLESERAARNKAE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3039 KQRRvveeeirilklnfekassgklDLELELNKLKNIAEETQ-----QSKLRAEEEAE-KQRKLAMEEEkrrreaeetvK 3112
Cdd:pfam01576 292 KQRR---------------------DLGEELEALKTELEDTLdttaaQQELRSKREQEvTELKKALEEE----------T 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3113 KITAAEKEAGRQRKIAQdeLDRLKKKAEEARKqkDKADSEAEKQIVAASQAALKCRTaeqqvqSVLAQQKEDSMmHKKLQ 3192
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQA--LEELTEQLEQAKR--NKANLEKAKQALESENAELQAEL------RTLQQAKQDSE-HKRKK 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3193 QEyekakklakeaeaakekaekeavllrKQAEEAESQKAaaekeaaiqakaqeDAERLRKEAEfEAAKRAQAE----NAA 3268
Cdd:pfam01576 410 LE--------------------------GQLQELQARLS--------------ESERQRAELA-EKLSKLQSElesvSSL 448
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3269 LEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQkdlLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQ 3348
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ---LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3349 MEELlkvKLKIEKENQLL---------IKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEAS----RLRQIAEEDLVQ 3415
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLealeegkkrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldHQRQLVSNLEKK 602
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3416 QRALAEKMLKEKMQAIQEAS-RLKAEAEllQRQKDLAQEQAQRLLEdkELMQKRldEETEEYQKSLEAERKrqlEIVAEA 3494
Cdd:pfam01576 603 QKKFDQMLAEEKAISARYAEeRDRAEAE--AREKETRALSLARALE--EALEAK--EELERTNKQLRAEME---DLVSSK 673
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3495 EKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATkdkstvmQQLEVerrnnskeaddlrnaiaNLETEKARL 3574
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK-------LRLEV-----------------NMQALKAQF 729
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3575 KKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLiEDEKKRLESQYE------EEAKKA--KALTDEQ 3646
Cdd:pfam01576 730 ERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKL-ELDLKELEAQIDaankgrEEAVKQlkKLQAQMK 808
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3647 ERQRKLMEeekkkLHATMDEALSKQKEAEREMLNKQKEMQELE---------KKRLEQEK---------------VLAEE 3702
Cdd:pfam01576 809 DLQRELEE-----ARASRDEILAQSKESEKKLKNLEAELLQLQedlaaseraRRQAQQERdeladeiasgasgksALQDE 883
|
1050
....*....|....*..
gi 1838104091 3703 NKKLRDQLQQLEEAQKE 3719
Cdd:pfam01576 884 KRRLEARIAQLEEELEE 900
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2601-2864 |
6.28e-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: 75.93 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2601 EKAAEAERLRKLAQEEAEK---LHKQVIEETQKKRTA---EEELKRKSEAEK----EAAKQKQKALE-----DLENLKM- 2664
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARqaeMDRQAAIYAEQERMAmerERELERIRQEERkrelERIRQEEIAMEisrmrELERLQMe 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2665 ---------QAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLK 2735
Cdd:pfam17380 387 rqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2736 KQQEDALKAREEAEKELDKwRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKE---MAE 2812
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEeerRKQ 545
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 2813 KELERQRKVadstAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEV 2864
Cdd:pfam17380 546 QEMEERRRI----QEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1270-1367 |
7.67e-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: 67.79 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQ-RMTDGYQNircdNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSN-QENLEQAFNVAERDLGVTRLL 1347
Cdd:cd21230 1 TPKQRLLGWIQnKIPQLPIT----NFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLI 76
|
90 100
....*....|....*....|
gi 1838104091 1348 DPEDVDVPHPDEKSIITYVS 1367
Cdd:cd21230 77 TPEEIINPNVDEMSVMTYLS 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3243-3780 |
8.34e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3243 AQEDAERLRkEAEfEAAKRAQAENAALEQKKKADAEMAKHKKLAE--QTLKQKFQVEQELTKVKLKlddtDKQKDLLDDE 3320
Cdd:COG4913 230 LVEHFDDLE-RAH-EALEDAREQIELLEPIRELAERYAAARERLAelEYLRAALRLWFAQRRLELL----EAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3321 LQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL-LKVKLKIEKENQLLiKKDKDKAQQLLAEEAENMKRL----AKEAAIL 3395
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERL-ERELEERERRRARLEALLAALglplPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3396 SVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQK---DLAQEQAQRLLEDK---------- 3462
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDALAEAlgldeaelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3463 --ELMQKRLDEEteEYQKSLE-------------AERKRQ-LEIVaEAEKLKLQVSQLSVAQAKAEEEAKRFKKQ----- 3521
Cdd:COG4913 463 vgELIEVRPEEE--RWRGAIErvlggfaltllvpPEHYAAaLRWV-NRLHLRGRLVYERVRTGLPDPERPRLDPDslagk 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3522 ---ADNIAARLLETEIAtkDKSTVM-----QQLEVERR-------------------------------NNSKEADDLRN 3562
Cdd:COG4913 540 ldfKPHPFRAWLEAELG--RRFDYVcvdspEELRRHPRaitragqvkgngtrhekddrrrirsryvlgfDNRAKLAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3563 AIANLETEKARLKKDAEELQNKSKEMADaqmkQIEHEKTMLQQTFlTEKEMLLKKERL--IEDEKKRLES------QYEE 3634
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQE----RREALQRLAEYSW-DEIDVASAEREIaeLEAELERLDAssddlaALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3635 EAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLE-------QEKVLAEENKKLR 3707
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalGDAVERELRENLE 772
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3708 DQLQQLEEAQKEKNTQVISAatVETTKNVYNGqNAGDVVDSVENKPDplsFDGIRDkvpasRLRDVGLLSKKE 3780
Cdd:COG4913 773 ERIDALRARLNRAEEELERA--MRAFNREWPA-ETADLDADLESLPE---YLALLD-----RLEEDGLPEYEE 834
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2524-3168 |
8.56e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2524 KREVAALDAENQKKNIELELHELKKLSEQQINDKSQLvddalqsrtkieeeiHIIRIQLETTLNQKSTAETELKQLREKA 2603
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELI---------------KEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2604 AEAERLrklaqeeaeklhKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALED-LENLKMQAEEAERKVKQAQIEKEK 2682
Cdd:PRK03918 224 EKLEKE------------VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEErIEELKKEIEELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2683 qiqiahvAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEA 2762
Cdd:PRK03918 292 -------AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2763 LRLR-LQAEEEAHKKSLAQEEAEkqkeeaerEAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELirLRA 2841
Cdd:PRK03918 365 EEAKaKKEELERLKKRLTGLTPE--------KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--KKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2842 EFDNAEQQRSLLEDELYRLKNEVIAaqqqrkqledELAKMRSEMEILIQLKSRAEKEtMSNTEKsKMLLDAEASKMRDVA 2921
Cdd:PRK03918 435 KGKCPVCGRELTEEHRKELLEEYTA----------ELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESELIKLKELA 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2922 EEagkLRAIAEEAKyqrQIAEEEAARQRAEAERiLKEKLAAIS-EATRLKTEAEIA---LKEKEAENERLRRAAEDEAYQ 2997
Cdd:PRK03918 503 EQ---LKELEEKLK---KYNLEELEKKAEEYEK-LKEKLIKLKgEIKSLKKELEKLeelKKKLAELEKKLDELEEELAEL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2998 RKALEDEANQHKKEIEEKIVQLKKssqaeMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE 3077
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEP-----FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3078 ETQqsKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARK-QKDKADSEAEKQ 3156
Cdd:PRK03918 651 ELE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlEKALERVEELRE 728
|
650
....*....|..
gi 1838104091 3157 IVAASQAALKCR 3168
Cdd:PRK03918 729 KVKKYKALLKER 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3840-3877 |
8.82e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 8.82e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1838104091 3840 LLEAQAATGYMLDPIKNKKLSVNEAVKEGLIGPELHNK 3877
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1731-1920 |
1.04e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.55 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1731 LHAFISASTKELMWLNDKEEEEVNFDWSDKNPNMTAKKDNYSGLMRELELREKKVNDLQAMGERLVRDGHPGKKTVEDFT 1810
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1811 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRTTTATRLEDLLQDAVEEKELLNEY 1890
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1838104091 1891 KTLATSLNKRAKSIIQLKPRNPTTSIKGKL 1920
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1272-1371 |
1.25e-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: 66.98 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1272 KEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMgRVYQQSNQ----ENLEQAFNVAER-DLGVTRL 1346
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK-INKKPKSPfkkrENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....*
gi 1838104091 1347 LDPEDVdVPHPDEKSIITYVSSLYD 1371
Cdd:cd00014 80 FEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5419-5457 |
1.25e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.04 E-value: 1.25e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 5419 LLEAQACTGGIIDPTTGERLSVTDAEEKGLVDKIMVDRL 5457
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2592-3331 |
1.29e-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: 75.01 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2592 AETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKeaakQKQKALEDLENLKMQAEEAER 2671
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ----QTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2672 KVKQAQI----EKEKQIQIAHVAAEKSATaELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKK---QQEDALKA 2744
Cdd:TIGR00618 258 KQQLLKQlrarIEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKllmKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQKANEALRLRLQAEEEAhkkslaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEKELERQRKVAdS 2824
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVAT----------------SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL-C 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2825 TAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTE 2904
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2905 KskmLLDAEASKMrdvaeeagklraiAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEA-TRLKTEAEIALKEKEAE 2983
Cdd:TIGR00618 480 Q---IHLQETRKK-------------AVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPlTRRMQRGEQTYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2984 NERLRRAAEDEAYQRKALEDEAnQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQrrvVEEEIRILKLNFEKASSGKL 3063
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQM-QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEAEDMLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3064 DLELELNKLKNIAEETQQSKLRAEEEAEKQRKLameEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKA---E 3140
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQ---LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3141 EARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEdsmMHKKLQQEYEKAKKLA--KEAEAAKEKAEKEAVL 3218
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED---ALNQSLKELMHQARTVlkARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3219 LRKQAEEAESQKAAAEKEAAIQAKAQEDAErlrKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQkfqveQ 3298
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKT---LEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATL-----G 845
|
730 740 750
....*....|....*....|....*....|...
gi 1838104091 3299 ELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDA 3331
Cdd:TIGR00618 846 EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2432-3020 |
1.50e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2432 NIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQKKMADLqAELDKQKKLAEAHAKAIAKAEKEA 2511
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2512 DELKHQMKQ-EVSKREVAALDAENQKKNIELE-----LHELKKLSEQQINDKSQLVD--DALQSRTKIEEEIHIIRIQLE 2583
Cdd:PRK03918 248 ESLEGSKRKlEEKIRELEERIEELKKEIEELEekvkeLKELKEKAEEYIKLSEFYEEylDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2584 TTLNQKSTAETELKQLREKaaEAERLRKLaqEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKqkaLEDLENLK 2663
Cdd:PRK03918 328 ERIKELEEKEERLEELKKK--LKELEKRL--EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE---LEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2664 MQAEEAERKVKQ--AQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKleESLKQEHGTVLQLQQEAAHLKKQQEDA 2741
Cdd:PRK03918 401 EEIEEEISKITAriGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2742 LKAREEAEKELDKWRqkanEALRLRLQAEEeahKKSLAQEEAEKQKEEAEREAKKRAKAEESALKqkemaekeLERQRKV 2821
Cdd:PRK03918 479 RKELRELEKVLKKES----ELIKLKELAEQ---LKELEEKLKKYNLEELEKKAEEYEKLKEKLIK--------LKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2822 ADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIaaqqqrKQLEDELAKMRSEMEILIQLKSrAEKETMS 2901
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV------EELEERLKELEPFYNEYLELKD-AEKELER 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2902 NTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAK-YQRQIAEEEAARQR---AEAERILKEKLAAISEATRLKTEAEIAL 2977
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEeLEKKYSEEEYEELReeyLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1838104091 2978 KEKEAENERLRRAAEDEAYQRKALEDeanqhKKEIEEKIVQLK 3020
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALER-----VEELREKVKKYK 734
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2459-3002 |
1.55e-12 |
|
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: 74.39 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2459 TETQRRLEDEEKAAKILKAEEQKKMADLQAELD----KQKKLAEAHAKAIAKAEKEAD--ELKHQMKQEVSKREVAALDA 2532
Cdd:pfam05557 44 DRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEALNKKLNEKESQLADarEVISCLKNELSELRRQIQRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2533 ENQKKNIELELHELK---KLSEQQINDKSQLVDDaLQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAA---EA 2606
Cdd:pfam05557 124 ELELQSTNSELEELQerlDLLKAKASEAEQLRQN-LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAripEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2607 ERLRKLAQEEAEKLHKqVIEETQKKRTAEEELKRKSEAEkEAAKQKQKALEdLENLKMQAEEAERKvkqaQIEKEKQIQI 2686
Cdd:pfam05557 203 EKELERLREHNKHLNE-NIENKLLLKEEVEDLKRKLERE-EKYREEAATLE-LEKEKLEQELQSWV----KLAQDTGLNL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2687 AHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLR 2766
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKER 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2767 --LQAEEEAHKKSLAQEEAEKQKEEAEREAKKRakAEESALKQKEMaEKELERQRKVADSTAQQKLTAEQELIRLRAEFD 2844
Cdd:pfam05557 356 dgYRAILESYDKELTMSNYSPQLLERIEEAEDM--TQKMQAHNEEM-EAQLSVAEEELGGYKQQAQTLERELQALRQQES 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2845 NAEQQRSLLEDELYRLKNEVIAAQQQRkqLEDELAKMRSEMEiliqlksRAEKETMSNTEKSKML-------LDAEASKm 2917
Cdd:pfam05557 433 LADPSYSKEEVDSLRRKLETLELERQR--LREQKNELEMELE-------RRCLQGDYDPKKTKVLhlsmnpaAEAYQQR- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2918 rdvAEEAGKLRaiaeeakyqrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQ 2997
Cdd:pfam05557 503 ---KNQLEKLQ------------AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
....*
gi 1838104091 2998 RKALE 3002
Cdd:pfam05557 568 AKIQE 572
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3270-3720 |
2.01e-12 |
|
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: 74.29 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3270 EQKKKADAEMAKHKKLAEQTLKQKFQV-------EQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEEL 3342
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFlteikkkEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3343 FKVKVQmeeLLKVKLKIEKENQLL------------IKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAE 3410
Cdd:TIGR04523 197 LKLELL---LSNLKKKIQKNKSLEsqiselkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3411 EDLVQQRALAEKMLKEKMQAIQEASRLKAEA----------ELLQRQKDLAQEQAQ-------------------RLLED 3461
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnkelksELKNQEKKLEEIQNQisqnnkiisqlneqisqlkKELTN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3462 KELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNiaarlLETEIATKDKSt 3541
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-----LQQEKELLEKE- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3542 vMQQLEVERRNNSKEADDLRNAIANLETE------------------KARLKKDAEELQNKSKEMAD--AQMKQIEHEKT 3601
Cdd:TIGR04523 428 -IERLKETIIKNNSEIKDLTNQDSVKELIiknldntresletqlkvlSRSINKIKQNLEQKQKELKSkeKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3602 MLQQTFLT---EKEMLLKKERLIEDEKKRLESQYEEeaKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREM 3678
Cdd:TIGR04523 507 ELEEKVKDltkKISSLKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1838104091 3679 LNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2708-3094 |
2.78e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2708 EKTSKLEEsLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANealRLRLQAEEEAHKKSLAQEEAEKqk 2787
Cdd:COG4717 75 ELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERL-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2788 eeaeREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQK-LTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIA 2866
Cdd:COG4717 149 ----EELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2867 AQQQRKQLEDELA------KMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMR----------------DVAEEA 2924
Cdd:COG4717 225 LEEELEQLENELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllarekaSLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2925 GKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKT--------EAEIALKEKEAENERLRRAA----E 2992
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEllreaeelEEELQLEELEQEIAALLAEAgvedE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2993 DEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQR-RVVEEEIRILKLNFEKASSGKLDLELELNK 3071
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420
....*....|....*....|...
gi 1838104091 3072 LkniAEETQQSKLRAEEEAEKQR 3094
Cdd:COG4717 465 L---EEDGELAELLQELEELKAE 484
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3306-3756 |
2.89e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3306 KLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVE----------EELFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQ 3375
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADevleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3376 QLLAEEAENMKRLAKeaAILSVESQEASRLRQiaeEDLVQQRALAEKMLKEKMQAIQEAsrlKAEAELLQRQKDLAQEQA 3455
Cdd:PRK02224 287 RLEELEEERDDLLAE--AGLDDADAEAVEARR---EELEDRDEELRDRLEECRVAAQAH---NEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3456 QRLLEDKElmqkRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIA 3535
Cdd:PRK02224 359 EELREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3536 TKDKSTVM---QQL-----------EVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAqmKQIEHEKT 3601
Cdd:PRK02224 435 LRTARERVeeaEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3602 MLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLH--ATMDEALSKQKEaEREML 3679
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREevAELNSKLAELKE-RIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3680 NKQKEM--------QELEKKRlEQEKVLAEENKKLRDQLQQLEEAQKEKNTQViSAATVETTKNvyNGQNAGDVVDSVEN 3751
Cdd:PRK02224 592 ERIRTLlaaiadaeDEIERLR-EKREALAELNDERRERLAEKRERKRELEAEF-DEARIEEARE--DKERAEEYLEQVEE 667
|
....*
gi 1838104091 3752 KPDPL 3756
Cdd:PRK02224 668 KLDEL 672
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4168-4205 |
3.74e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.74e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1838104091 4168 LEAQAGTGYVVDPVNNQKYTVDEAVKAGVVGPELHEKL 4205
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2453-2769 |
3.77e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 73.23 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2453 QYIKFITETQRRLEdEEKAAKILKAEEQKKMADL----QAELDKQKKLAEAHAKAIAKAEKEADelkhQMKQEVSKREVA 2528
Cdd:pfam17380 289 QQEKFEKMEQERLR-QEKEEKAREVERRRKLEEAekarQAEMDRQAAIYAEQERMAMERERELE----RIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2529 ALDAENQKKNIElELHELKKLS--EQQINDKSQlvddalqsrtkieeeihiirIQLETTLNQKSTAETELKQLREKAAEA 2606
Cdd:pfam17380 364 RIRQEEIAMEIS-RMRELERLQmeRQQKNERVR--------------------QELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2607 ERLRKlAQEEAEKLHKQVIEETQKK---RTAEEELKRKSEAEK-----EAAKQKQKALEDLENLKMQAEEAERKVKQAQI 2678
Cdd:pfam17380 423 EQIRA-EQEEARQREVRRLEEERARemeRVRLEEQERQQQVERlrqqeEERKRKKLELEKEKRDRKRAEEQRRKILEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2679 EKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQehgtvlQLQQEAAHLKKQQEDALKAREE------AEKEL 2752
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER------RKQQEMEERRRIQEQMRKATEErsrleaMERER 575
|
330
....*....|....*...
gi 1838104091 2753 DKWRQ-KANEALRLRLQA 2769
Cdd:pfam17380 576 EMMRQiVESEKARAEYEA 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3242-3736 |
4.27e-12 |
|
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: 73.22 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAER---LRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLD 3318
Cdd:pfam05483 216 KLKEDHEKiqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3319 DELQRLKDEVDDAVKQRGQVEEELF-----------KVKVQMEELLKVKLKIE------KENQLLIKKDKDKAQQLLAEE 3381
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNKAKAAHSfvvtefEATTCSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3382 AENMKRLAKEAAILSVESQEASRL---RQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAE----LLQ-RQKDLAQE 3453
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFknnKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQelifLLQaREKEIHDL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3454 QAQrlLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQ-------VSQLSVAQAKAEEEAKRFKKQADNIA 3526
Cdd:pfam05483 456 EIQ--LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEnkeltqeASDMTLELKKHQEDIINCKKQEERML 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3527 AR---LLETEIATKDKSTVMQQLEVERRNNSK-EADDLRNAIANLETEKARLKKDAEELQNKSKEMAdaqmKQIEHEKTM 3602
Cdd:pfam05483 534 KQienLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK----KQIENKNKN 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3603 LQQtfLTEKEMLLKKERLIEDEK--------KRLESQYEEEAKKAKALTDEQERQ---RKLMEE----EKKKLHATMDEA 3667
Cdd:pfam05483 610 IEE--LHQENKALKKKGSAENKQlnayeikvNKLELELASAKQKFEEIIDNYQKEiedKKISEEklleEVEKAKAIADEA 687
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 3668 LSKQKEAEREMLNKQKEMQEL-EKKRLEQEKVLAEENKKL-----RDQLQQLEEAQKEKNTQVISAATVETTKNV 3736
Cdd:pfam05483 688 VKLQKEIDKRCQHKIAEMVALmEKHKHQYDKIIEERDSELglyknKEQEQSSAKAALEIELSNIKAELLSLKKQL 762
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2460-3015 |
8.27e-12 |
|
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: 72.06 E-value: 8.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2460 ETQRRLEDEEKAAKIL---KAEEQKKMADLQAELDKQKKLA---EAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAE 2533
Cdd:pfam05483 230 EYKKEINDKEKQVSLLliqITEKENKMKDLTFLLEESRDKAnqlEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2534 NQKKNIELELHELKKLSEQQINDKSQLVDDALQSRTkieeEIHIIRIQLETTLnqkSTAETELKQLREKAAEAERLRKLA 2613
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA----AHSFVVTEFEATT---CSLEELLRTEQQRLEKNEDQLKII 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2614 QEEAEKLHKQVIEETQKKRTAEEELK--RKSEAEKEAAKQKQKALEDL-ENLK---------MQAEEAERKVKQAQIEKE 2681
Cdd:pfam05483 383 TMELQKKSSELEEMTKFKNNKEVELEelKKILAEDEKLLDEKKQFEKIaEELKgkeqeliflLQAREKEIHDLEIQLTAI 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2682 KQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANE 2761
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2762 ALRLRlqAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA--EKELERQRKVADSTAQQKLTAEQELIRL 2839
Cdd:pfam05483 543 EMNLR--DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKKQIENKNKNIEELHQENKAL 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2840 RAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMrsemeilIQLKSRAEKETMSNTEKSKMLLDAEASKMRD 2919
Cdd:pfam05483 621 KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2920 VaeeagklraiaeEAKYQRQIAEEEA--ARQRAEAERILKEKLAAI-------SEATRLKTEAEIALKEKEAENERLRRA 2990
Cdd:pfam05483 694 I------------DKRCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
570 580
....*....|....*....|....*
gi 1838104091 2991 AEDEAYQRKALEDEANQHKKEIEEK 3015
Cdd:pfam05483 762 LEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
1144-1258 |
9.25e-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: 64.95 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1144 IEDERDrvqKKTFTKWVNkhlikraeS---QHHVTDLYEDLRDGHNLISLLEVL-------SGDTLPREKGRMRFHKLQN 1213
Cdd:cd21298 2 IEETRE---EKTYRNWMN--------SlgvNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIEN 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1838104091 1214 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1258
Cdd:cd21298 71 CNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2647-3195 |
1.18e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2647 EAAKQKQKALEDLENLKMQAEEAERKVKQ-AQIEKEKQiQIAHVAAEKSATAELQSTQRSFVEKTSkleeslkqehgtVL 2725
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRR------------LE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2726 QLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKkslaqeeaekqkeeaerEAKKRAKAEESAL 2805
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE-----------------QLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2806 KQKEMAEKELERQRKVADSTAQqklTAEQELIRLRAEF----DNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAkm 2881
Cdd:COG4913 355 EERERRRARLEALLAALGLPLP---ASAEEFAALRAEAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2882 rsemeiliQLKSRaeketmsnteksKMLLDAEASKMRD-VAEEAGK----LRAIAEEAkyqrQIAEEEAARQRAeAERIL 2956
Cdd:COG4913 430 --------SLERR------------KSNIPARLLALRDaLAEALGLdeaeLPFVGELI----EVRPEEERWRGA-IERVL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2957 ----------KEKLAAISEAT-RLKTEAEI-ALKEKEAENERLRRAAEDEAYQRKaLEDEANQHKKEIEEKIVQ----LK 3020
Cdd:COG4913 485 ggfaltllvpPEHYAAALRWVnRLHLRGRLvYERVRTGLPDPERPRLDPDSLAGK-LDFKPHPFRAWLEAELGRrfdyVC 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3021 KSSQAEMQR-QKAMVDDTL---------KQRRVVEEEIRILKLNFEKassgKLD-LELELNKLKNIAEETQQSKLRAEEE 3089
Cdd:COG4913 564 VDSPEELRRhPRAITRAGQvkgngtrheKDDRRRIRSRYVLGFDNRA----KLAaLEAELAELEEELAEAEERLEALEAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3090 AEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQ-----DELDRLKKKAEEARKQKDKADSEAEKQIVAASQAA 3164
Cdd:COG4913 640 LDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
570 580 590
....*....|....*....|....*....|.
gi 1838104091 3165 LKCRTAEQQVQSVLAQQKEDSMMHKKLQQEY 3195
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3242-3752 |
1.56e-11 |
|
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: 71.29 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQK---DLLD 3318
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcNLLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3319 DELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKV--KLKIEKENQLL-----IKKDKDKAQQLLAEEAENMKRLAKE 3391
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAfeELRVQAENARLemhfkLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3392 AAILSVESQEasrlrqiaEEDLVQQRALAEKMLKEKMQAIQEASRLKAE--AELLQRQKDLAQE--QAQRLLEDKELMQK 3467
Cdd:pfam05483 242 VSLLLIQITE--------KENKMKDLTFLLEESRDKANQLEEKTKLQDEnlKELIEKKDHLTKEleDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3468 RLDEETEEYQKS---LEAERKRQLEIVAEAEKL-KLQVSQLSVAQAKAEE----EAKRFKKQADNIaaRLLETEIatKDK 3539
Cdd:pfam05483 314 ALEEDLQIATKTicqLTEEKEAQMEELNKAKAAhSFVVTEFEATTCSLEEllrtEQQRLEKNEDQL--KIITMEL--QKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3540 STVMQQLEVERRNNSKEADDLRNAIANLET---EKARLKKDAEELQNKSKEMADA-QMKQIEHEKTMLQQTFLTEKEMLL 3615
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLlQAREKEIHDLEIQLTAIKTSEEHY 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3616 KKErliedeKKRLESQYEEEAKKAKALTDEQErqrKLMEEEKKKLHATMD---------EALSKQKEAEREMLNKQKEMQ 3686
Cdd:pfam05483 470 LKE------VEDLKTELEKEKLKNIELTAHCD---KLLLENKELTQEASDmtlelkkhqEDIINCKKQEERMLKQIENLE 540
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3687 ELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVETTKNVYNGQNAGDVVDSVENK 3752
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3245-3515 |
1.61e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 71.31 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3245 EDAERLRK-EAEFEAAKRAQAENAALEQKKKAD-AEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDllddelQ 3322
Cdd:pfam17380 319 EEAEKARQaEMDRQAAIYAEQERMAMERERELErIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN------E 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3323 RLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQllikkdkDKAQQLLAEEAENMKRLAKEAAilsVESQEA 3402
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ-------REVRRLEEERAREMERVRLEEQ---ERQQQV 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3403 SRLRQIAEEDlvQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEA 3482
Cdd:pfam17380 463 ERLRQQEEER--KRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
250 260 270
....*....|....*....|....*....|...
gi 1838104091 3483 ERKRQLEIvaeAEKLKLQVSQLSVAQAKAEEEA 3515
Cdd:pfam17380 541 ERRKQQEM---EERRRIQEQMRKATEERSRLEA 570
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2474-3021 |
1.68e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2474 ILKAEEQKKMadlqaeLDKQKKLAEAHAKAIAKAEkEADELKHQMKQEVSKREVAALDAEnqkknIELELHELKKLsEQQ 2553
Cdd:COG4913 244 LEDAREQIEL------LEPIRELAERYAAARERLA-ELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARL-EAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2554 INDKSQLVDDALQSRTkieeeihiiriQLETTLNQ-----KSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEEt 2628
Cdd:COG4913 311 LERLEARLDALREELD-----------ELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2629 qkkrtaEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIqiahvaaeksatAELQSTQRSFve 2708
Cdd:COG4913 379 ------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI------------ASLERRKSNI-- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2709 ktskleeslkqeHGTVLQLQQE-AAHLKKQQEDA--------LKAREE-----AEKEL----------DKWRQKANEA-- 2762
Cdd:COG4913 439 ------------PARLLALRDAlAEALGLDEAELpfvgelieVRPEEErwrgaIERVLggfaltllvpPEHYAAALRWvn 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2763 ---LRLRLQAEEEahkkslaqeeaekqkeEAEREAKKRAKAEESALKQK---------EMAEKELERQRKVA--DSTAQQ 2828
Cdd:COG4913 507 rlhLRGRLVYERV----------------RTGLPDPERPRLDPDSLAGKldfkphpfrAWLEAELGRRFDYVcvDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2829 K-----LTAE------------QELIRLRAE----FDNAEQqRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEI 2887
Cdd:COG4913 571 RrhpraITRAgqvkgngtrhekDDRRRIRSRyvlgFDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2888 LIQLKSRAEKE--------TMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAAR---QRAEAERIL 2956
Cdd:COG4913 650 LQRLAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEEL 729
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 2957 KEKLAAISEATRLKTEAEIALKEkeaenERLRRAAEDEAY---------QRKALEDEANQHKKEIEEKIVQLKK 3021
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLE-----ERFAAALGDAVErelrenleeRIDALRARLNRAEEELERAMRAFNR 798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3284-3516 |
2.46e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3284 KLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELfkvKVQMEELLKVKLKIEKEN 3363
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3364 QLLIKKDKDKAQQLLAeeAENMKRLAKEAAILSVES-QEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAE 3442
Cdd:COG4942 97 AELEAQKEELAELLRA--LYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 3443 LLQRQKDLAQEQAQRLLEDKELMQKRLdeetEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAK 3516
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLL----ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3314-3720 |
2.54e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3314 KDLLDDE---LQRLKDEVDdavkqrGQVEEELFKVKVQME-ELLKVKLKIEK--ENQLLIKKDKDKAQQLLAEEAENMKR 3387
Cdd:PRK02224 179 ERVLSDQrgsLDQLKAQIE------EKEEKDLHERLNGLEsELAELDEEIERyeEQREQARETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3388 LAK-EAAILSVES--QEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDlaqeqaqrlledkel 3464
Cdd:PRK02224 253 LETlEAEIEDLREtiAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE--------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3465 mqkRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLsvaqakaEEEAKRFKKQADNIAARLLETEIATKDKSTVMQ 3544
Cdd:PRK02224 318 ---ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3545 QLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEmadaqmkqiehektmLQQTFLTEKEMLLKKERLIEDE 3624
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE---------------LEATLRTARERVEEAEALLEAG 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3625 KKRLESQYEEEAKKAKALTDEQERQRKLmEEEKKKLHATMD------EALSKQKEAEREMLNKQKEMQELEKKRLEQEKV 3698
Cdd:PRK02224 453 KCPECGQPVEGSPHVETIEEDRERVEEL-EAELEDLEEEVEeveerlERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
410 420
....*....|....*....|....*
gi 1838104091 3699 LAEENKK---LRDQLQQLEEAQKEK 3720
Cdd:PRK02224 532 IEEKRERaeeLRERAAELEAEAEEK 556
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2591-2835 |
2.58e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 69.45 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2591 TAETELKQLREKAAEAERlrklAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDlenlkmQAEEAE 2670
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKR----AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEE------AAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2671 RKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEhgtvlqlQQEAAHLKKQQEDALKAREEAEK 2750
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAEAEAAAKAAAEAKK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2751 eldkwrqkanealrlrlQAEEEAHKKSlaqeeaekqkeeaEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKL 2830
Cdd:PRK09510 202 -----------------KAEAEAKKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAA 251
|
....*
gi 1838104091 2831 TAEQE 2835
Cdd:PRK09510 252 AAKAA 256
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
1147-1249 |
2.59e-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: 63.98 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1147 ERDRvQKKTFTKWVNKHLIKRAesqhhVTDLYEDLRDGHNLISLLEVLSGDT--------LPREKGRMRFHKLQNVQIAL 1218
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA-----VNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAV 77
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1219 DFLRHRQVKLVNIRNDDIADGNPKLTLGLIW 1249
Cdd:cd21300 78 ELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5069-5107 |
3.12e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.80 E-value: 3.12e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 5069 LLEAQAATGYVIDPIKNLKLTVLEAVRMGIVGPEFKDKL 5107
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2634-3733 |
3.21e-11 |
|
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: 70.46 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2634 AEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKV--KQAQIEKEKQIqiahVAAEKSATAELQSTQRSFVE--- 2708
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQItsKEAQLESSREI----VKSYENELDPLKNRLKEIEHnls 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2709 KTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQ---KANEALRLRLQAEEEAHKKslaqeeaek 2785
Cdd:TIGR00606 263 KIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQrtvREKERELVDCQRELEKLNK--------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2786 qkeeaEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVI 2865
Cdd:TIGR00606 334 -----ERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2866 AAQQQRKQLEDELAKMRSEMEiliqlKSRAEKETMSNT-EKSKMLLDAEASKMRDVAEEAGKLRAIAEEakyqrqIAEEE 2944
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQAD-----EIRDEKKGLGRTiELKKEILEKKQEELKFVIKELQQLEGSSDR------ILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2945 AARQRAEAERILKEKlaaiSEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRkaledeaNQHKKEIEEKIVQLKKSSQ 3024
Cdd:TIGR00606 478 QELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL-------NHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3025 AEMQ--RQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKL-KNIAE-ETQQSKLRAEEEAEKQRKLAMEE 3100
Cdd:TIGR00606 547 KDEQirKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLnKELASlEQNKNHINNELESKEEQLSSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3101 EkrrreaeetVKKITAAEKEagrqrkiaQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQ 3180
Cdd:TIGR00606 627 K---------LFDVCGSQDE--------ESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3181 QKEDSMMHKKLQQEYEKAKKLAKEAEAakekaekeavLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAK 3260
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTES----------ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3261 RAQAENAALEQKKKADAEMAKHKK----LAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDavkqrg 3336
Cdd:TIGR00606 760 IQRLKNDIEEQETLLGTIMPEEESakvcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQE------ 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3337 qveeelfkvkvQMEELLKVKLKIEkENQLLIKkDKDKAQQLLAEEAENMKrlakeaailsvesqeaSRLRQIAEEdlVQQ 3416
Cdd:TIGR00606 834 -----------KQHELDTVVSKIE-LNRKLIQ-DQQEQIQHLKSKTNELK----------------SEKLQIGTN--LQR 882
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3417 RALAEKMLKEKMQAIQEASRLKAEAellqRQKDLAQEQAqrlledkelMQKRLDEETEEYQKSLEAERKRQLEIVAEAEK 3496
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLIREIKDA----KEQDSPLETF---------LEKDQQEKEELISSKETSNKKAQDKVNDIKEK 949
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3497 LKLQVSQLSVAQAKAEEEAKRFKKQAdniaarllETEIATkdkstVMQQLEVERRNNSKEADDLRNAIANLETEKARLK- 3575
Cdd:TIGR00606 950 VKNIHGYMKDIENKIQDGKDDYLKQK--------ETELNT-----VNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERw 1016
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3576 -KDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKrlesqyeeeaKKAKALTDEQERQRKLME 3654
Cdd:TIGR00606 1017 lQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKR----------NHVLALGRQKGYEKEIKH 1086
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3655 EEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKR--LEQEKV------LAEENKKLRDQLQQLEEAQKEKNTQVIS 3726
Cdd:TIGR00606 1087 FKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYktLDQAIMkfhsmkMEEINKIIRDLWRSTYRGQDIEYIEIRS 1166
|
....*..
gi 1838104091 3727 AATVETT 3733
Cdd:TIGR00606 1167 DADENVS 1173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3431-3728 |
3.67e-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: 70.47 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3431 IQEA---SRLKAEAELLQRQKDLAQEQAQRLlEDkelmqkrLDEETEEYQKSLEAERK---RQLEIVAEAEKLKLQVSQL 3504
Cdd:TIGR02168 161 FEEAagiSKYKERRKETERKLERTRENLDRL-ED-------ILNELERQLKSLERQAEkaeRYKELKAELRELELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3505 SVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKStvMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDaeelqnk 3584
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEK--LEELRLEVSELEEEIEELQKELYALANEISRLEQQ------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3585 sKEMADAQMKQIEHEKTMLQqtfltekemllkkERLIEDEKKRLESQYEeeakkAKALTDEQERQRKLMEEEKKKLhatm 3664
Cdd:TIGR02168 304 -KQILRERLANLERQLEELE-------------AQLEELESKLDELAEE-----LAELEEKLEELKEELESLEAEL---- 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 3665 DEALSKQKEAEREMLNKQKEMQELEKKR---LEQEKVLAEENKKLRDQLQQLEEaQKEKNTQVISAA 3728
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVaqlELQIASLNNEIERLEARLERLED-RRERLQQEIEEL 426
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1272-1367 |
4.28e-11 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 62.79 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1272 KEKLLCWSQRMtdgYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQ-ENLEQAFNVAERDLGVTRLLDPE 1350
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCPNWRKLDPSNSlENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1838104091 1351 DVDVPHPDEKSIITYVS 1367
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1153-1252 |
5.11e-11 |
|
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: 62.98 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1153 KKTFTKWVNKHLIKRAESQHHVT------DLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHKLQNVQIALDFL 1221
Cdd:cd21217 3 KEAFVEHINSLLADDPDLKHLLPidpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1838104091 1222 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1252
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3261-3706 |
5.20e-11 |
|
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: 69.75 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3261 RAQAENAALEQ--KKKADAEMAKH------------KKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKD 3326
Cdd:pfam05483 203 RVQAENARLEMhfKLKEDHEKIQHleeeykkeindkEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3327 EVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKdkdkAQQLLAEEAENMKRLAKEAAILSVESQEASRLR 3406
Cdd:pfam05483 283 NLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT----ICQLTEEKEAQMEELNKAKAAHSFVVTEFEATT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3407 QIAEEDLVQQRALAEK---MLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKElmqkRLDEETEEYQKSLEAE 3483
Cdd:pfam05483 359 CSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE----KLLDEKKQFEKIAEEL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3484 RKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLrna 3563
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM--- 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3564 ianleteKARLKKDAEELQNKSKEmADAQMKQIEHektmlqqtfLTEKEMLLKkerlieDEKKRLESQYEEEAKKAKALT 3643
Cdd:pfam05483 512 -------TLELKKHQEDIINCKKQ-EERMLKQIEN---------LEEKEMNLR------DELESVREEFIQKGDEVKCKL 568
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3644 DEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKL 3706
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2458-3019 |
6.46e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2458 ITETQRRLEDEEKAAKILK--AEEQKKMADLQAELDKQKKLAEA-----HAKAIAKAEKEADELKHQMKQEVSKREvaal 2530
Cdd:COG4913 237 LERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELE---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2531 DAENQKKNIELELHELKKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQ-KSTAETELKQLREKAAEAERL 2609
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2610 RKLAQEEAEKLHKQVIEETQKKRTAEEELKRKsEAEKEAAKQKQKAL-------------------EDL----ENLKMQA 2666
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELREL-EAEIASLERRKSNIparllalrdalaealgldeAELpfvgELIEVRP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2667 EEA--------------------ERKVKQA-----QIEKEKQIQIAHVAAEKSATAELQSTQRSFVEK----TSKLEESL 2717
Cdd:COG4913 472 EEErwrgaiervlggfaltllvpPEHYAAAlrwvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2718 KQEhgtvlqLQQEAAHLKKQQEDALKAREEA--------------EKELDKWRQKAN----------EALRLRLQAEEEA 2773
Cdd:COG4913 552 EAE------LGRRFDYVCVDSPEELRRHPRAitragqvkgngtrhEKDDRRRIRSRYvlgfdnraklAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2774 HKKSlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEKELERQR---KVADSTAQQKLTAEQELIRLRAEFDNAEQqr 2850
Cdd:COG4913 626 LAEA--------------EERLEALEAELDALQERREALQRLAEYSwdeIDVASAEREIAELEAELERLDASSDDLAA-- 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2851 slLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAI 2930
Cdd:COG4913 690 --LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2931 AEEAKYQRQIAEEEAARQRAEAERILKE--------------KLAAISE-ATRLKTEAEIALKEKEAENERLRRAAEDEa 2995
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIE- 846
|
650 660
....*....|....*....|....
gi 1838104091 2996 yQRKALEDEANQHKKEIEEKIVQL 3019
Cdd:COG4913 847 -FVADLLSKLRRAIREIKERIDPL 869
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2348-3098 |
7.16e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2348 KERQEKIQAVSITDSKT-LKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQLVAYNAKADPHASPLKKNKM 2426
Cdd:TIGR02169 207 REKAERYQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2427 DsasdniiqEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAE-----------------EQKKMADLQAE 2489
Cdd:TIGR02169 287 E--------EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkllaeieelereieeERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2490 LDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKNIELELHELKKLSEQQINDKSQLVD-----DA 2564
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGieakiNE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2565 LQSRTKIEEEIHIIRIQ-LETTLNQKSTAETELKQLREKAAEAE-RLRKLAQEEAEKL-HKQVIEETQKKRTAEEELKRK 2641
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWkLEQLAADLSKYEQELYDLKEEYDRVEkELSKLQRELAEAEaQARASEERVRGGRAVEEVLKA 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2642 S--------------EAEKEAA--------------KQKQKALEDLENLK-MQAEEAE----RKVKQAQ----------- 2677
Cdd:TIGR02169 519 SiqgvhgtvaqlgsvGERYATAievaagnrlnnvvvEDDAVAKEAIELLKrRKAGRATflplNKMRDERrdlsilsedgv 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2678 -------IEKEKQIQIA-------HVAAEKSATAELQSTQRSFV-----------------EKTSKLEESLKQEHGTVLQ 2726
Cdd:TIGR02169 599 igfavdlVEFDPKYEPAfkyvfgdTLVVEDIEAARRLMGKYRMVtlegelfeksgamtggsRAPRGGILFSRSEPAELQR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2727 LQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRL--RLQAEEEAhkksLAQEEAEKQKEEAEREAKKRAKAEESA 2804
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigEIEKEIEQ----LEQEEEKLKERLEELEEDLSSLEQEIE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2805 LKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSE 2884
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2885 MEIL--------IQLKSRAEKETMSNTEKSKMLldaeaskmrdvaeeagklraiAEEAKYQRQIAEEEAARQRAEAERil 2956
Cdd:TIGR02169 835 IQELqeqridlkEQIKSIEKEIENLNGKKEELE---------------------EELEELEAALRDLESRLGDLKKER-- 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2957 keklaaiSEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEAnqhkKEIEEKIVQLKKSSQAEMQrqkamVDD 3036
Cdd:TIGR02169 892 -------DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----SEIEDPKGEDEEIPEEELS-----LED 955
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3037 TLKQRRVVEEEIRILK-LN------FEKASSGKLDLELELNKLKniaEETQQSKLRAEEEAEKQRKLAM 3098
Cdd:TIGR02169 956 VQAELQRVEEEIRALEpVNmlaiqeYEEVLKRLDELKEKRAKLE---EERKAILERIEEYEKKKREVFM 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2422-2754 |
8.16e-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: 69.32 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2422 KKNKMDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQK---KMADLQAELDKQKKLAE 2498
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2499 AHAKAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKNI---ELELHELK----------KLSEQQINDKSQLVDDAL 2565
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLLNeeaanlrerlESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2566 QSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAE 2645
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2646 KEAAKQKQKALEDLENLKMQAEEaerkvkQAQIEKEkqIQIAHVAAEKSATAELQstqrsfvEKTSKLEESLKqEHGTV- 2724
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSE------EYSLTLE--EAEALENKIEDDEEEAR-------RRLKRLENKIK-ELGPVn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1838104091 2725 -------LQLQQEAAHLKKQQEDALKAR---EEAEKELDK 2754
Cdd:TIGR02168 989 laaieeyEELKERYDFLTAQKEDLTEAKetlEEAIEEIDR 1028
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4243-4281 |
1.18e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 1.18e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 4243 LLDAQMTTGGIIDPVKSHHIPHDVACKRNYFDDEMKQIL 4281
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2595-3006 |
1.20e-10 |
|
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: 68.12 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAaEAERLRKlAQEEAEKLHKQVIEETQKKRTAEEELKRK-SEAEKEAAKQKQkalEDLEN--------LKMQ 2665
Cdd:NF033838 103 ELNVLKEKS-EAELTSK-TKKELDAAFEQFKKDTLEPGKKVAEATKKvEEAEKKAKDQKE---EDRRNyptntyktLELE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2666 AEEAERKVKQAQIEKEKQiqiahvaaeksataelqstqrsfVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAR 2745
Cdd:NF033838 178 IAESDVEVKKAELELVKE-----------------------EAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2746 EEAEKELDKWRQKANEalRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKkrAKAEESALKQKEMAEKELERQRKVADst 2825
Cdd:NF033838 235 EEAKRRADAKLKEAVE--KNVATSEQDKPKRRAKRGVLGEPATPDKKEND--AKSSDSSVGEETLPSPSLKPEKKVAE-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2826 AQQKLTAEQElirlRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKmrsemeiliqlksrAEKETMSNTEK 2905
Cdd:NF033838 309 AEKKVEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVK--------------EEAKEPRNEEK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2906 SKMLLDAEASKMrdvaEEAGKLraiaEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENE 2985
Cdd:NF033838 371 IKQAKAKVESKK----AEATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQP 442
|
410 420
....*....|....*....|....
gi 1838104091 2986 RLRRAAEDEA---YQRKAlEDEAN 3006
Cdd:NF033838 443 KAEKPADQQAeedYARRS-EEEYN 465
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3596-3808 |
1.41e-10 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 68.31 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3596 IEHEKTMLQqtflTEKEMLlkkERLIED-EKKRLEsqYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQ--- 3671
Cdd:PRK00409 504 IEEAKKLIG----EDKEKL---NELIASlEELERE--LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAeke 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3672 -----KEAEREMLNKQKEMQELEKKRLEQ--EKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVETTKNVYNGQNaGD 3744
Cdd:PRK00409 575 aqqaiKEAKKEADEIIKELRQLQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQK-GE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 3745 VVDSVENKPDPLSFDGIRDKVPASRLRdvglLSKKEFDKLKKGKATVQQLGETEKLKLILKGKD 3808
Cdd:PRK00409 654 VLSIPDDKEAIVQAGIMKMKVPLSDLE----KIQKPKKKKKKKPKTVKPKPRTVSLELDLRGMR 713
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3256-3499 |
1.51e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3256 FEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQR 3335
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3336 GQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLlAEEAENMKRLAKE-AAILSVESQEASRLRQIAEEdLV 3414
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPArREQAEELRADLAELAALRAE-LE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3415 QQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEA 3494
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1838104091 3495 EKLKL 3499
Cdd:COG4942 251 LKGKL 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2845-3718 |
2.06e-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: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2845 NAEQQRSLLEDELyRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDA----EASKMR-- 2918
Cdd:COG3096 276 HANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAlrqqEKIERYqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2919 DVAEEAGKLRA---IAEEAKYQRQIAEEEAARQRAEAERiLKEKLA---------------------AISEATRLKTEAE 2974
Cdd:COG3096 355 DLEELTERLEEqeeVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2975 IALKEKEAENERLRRAAED------EAYQRKALEDEA-NQHkkeieEKIVQLKKSSQAEMQRQKAmvDDTLKQrrvVEEE 3047
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQateevlELEQKLSVADAArRQF-----EKAYELVCKIAGEVERSQA--WQTARE---LLRR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3048 IRILKLNFEKASSgkldLELELNKLKNIAEETQQSKLRAEE---EAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQ 3124
Cdd:COG3096 504 YRSQQALAQRLQQ----LRAQLAELEQRLRQQQNAERLLEEfcqRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3125 RKIAQDELDRLKKKAEEARKQkdkadseAEKQIVAasQAALKcRTAEQQVQSVLAQQKEDSMMHKKLQQEyekakklake 3204
Cdd:COG3096 580 RSELRQQLEQLRARIKELAAR-------APAWLAA--QDALE-RLREQSGEALADSQEVTAAMQQLLERE---------- 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3205 aeaAKEKAEKEAVLLRKQAEEAEsqkaaaekEAAIQAKAQEDAERLRKEAE-FEAAKRAQA-ENAALEqkkkaDAemAKH 3282
Cdd:COG3096 640 ---REATVERDELAARKQALESQ--------IERLSQPGGAEDPRLLALAErLGGVLLSEIyDDVTLE-----DA--PYF 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3283 KKL---AEQTLkqkfqVEQELTKVKLKLDDTDkqkDLLDDEL--QRLKDEVDDAVKQrgqVEEELFKVKVQMEEllkVKL 3357
Cdd:COG3096 702 SALygpARHAI-----VVPDLSAVKEQLAGLE---DCPEDLYliEGDPDSFDDSVFD---AEELEDAVVVKLSD---RQW 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3358 KIEK--ENQLLIKKDKDKAQQLLAEEAENmkrLAKEAAILSVESQEASRLRQIAEEDLVQQRALA-----EKMLKEKMQA 3430
Cdd:COG3096 768 RYSRfpEVPLFGRAAREKRLEELRAERDE---LAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQR 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3431 IQEASRLKAEAE----LLQRQKDLAQEQAQ---------RLLEDKELMQkRLDEETEEYQKSLEAERK--------RQLE 3489
Cdd:COG3096 845 RSELERELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETLAD-RLEELREELDAAQEAQAFiqqhgkalAQLE 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3490 -IVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIaarlleTEIatkdkstvmqqleVERRN--NSKEADDLRNAIAN 3566
Cdd:COG3096 924 pLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL------SEV-------------VQRRPhfSYEDAVGLLGENSD 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3567 L-ETEKARLKkDAEELQNKSKEM---ADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKkakal 3642
Cdd:COG3096 985 LnEKLRARLE-QAEEARREAREQlrqAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERAR----- 1058
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3643 tdeqerqrklmeEEKKKLHatmdEALSkQKEAEREMLNKQKEMQELEKKRLEQEkvLAEENKKLRDQLQQLEEAQK 3718
Cdd:COG3096 1059 ------------IRRDELH----EELS-QNRSRRSQLEKQLTRCEAEMDSLQKR--LRKAERDYKQEREQVVQAKA 1115
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2445-3007 |
2.41e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2445 SELMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQKK--MADLQAELDKQKKlaeahakAIAKAEKEADELKHQMKQEV 2522
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERReeLETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2523 SKREVAALDAENQKKNIELELHELKKLSEQQ---INDKSQLVDDALQSRTkieeeihiiriqlettlnQKSTAETELKQL 2599
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARReelEDRDEELRDRLEECRV------------------AAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2600 REKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQie 2679
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR-- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2680 kekqiqiahvAAEKSATAELQSTQRSFVEKTSKLEE-----------------SLKQEHGTVLQLQQEAAHLKKQQE--- 2739
Cdd:PRK02224 426 ----------EREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEeve 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2740 ---DALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLaqeeaekqkeeaeREAKKRAKAEEsalkqkemAEKELE 2816
Cdd:PRK02224 496 erlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE-------------RAEELRERAAE--------LEAEAE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2817 RQRKVADstaqqklTAEQELIRLRAEFDNAEQQRSLLEDELYRLkNEVIAAQQQRKQLEDELAKMRSemeiliQLKSRAE 2896
Cdd:PRK02224 555 EKREAAA-------EAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLRE------KREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2897 KEtmsntEKSKMLLDAEASKMRDVAEEAGKLRaiAEEAKYQRQIAEEEAARqraeaeriLKEKLAAISEAtRLKTEAEIA 2976
Cdd:PRK02224 621 LN-----DERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQ--------VEEKLDELREE-RDDLQAEIG 684
|
570 580 590
....*....|....*....|....*....|....*
gi 1838104091 2977 LKEKEAEN-ERLRRAAEDEAYQRKALE---DEANQ 3007
Cdd:PRK02224 685 AVENELEElEELRERREALENRVEALEalyDEAEE 719
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2868-3194 |
3.15e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.07 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2868 QQQRKQLEDELAKMRSEMEILIQLKSRAEKetMSNTEKSKmlldaEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAAR 2947
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRK--LEEAEKAR-----QAEMDRQAAIYAEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2948 qraEAERILKEKLAAisEATRLKtEAEIALKEKEAENERLRRAAEdEAYQRKALEDEANQHKKEIEEKIVQLKKssQAEM 3027
Cdd:pfam17380 361 ---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRA--EQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3028 QRQKAMvddtlkqRRVVEEEIRilklnfekassgkldlELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREA 3107
Cdd:pfam17380 432 ARQREV-------RRLEEERAR----------------EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3108 EETV-KKITAAEKEAGRQ--------RKIAQDEL-DRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSV 3177
Cdd:pfam17380 489 AEEQrRKILEKELEERKQamieeerkRKLLEKEMeERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
|
330
....*....|....*..
gi 1838104091 3178 LAQQKEDSMMHKKLQQE 3194
Cdd:pfam17380 569 EAMEREREMMRQIVESE 585
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4908-4945 |
3.28e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 3.28e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1838104091 4908 LEAQTATGGIIDPEFQFHLPADIAMQRGYVNKETNERL 4945
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2719-3047 |
4.66e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.30 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2719 QEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRA 2798
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2799 KAEESALKQKEMAeKELERQRKVAdstaQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDel 2878
Cdd:pfam17380 359 KRELERIRQEEIA-MEISRMRELE----RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2879 AKMRsEMEILIQLKSRaekeTMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEaarQRAEAERILKE 2958
Cdd:pfam17380 432 ARQR-EVRRLEEERAR----EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ---RRKILEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2959 KLAAISEATRLKT--EAEIALKEKEAENERLRRAAEDEAYQRKALEDeanqhKKEIEEkivQLKKSSQaEMQRQKAMVDD 3036
Cdd:pfam17380 504 RKQAMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEE-----RRRIQE---QMRKATE-ERSRLEAMERE 574
|
330
....*....|.
gi 1838104091 3037 TLKQRRVVEEE 3047
Cdd:pfam17380 575 REMMRQIVESE 585
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3318-3527 |
5.49e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 65.24 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3318 DDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLiKKDKDKAQQLLAE----EAENMKRLAKEAA 3393
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEaeaeIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3394 ILSVESQEASRLRQIAE----EDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRL 3469
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3470 DEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAA 3527
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2350-3228 |
5.55e-10 |
|
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: 66.61 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2350 RQEKIQAVSITDSKTLKE-QLSQEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQLVAynakadphaspLKKNKMDS 2428
Cdd:TIGR00606 213 KQYKEKACEIRDQITSKEaQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-----------LKSRKKQM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2429 ASDNiiqeyvtlrtryselMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQKKMADLQAELDKQKKlaEAHAKAIAKAE 2508
Cdd:TIGR00606 282 EKDN---------------SELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNK--ERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2509 KEADELKHQMKQEVSKREVAALDAENQKKNIELELHELKK--LSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTl 2586
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERL- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2587 nqKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQA 2666
Cdd:TIGR00606 424 --KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2667 EEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEE--SLKQEHGTVLQLQQEAAHLKKQQEDALKA 2744
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirKIKSRHSDELTSLLGYFPNKKQLEDWLHS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQKANEALRlRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALkqkEMAEKELERQRKVADS 2824
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELA-SLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL---ERLKEEIEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2825 TAQQKLTAEQELIRLRAE-------FDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLK----- 2892
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqs 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2893 --SRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEK----LAAISEA 2966
Cdd:TIGR00606 738 iiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERkiaqQAAKLQG 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2967 TRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEanqhkkeieEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEE 3046
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ---------QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3047 EI-----RILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEA 3121
Cdd:TIGR00606 889 QLvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3122 GRQRKIAQDELDRLKKKAEEARKQKDK---------ADSEAEKQIVAASQAALKCRTAEQQVQSV-------LAQQKEDS 3185
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQLEECEKHQEKinedmrlmrQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkqhLKEMGQMQ 1048
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3186 MM-----HKKLQQEYEKAKKLAKEAEAAKEKAEKEAV-----LLRKQAEEAES 3228
Cdd:TIGR00606 1049 VLqmkqeHQKLEENIDLIKRNHVLALGRQKGYEKEIKhfkkeLREPQFRDAEE 1101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2842-3523 |
5.78e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2842 EFDNAEQQRSLLE--DELYRLKNEVIAAQQQRKQLE------DELAKMRSEMEILIQLKSRAEKETMsntEKSKMLLDAE 2913
Cdd:COG4913 220 EPDTFEAADALVEhfDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFA---QRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2914 ASKMRDVAEEAGKLRAIAEEAK---------YQRQIAE------EEAARQRAEAERILKEKLAAISEATRLKTEAEIALK 2978
Cdd:COG4913 297 LEELRAELARLEAELERLEARLdalreeldeLEAQIRGnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2979 EKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKkssqaemqrqkamvddtlKQRRVVEEEIRILKlnfeka 3058
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR------------------RELRELEAEIASLE------ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3059 sSGKLDLELELNKLKN-IAEETQQSK-----------LRAEEE-----AEK------------QRKLAMeeekrrreaee 3109
Cdd:COG4913 433 -RRKSNIPARLLALRDaLAEALGLDEaelpfvgelieVRPEEErwrgaIERvlggfaltllvpPEHYAA----------- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3110 tVKKITAAEKEAGRQRkiaqdeLDRLKKKAEEARKQKDKADSEAEK-------------QIVAASQAALKCRTAEQ---- 3172
Cdd:COG4913 501 -ALRWVNRLHLRGRLV------YERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleAELGRRFDYVCVDSPEElrrh 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3173 --------QV-QSVLAQQKEDsmmHKKLQQEYekakklakeaeaakekaekeaVL----------LRKQAEEAESQKAAA 3233
Cdd:COG4913 574 praitragQVkGNGTRHEKDD---RRRIRSRY---------------------VLgfdnraklaaLEAELAELEEELAEA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3234 EKEAAIQAKAQEDAERLR------KEAEFEAAKRAQAEN--AALEQKKKA-DAEMAKHKKLAEQ--TLKQKFQ-VEQELT 3301
Cdd:COG4913 630 EERLEALEAELDALQERRealqrlAEYSWDEIDVASAEReiAELEAELERlDASSDDLAALEEQleELEAELEeLEEELD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3302 KVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFkvkvqmEELLKVKLKIEKENQLL--IKKDKDKAQQLLA 3379
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL------EERFAAALGDAVERELRenLEERIDALRARLN 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3380 EEAENMKRLAKEA----------AILSVESQE--ASRLRQIAEEDLVQQRALAEKMLKEkmQAIQEASRLKAEaelLQRQ 3447
Cdd:COG4913 784 RAEEELERAMRAFnrewpaetadLDADLESLPeyLALLDRLEEDGLPEYEERFKELLNE--NSIEFVADLLSK---LRRA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3448 KDLAQEQAQRL---LEDKE---------LMQKRLDEETEEYQKSL-EAERKRQLEIVAEAEKLKLQVSQLsVAQAKAEEE 3514
Cdd:COG4913 859 IREIKERIDPLndsLKRIPfgpgrylrlEARPRPDPEVREFRQELrAVTSGASLFDEELSEARFAALKRL-IERLRSEEE 937
|
....*....
gi 1838104091 3515 AKRFKKQAD 3523
Cdd:COG4913 938 ESDRRWRAR 946
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3244-3632 |
7.09e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3244 QEDAERLRKEAEFEAAKRAQAE-NAALEQKKKADAEMAKHKKLAEQtLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQ 3322
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEElEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3323 RLKDevddAVKQRGQVEEELFKVKVQMEELLKvKLKIEKENQLL--------IKKDKDKAQQLLAEEAENMKRLAKEAAI 3394
Cdd:COG4717 157 ELRE----LEEELEELEAELAELQEELEELLE-QLSLATEEELQdlaeeleeLQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3395 LSVESQEASRLRQIAEEDLVQQRA---------------------------------LAEKMLKEKMQAIQEAsrlkAEA 3441
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllalLFLLLAREKASLGKEA----EEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3442 ELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQ------LSVAQAKAEEE- 3514
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEqeiaalLAEAGVEDEEEl 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3515 ---AKRFKKQADNIAA-RLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMA- 3589
Cdd:COG4717 388 raaLEQAEEYQELKEElEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEe 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1838104091 3590 DAQMKQIEHEKTMLQQTF--LTEKEMLLKK-ERLIEDEKKRLESQY 3632
Cdd:COG4717 468 DGELAELLQELEELKAELreLAEEWAALKLaLELLEEAREEYREER 513
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5417-5454 |
8.89e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 56.72 E-value: 8.89e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1838104091 5417 QRLLEAQACTGGIIDPTTGERLSVTDAEEKGLVDKIMV 5454
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
3276-3744 |
8.99e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.91 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3276 DAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLL-------DDELQRLKDEVDDAVKQRGQVEEELFKVKVQ 3348
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLkgrifpvEDQLEALKSESQNKIELLLQQHQDRIEQLIS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3349 MEELLKVKLKiEKENQLLIKKDKDKAQ-QLLAEEAEN--------MKRLAKEAAILSVESQEASRLRQIAEEDLVQQRAL 3419
Cdd:pfam15921 275 EHEVEITGLT-EKASSARSQANSIQSQlEIIQEQARNqnsmymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3420 AEKMLKE----KMQAIQEASRL-----KAEAELLQRQKDLAQEQAQ-RLLEDKEL--------MQKRLDEETEEYQ---- 3477
Cdd:pfam15921 354 ANSELTEarteRDQFSQESGNLddqlqKLLADLHKREKELSLEKEQnKRLWDRDTgnsitidhLRRELDDRNMEVQrlea 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3478 --KSLEAERKRQLE-----IVAEAEKLKlQVSQLSvaqAKAEEEAKRFKKQADNIAAR---LLETEIATKDKSTVMQQLE 3547
Cdd:pfam15921 434 llKAMKSECQGQMErqmaaIQGKNESLE-KVSSLT---AQLESTKEMLRKVVEELTAKkmtLESSERTVSDLTASLQEKE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3548 VERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKT--MLQQTFLTEKEMLLKKERL---IE 3622
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVieILRQQIENMTQLVGQHGRTagaMQ 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3623 DEKKRLESQYEE---EAKKAKALTDEQERQ-RKL------MEEEKKKLHATMDEALSKQKEAERE---MLNKQKEMQELE 3689
Cdd:pfam15921 590 VEKAQLEKEINDrrlELQEFKILKDKKDAKiRELearvsdLELEKVKLVNAGSERLRAVKDIKQErdqLLNEVKTSRNEL 669
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3690 KKRLEQEKVLaeeNKKLRDQLQQLEEAQKEKNTQVISAAT-VETTKNVYNGQNAGD 3744
Cdd:pfam15921 670 NSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSeLEQTRNTLKSMEGSD 722
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3351-3715 |
9.11e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3351 ELLKVKLKIEKEnQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRAL---------AE 3421
Cdd:PRK04863 283 VHLEEALELRRE-LYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIeryqadleeLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3422 KMLKEKMQAIQEASRLKAEAEllqRQKDLAQEQAQRL---LEDkelMQKRLDE-ETE--EYQKSLEA-ERKRQL------ 3488
Cdd:PRK04863 362 ERLEEQNEVVEEADEQQEENE---ARAEAAEEEVDELksqLAD---YQQALDVqQTRaiQYQQAVQAlERAKQLcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3489 ----------EIVAEAEKLKLQV----SQLSVAQAKAEEEAKRFKkqadniAARLLETEIATKDKSTVMQQLEVERRNNS 3554
Cdd:PRK04863 436 tadnaedwleEFQAKEQEATEELlsleQKLSVAQAAHSQFEQAYQ------LVRKIAGEVSRSEAWDVARELLRRLREQR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3555 KEADDLrnaiANLETEKARLKKDAEELQNKSKEMADAQMKQIehektmlqQTFLTEKEMllkkERLIEDEKKRLESqYEE 3634
Cdd:PRK04863 510 HLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLG--------KNLDDEDEL----EQLQEELEARLES-LSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3635 EAKKAKALTDEQERQRKLMEEEKKKLHA------TMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRD 3708
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAA 652
|
....*..
gi 1838104091 3709 QLQQLEE 3715
Cdd:PRK04863 653 RKQALDE 659
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1635-1824 |
9.82e-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: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1635 LHYLKDLLIWVEENQIRINESEWGSDLPSVESQLGSHRGLHQTIEDFRAKIERARADESQI---SPVSKGAYRDYMGKLD 1711
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1712 LHYGKLLNSSKSRLRNLD---SLHAFISASTKELMWLNDKEEEEVNFDWSDKNPNMTAKKDNYSGLMRELELREKKVNDL 1788
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838104091 1789 QAMGERLVRDGHPGK-KTVEDFTAALQTQWSWILQLC 1824
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2640-3087 |
1.03e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2640 RKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQ 2719
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2720 EHGTVLQLQQEAAHLKKQQEDalkaREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAK 2799
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2800 AEESALKQKemaEKELERQRKVADstAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAA----------QQ 2869
Cdd:COG4717 220 EELEELEEE---LEQLENELEAAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallfllLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2870 QRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQR 2949
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2950 ------AEAERILKEKLAAISEATRLK---TEAEIALKEKEAENERLRRAAEDEAYQRKAleDEANQHKKEIEEKIVQLK 3020
Cdd:COG4717 375 llaeagVEDEEELRAALEQAEEYQELKeelEELEEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELR 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3021 KSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLN--FEKASSGKLDLELeLNKLKNIAEETQQSKLRAE 3087
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELLQELEELKAELRelAEEWAALKLALEL-LEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3507-3728 |
1.14e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3507 AQAKAEEEAKRFKKQADNIAARLLETEiatKDKSTVMQQLEV----------ERRNNSKEADDLRNAIANLETEKARLKK 3576
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALK---KEEKALLKQLAAlerriaalarRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3577 DAEELQNKSKEMADAQMKQIEHEKTML---QQTFLTEKEMLLKKERLIEDEKKRLESQyeeeakkaKALTDEQERQRKLM 3653
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEEL--------RADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3654 EEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAE---ENKKLRDQLQQLEEAQKEKNTQVISAA 3728
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2808-3542 |
1.25e-09 |
|
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: 65.16 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2808 KEMAEKELERQRKVADSTAQQKLTAEQELIR----LRAEFDNAEQQRSlledelyrlknEVIAAQ-QQRKQLEDELAKMR 2882
Cdd:pfam07111 18 QDVLERRLDTQRPTVTMWEQDVSGDGQGPGRrgrsLELEGSQALSQQA-----------ELISRQlQELRRLEEEVRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2883 semEILIQLKSRAEKETMSntekskmlLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAA 2962
Cdd:pfam07111 87 ---ETSLQQKMRLEAQAME--------LDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2963 ISEAtrlkteAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKsSQAEMQRQKAMVDDTlkqRR 3042
Cdd:pfam07111 156 LTQA------HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSK-TQEELEAQVTLVESL---RK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3043 VVEEEIrilkLNFEKASSGKLDLELELNKLKNIAEEtqQSKLRAEEEAEKQRKLAMEEEKRRREAEETvKKITAAEKEAG 3122
Cdd:pfam07111 226 YVGEQV----PPEVHSQTWELERQELLDTMQHLQED--RADLQATVELLQVRVQSLTHMLALQEEELT-RKIQPSDSLEP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3123 RQRKIAQDELDRLKKKAEEARKQKDKADSEAEKqivaaSQAALKCRTAEQQVQsVLAQQKEDSMMHKKLQQEYEKAKKLA 3202
Cdd:pfam07111 299 EFPKKCRSLLNRWREKVFALMVQLKAQDLEHRD-----SVKQLRGQVAELQEQ-VTSQSQEQAILQRALQDKAAEVEVER 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3203 KEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENA---ALEQKKKADAEM 3279
Cdd:pfam07111 373 MSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRlsyAVRKVHTIKGLM 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3280 AKHKKLAE---QTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQR----LKDEVDDAvKQRGQVEEelfkvkvqmEEL 3352
Cdd:pfam07111 453 ARKVALAQlrqESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsahlIQQEVGRA-REQGEAER---------QQL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3353 LKVKLKIEKENQllikkdkdKAQQLLAEEAENMKrLAKEAAILSVEsqEASRLRQiaeeDLVQQRALAEKMLKEKMQAIQ 3432
Cdd:pfam07111 523 SEVAQQLEQELQ--------RAQESLASVGQQLE-VARQGQQESTE--EAASLRQ----ELTQQQEIYGQALQEKVAEVE 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3433 eaSRLKAEAELLQRQKDLA-QEQAQRLLEDKELMQK--RLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQA 3509
Cdd:pfam07111 588 --TRLREQLSDTKRRLNEArREQAKAVVSLRQIQHRatQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATL 665
|
730 740 750
....*....|....*....|....*....|...
gi 1838104091 3510 KAEEEAKRFKKQadniaaRLLETEIATKDKSTV 3542
Cdd:pfam07111 666 QQEGLLSRYKQQ------RLLAVLPSGLDKKSV 692
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2811-3033 |
1.63e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 63.70 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2811 AEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIq 2890
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2891 lksRAEKETMSNTEKSKMLLDAEaskmrDVAEEAGKLRAIAEEAKYQRQI------AEEEAARQRAEAERILKEKLAAIS 2964
Cdd:COG3883 93 ---RALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 2965 EATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAM 3033
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3379-3720 |
1.73e-09 |
|
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: 64.15 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3379 AEEAENMKRLAKEAAILSVESQEASRLRQiaeEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRL 3458
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3459 LEDKELMQKRLDEET---EEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIA 3535
Cdd:pfam07888 93 REKHEELEEKYKELSassEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3536 TKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKskeMADAQMKQIEHEKTMLQQTFLteKEMLL 3615
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHRKEAENEALLEELRSL--QERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3616 KKERLIEDEKKRLES--------QYE------EEAKKAKALTD------------EQERQ--RKLMEEEKKKLHATMDEA 3667
Cdd:pfam07888 248 ASERKVEGLGEELSSmaaqrdrtQAElhqarlQAAQLTLQLADaslalregrarwAQEREtlQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3668 LSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:pfam07888 328 QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
1272-1370 |
1.97e-09 |
|
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: 58.13 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1272 KEKLLCWSQRMTDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQENLEQAFNVAERDLGVTRLLDPED 1351
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1838104091 1352 VdVPHPDEKSIITYVSSLY 1370
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3244-3634 |
2.15e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3244 QEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQR 3323
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3324 LKDEVDDAVKQRGQVEEELFKVKVQMEEL------LKVKLKIEKENqllikkdKDKAQQLLAE-EAENMKRLAKEAAIls 3396
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELrereaeLEATLRTARER-------VEEAEALLEAgKCPECGQPVEGSPH-- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3397 VESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQE---QAQRLLEDKELMQKRLDEET 3473
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELRERA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3474 EEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARL-LETEIAT-KDKSTVMQQLEVERR 3551
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAdAEDEIERlREKREALAELNDERR 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3552 NNSKE----ADDLRNAIANLETEKARLKKD-AEELQnkskEMADAQMKQIEHEKTMLQQTF------LTEKEMLLKKERL 3620
Cdd:PRK02224 627 ERLAEkrerKRELEAEFDEARIEEAREDKErAEEYL----EQVEEKLDELREERDDLQAEIgaveneLEELEELRERREA 702
|
410
....*....|....
gi 1838104091 3621 IEDEKKRLESQYEE 3634
Cdd:PRK02224 703 LENRVEALEALYDE 716
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2943-3580 |
2.24e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2943 EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKAL--EDEANQHKKEI--EEKIVQ 3018
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNLlkETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3019 LKKSSQAEMQRQKAM-----VDDTLKQRRVVEEEIRIlklnfeKASSGKLDLELelnKLKNIAEETQQSKLRAEEEAEKQ 3093
Cdd:pfam05483 168 AEKTKKYEYEREETRqvymdLNNNIEKMILAFEELRV------QAENARLEMHF---KLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3094 RKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQ 3173
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3174 VQSV------LAQQKEDSMmhkklQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDA 3247
Cdd:pfam05483 319 LQIAtkticqLTEEKEAQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3248 ERL-----RKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTL-----------------------------KQK 3293
Cdd:pfam05483 394 EEMtkfknNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseehylKEV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3294 FQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKvKLKIEKENQLLIKKDKDK 3373
Cdd:pfam05483 474 EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLRDELES 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3374 AQQLLAEEAENMK----RLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKD 3449
Cdd:pfam05483 553 VREEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3450 LAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAK-----------RF 3518
Cdd:pfam05483 633 AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKH 712
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3519 KKQADNIA----ARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEE 3580
Cdd:pfam05483 713 KHQYDKIIeerdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3014-3721 |
2.36e-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: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3014 EKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILK-----------------------LNFEKASSGKLDLELELN 3070
Cdd:pfam12128 182 DKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRqqvehwirdiqaiagimkirpefTKLQQEFNTLESAELRLS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3071 KLK------NIAEETQQsKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAeKEAGRQRKIAQDELDRLKKKAEEARK 3144
Cdd:pfam12128 262 HLHfgyksdETLIASRQ-EERQETSAELNQLLRTLDDQWKEKRDELNGELSAA-DAAVAKDRSELEALEDQHGAFLDADI 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3145 QKDKADSEAEKQI------VAASQAAL--KCRTAEQQVQSVLAQQKED-----SMMHKKLQQEYEKAKklakeaeaakek 3211
Cdd:pfam12128 340 ETAAADQEQLPSWqselenLEERLKALtgKHQDVTAKYNRRRSKIKEQnnrdiAGIKDKLAKIREARD------------ 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3212 aekeavllrKQAEEAESQKAAAEKEAAIQAKAQ----EDAERLRKEAEFEAAKR---AQAENAALEQKKKADAEMAKHKK 3284
Cdd:pfam12128 408 ---------RQLAVAEDDLQALESELREQLEAGklefNEEEYRLKSRLGELKLRlnqATATPELLLQLENFDERIERARE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3285 LAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDdavkqrgQVEEELFKVKVQMEELLKVKLKIEKEN- 3363
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALD-------ELELQLFPQAGTLLHFLRKEAPDWEQSi 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3364 ------QLLIKKDKDKAQQLLAEEAENM-----KRLAKEAAILSVESQEASRLR-QIAEEDLVQQRALAEKMLKEKMQAI 3431
Cdd:pfam12128 552 gkvispELLHRTDLDPEVWDGSVGGELNlygvkLDLKRIDVPEWAASEEELRERlDKAEEALQSAREKQAAAEEQLVQAN 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3432 QEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEaERKRQLEivAEAEKLKLQVSQLSVAQAKA 3511
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQLKQLDKKHQAWLEEQKEQ 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3512 EEEAKRFKKQAdniaarLLETEIATKDK-STVMQQLEVERRNNSKEADDLRNAIANletEKARLKKDAEELQNKSKEMAD 3590
Cdd:pfam12128 709 KREARTEKQAY------WQVVEGALDAQlALLKAAIAARRSGAKAELKALETWYKR---DLASLGVDPDVIAKLKREIRT 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3591 -----AQMKQIEHEKT----MLQQTFLTEKEMLLKKERLIEDEKKRLESQYeeeakkaKALTDEQERQRKLMEEEKK--- 3658
Cdd:pfam12128 780 lerkiERIAVRRQEVLryfdWYQETWLQRRPRLATQLSNIERAISELQQQL-------ARLIADTKLRRAKLEMERKase 852
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3659 KLHATMDEALSKQKeAEREMLNKQKEMQELEKKRLEQEKVLAeENKKLRDQLQQLEEAQKEKN 3721
Cdd:pfam12128 853 KQQVRLSENLRGLR-CEMSKLATLKEDANSEQAQGSIGERLA-QLEDLKLKRDYLSESVKKYV 913
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3380-3715 |
2.96e-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: 62.63 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3380 EEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEasRLKAEAELLQRQKDLAQEQAQRLL 3459
Cdd:pfam13868 6 DELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3460 EDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFK---KQADNIAARLLETEIAT 3536
Cdd:pfam13868 84 EREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKeleKEEEREEDERILEYLKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3537 KDKSTVMQQLEVERRNNSKEA--DDLRNAIANLETEKA-----RLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFlt 3609
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEReiARLRAQQEKAQDEKAerdelRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3610 eKEMLLKKERLIEDEKKRlESQYEEEAKKAKALTDEQERqrklMEEEKKKLhatmdealsKQKEAEREMlnkQKEMQELE 3689
Cdd:pfam13868 242 -EEQIELKERRLAEEAER-EEEEFERMLRKQAEDEEIEQ----EEAEKRRM---------KRLEHRREL---EKQIEERE 303
|
330 340
....*....|....*....|....*.
gi 1838104091 3690 KKRLEQEKVLAEENKKLRDQLQQLEE 3715
Cdd:pfam13868 304 EQRAAEREEELEEGERLREEEAERRE 329
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3009-3719 |
3.15e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3009 KKEIEEKIVQLKK--SSQAEMQRQKAMVDDTLKQrrvVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRA 3086
Cdd:PRK03918 171 IKEIKRRIERLEKfiKRTENIEELIKEKEKELEE---VLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3087 EEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRqrkiaqdeLDRLKKKAEEARKQKDKADseaekqivaasqaalK 3166
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKEKAEEYIKLSEFYE---------------E 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3167 CRTAEQQVQSVLAqqkedsmmhkKLQQEYEKakklakeaeaakekaekeavlLRKQAEEAESQKAAAEKEAAIQAKAQED 3246
Cdd:PRK03918 305 YLDELREIEKRLS----------RLEEEING---------------------IEERIKELEEKEERLEELKKKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3247 AERLRKEAE-FEAAKRAQAENAALEQKKKadaemakhkklaeqtlkqkfqvEQELTKVKLKLDDTDKQKDLLDDELQRLK 3325
Cdd:PRK03918 354 LEELEERHElYEEAKAKKEELERLKKRLT----------------------GLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3326 DEvddavkqRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKDKdkaQQLLAEEAENMKRLAKEAAILsvesqeASRL 3405
Cdd:PRK03918 412 AR-------IGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEI------EEKE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3406 RQIAEEdlvqqralaekmLKEKMQAIQEASRLKAEAELLQRQKDLAQEQaqrlledKELMQKRLDEETEEYQKSLEAERK 3485
Cdd:PRK03918 476 RKLRKE------------LRELEKVLKKESELIKLKELAEQLKELEEKL-------KKYNLEELEKKAEEYEKLKEKLIK 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3486 RQLEIVAEAEKLKlQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDkstvmqqlEVERRNNS-----KEADDL 3560
Cdd:PRK03918 537 LKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE--------ELEERLKElepfyNEYLEL 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3561 RNAIANLETEKARLKKDAEELQNKSKEMADAQmKQIEHEKTMLQQtfltekemllKKERLIEDEKKRLESQYEEEAKKAK 3640
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAFEELAETE-KRLEELRKELEE----------LEKKYSEEEYEELREEYLELSRELA 676
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3641 ALTDEQERQRKLMEEEKKKLHaTMDEALSKQKEAEREMLNKQKEMQELEKKRleqEKVLAEENKKLRDQLQQLEEAQKE 3719
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLE-KLKEELEEREKAKKELEKLEKALERVEELR---EKVKKYKALLKERALSKVGEIASE 751
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3916-3953 |
4.01e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.03 E-value: 4.01e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1838104091 3916 VLEAQLATGGIVDPINSHRVPNQTAYTQGQYDDEMNKI 3953
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2652-3380 |
4.40e-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: 63.70 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2652 KQKALEDLENLkMQAEEAERKVKQAQIEKEKQiQIAHVAAEKSATAELQSTQRSFvektskleESLKQEHGTVLQLQQEA 2731
Cdd:pfam12128 191 KEGKFRDVKSM-IVAILEDDGVVPPKSRLNRQ-QVEHWIRDIQAIAGIMKIRPEF--------TKLQQEFNTLESAELRL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2732 AHLKKqqedALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAqeeaekqkeeaerEAKKRAKAEESALKQKEMA 2811
Cdd:pfam12128 261 SHLHF----GYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD-------------ELNGELSAADAAVAKDRSE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2812 EKELERQRKVADSTAQQKLTAEQE-LIRLRAEFDNAEQQRSLLEDElyrlKNEVIAAQQQRK-----QLEDELAKMRSEM 2885
Cdd:pfam12128 324 LEALEDQHGAFLDADIETAAADQEqLPSWQSELENLEERLKALTGK----HQDVTAKYNRRRskikeQNNRDIAGIKDKL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2886 EiliqlKSRAEKETMSNTEKSKmlLDAEASKMRDvAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISE 2965
Cdd:pfam12128 400 A-----KIREARDRQLAVAEDD--LQALESELRE-QLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2966 atrlktEAEIALKEKEAENERLRRAAEDEAyQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRvve 3045
Cdd:pfam12128 472 ------RIERAREEQEAANAEVERLQSELR-QARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR--- 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3046 EEIRILKLNFEKASS----GKLDLELELNKLKNIAEETQQS------KLRAEEEAEKQRKLAMEEEKRRREAEETVKKIT 3115
Cdd:pfam12128 542 KEAPDWEQSIGKVISpellHRTDLDPEVWDGSVGGELNLYGvkldlkRIDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3116 AAEKEAGRQRKiaqdELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKC--------RTAEQQVQSVLAQQKEDSMM 3187
Cdd:pfam12128 622 AAEEQLVQANG----ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnkalaerkDSANERLNSLEAQLKQLDKK 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3188 HKKLQQEYekakklakeaeaakekaekeavllRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKraqAENA 3267
Cdd:pfam12128 698 HQAWLEEQ------------------------KEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELK 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3268 ALEQKKKAD-----------AEMAKHKKLAEQTLKQKFQVEQELT---------------KVKLKLDDTDKQKDLLDDEL 3321
Cdd:pfam12128 751 ALETWYKRDlaslgvdpdviAKLKREIRTLERKIERIAVRRQEVLryfdwyqetwlqrrpRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3322 QRLKDEVDdavKQRGQVEEELFKVKVQM----EELLKVKLKIEKENQLLIKKDKDKAQQLLAE 3380
Cdd:pfam12128 831 ARLIADTK---LRRAKLEMERKASEKQQvrlsENLRGLRCEMSKLATLKEDANSEQAQGSIGE 890
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3283-3722 |
4.72e-09 |
|
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: 63.12 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3283 KKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVK----LK 3358
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3359 IEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLK 3438
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3439 AEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEK---LKLQVSQLSVAQAKAEEEA 3515
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLETQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3516 KRFKKQADNIAARL--LETEIATKDKSTVM-----QQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEM 3588
Cdd:TIGR04523 471 KVLSRSINKIKQNLeqKQKELKSKEKELKKlneekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3589 ---------------ADAQMKQIEHEKTMLQQTfLTEKEMLLKKErliEDEKKRLESQYEEEAKKAKALTDEQErqrkLM 3653
Cdd:TIGR04523 551 dfelkkenlekeideKNKEIEELKQTQKSLKKK-QEEKQELIDQK---EKEKKDLIKEIEEKEKKISSLEKELE----KA 622
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3654 EEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNT 3722
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSL 691
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3331-3594 |
5.45e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3331 AVKQRGQVEEELFKVKVQMEELLKvKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAE 3410
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3411 EDLVQQRALAEKMLKeKMQAIQEASRLKaeaeLLQRQKDLAQeqaqrlledkelMQKRLdeeteEYQKSLEAERKRQlei 3490
Cdd:COG4942 97 AELEAQKEELAELLR-ALYRLGRQPPLA----LLLSPEDFLD------------AVRRL-----QYLKYLAPARREQ--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3491 vaeAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETE 3570
Cdd:COG4942 152 ---AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 1838104091 3571 KARLKKDAEELQNKSKEMADAQMK 3594
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2874-3412 |
5.85e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2874 LEDELAKMRSEMEiliqlksraeKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEE-AKYQRQIAEEEAARQRAEA 2952
Cdd:COG4717 47 LLERLEKEADELF----------KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2953 ERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEdEANQHKKEIEEKIVQLKKSSQAEMQRQka 3032
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATEEE-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3033 mVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKlRAEEEAEKQRKLAMEEEKRRREAEETVK 3112
Cdd:COG4717 194 -LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3113 KITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIvaasqaalkcrtAEQQVQSVLAQQKEDSMMHKKLQ 3192
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL------------EEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3193 QEYEKAKKLAKEAEAAkekaekeavlLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRkeaefEAAKRAQAENAALEQK 3272
Cdd:COG4717 340 LELLDRIEELQELLRE----------AEELEEELQLEELEQEIAALLAEAGVEDEEELR-----AALEQAEEYQELKEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3273 KKADAEMAKHKKLAEQTLKQkfqveqeltkvklklddtdKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 3352
Cdd:COG4717 405 EELEEQLEELLGELEELLEA-------------------LDEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3353 lkvklkiEKENQLlikkdkDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEED 3412
Cdd:COG4717 466 -------EEDGEL------AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2493-2650 |
6.48e-09 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 62.49 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2493 QKKLAEAHAKA---IAKAEKEADELKHQMKQEVsKREVAALDAEnQKKNIELELHELKKLsEQQINDKSQLVDDALQSRT 2569
Cdd:PRK12704 30 EAKIKEAEEEAkriLEEAKKEAEAIKKEALLEA-KEEIHKLRNE-FEKELRERRNELQKL-EKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2570 KIEEEIHIIRIQLETTLNQKSTAETELKQLREKA-AEAERLRKLAQEEA-EKLHKQVIEETQKKRTA---EEELKRKSEA 2644
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERISGLTAEEAkEILLEKVEEEARHEAAVlikEIEEEAKEEA 186
|
....*.
gi 1838104091 2645 EKEAAK 2650
Cdd:PRK12704 187 DKKAKE 192
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
3012-3763 |
9.28e-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: 62.44 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3012 IEEKIVQLKKSSQAEMQRQKAMVDDTLKQRrVVEEEIRILKLNfEKASSGKLdlelELNKLKNIAEETQqsklraeEEAE 3091
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDRIEQL-ISEHEVEITGLT-EKASSARS----QANSIQSQLEIIQ-------EQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3092 KQRKLAMEEEKRRREaeeTVKKITAAEKEAGRQrkiaqdeldrLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAE 3171
Cdd:pfam15921 310 NQNSMYMRQLSDLES---TVSQLRSELREAKRM----------YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3172 QQVQSVLAQqkedsmMHKKlQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKaaaekeaaiqakaqEDAERLR 3251
Cdd:pfam15921 377 DQLQKLLAD------LHKR-EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV--------------QRLEALL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3252 KEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRlkdevdda 3331
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-------- 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3332 vKQRGqveeelfkVKVQMEELLKVKLKIEKENQLLikkdkdkaqQLLAEEAENMKRLAKEAailsvesqEASRLrQIAEE 3411
Cdd:pfam15921 508 -KERA--------IEATNAEITKLRSRVDLKLQEL---------QHLKNEGDHLRNVQTEC--------EALKL-QMAEK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3412 DLVQQraLAEKMLKEKMQAIQEASRLKAEAELlqrqkdlaqEQAQRlleDKELMQKRLDEETEEYQKSLEAERKRQLEiv 3491
Cdd:pfam15921 561 DKVIE--ILRQQIENMTQLVGQHGRTAGAMQV---------EKAQL---EKEINDRRLELQEFKILKDKKDAKIRELE-- 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3492 AEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIaarLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEK 3571
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3572 ARLKKDAEELQN--KSKEMAD---------------AQMKQIEHEKTMLQqtFLTEKEMLLKKER-LIEDEKKRLESQYE 3633
Cdd:pfam15921 702 KSAQSELEQTRNtlKSMEGSDghamkvamgmqkqitAKRGQIDALQSKIQ--FLEEAMTNANKEKhFLKEEKNKLSQELS 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3634 EEAKKAKALTDEQERQRKLMEEEKKKLhATMDEALSKqkeAEREMLNKQK--EMQELEKKRLEQEKVLaeENKKLRDQLQ 3711
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKV-ANMEVALDK---ASLQFAECQDiiQRQEQESVRLKLQHTL--DVKELQGPGY 853
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3712 QLEEAQKEKNTQviSAATVETTKNVYNGQNAGDVVDSVENKPDPLSFDGIRD 3763
Cdd:pfam15921 854 TSNSSMKPRLLQ--PASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRD 903
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4574-4612 |
9.50e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 53.87 E-value: 9.50e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 4574 LIEAQMVSGGIIDPVNSHRVPTDVAYQKNIFSKEIEKTL 4612
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2587-2829 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2587 NQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVieetqkkRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQA 2666
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2667 EEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQStQRSFVEktskLEESLKQEHGTVLQLQQEAAHLKKQQED--ALKA 2744
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLS-PEDFLD----AVRRLQYLKYLAPARREQAEELRADLAElaALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADS 2824
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 1838104091 2825 TAQQK 2829
Cdd:COG4942 248 FAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3413-3730 |
1.43e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3413 LVQQRAlAEKMLKEKMQAIQEASRLKAEAELLQRQkDLAQEQAQRLLEDKELMQKRLDEET--EEYQKSLEAERKRQ--- 3487
Cdd:COG3206 60 LVEPQS-SDVLLSGLSSLSASDSPLETQIEILKSR-PVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGsnv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3488 LEIVAEAEKLKL------------QVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEiatkdkstvmQQLEVERRNN-- 3553
Cdd:COG3206 138 IEISYTSPDPELaaavanalaeayLEQNLELRREEARKALEFLEEQLPELRKELEEAE----------AALEEFRQKNgl 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3554 ---SKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEkemLLKKERLIEDEKKRLES 3630
Cdd:COG3206 208 vdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3631 QYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMD---EALSKQKEAEREMLNKQK----EMQELEKK--RLEQEkvlAE 3701
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaelEALQAREASLQAQLAQLEarlaELPELEAElrRLERE---VE 361
|
330 340 350
....*....|....*....|....*....|....*
gi 1838104091 3702 ENKKLRDQLQQ------LEEAQKEKNTQVISAATV 3730
Cdd:COG3206 362 VARELYESLLQrleearLAEALTVGNVRVIDPAVV 396
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
1144-1255 |
1.63e-08 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 56.06 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1144 IEDERDRVQ--KKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLP----REKGRMRFHKLQNVQIA 1217
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHL---AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLA 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 1838104091 1218 LDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1255
Cdd:cd21222 84 LELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5495-5533 |
1.85e-08 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 53.10 E-value: 1.85e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 5495 FLEVQYLTGGLIEPDVEGRVSLDESLKKGSIDARTAQKL 5533
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3297-3528 |
1.89e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3297 EQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlkvKLKIEKENQLlIKKDKDKAQQ 3376
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAE-IEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3377 LLAEEAENMKRLAKEAAILSVES-----QEASRLRQIAE------EDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQ 3445
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSESfsdflDRLSALSKIADadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3446 RQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNI 3525
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
...
gi 1838104091 3526 AAR 3528
Cdd:COG3883 251 AAG 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2542-3092 |
2.07e-08 |
|
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: 60.91 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2542 ELHELKKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAErlrklaqeeaEKLH 2621
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE----------EALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2622 KQVIEETQKKRTAEEELKRKSEAE--KEAAKQKQKALED-LENLKMQAEEAERKVKQAQIEKEkQIQIAHVAAEKSAT-- 2696
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKEsqLADAREVISCLKNeLSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASea 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2697 ----AELQSTQRSFVEKTSKLEEsLKQEhgtvLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKaNEALRlrlqaeEE 2772
Cdd:pfam05557 152 eqlrQNLEKQQSSLAEAEQRIKE-LEFE----IQSQEQDSEIVKNSKSELARIPELEKELERLREH-NKHLN------EN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2773 AHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKqKEMAEKELERQRKVADSTAQQKLTAEQelirLRAEFDNAEQQRSL 2852
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEKYREEAATLELE-KEKLEQELQSWVKLAQDTGLNLRSPED----LSRRIEQLQQREIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2853 LEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEIL-IQLKSRAE-------------KE---------------TMSNT 2903
Cdd:pfam05557 295 LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLnKKLKRHKAlvrrlqrrvllltKErdgyrailesydkelTMSNY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2904 EKSKMLLDAEASKMRDvaeeagKLRAIAEEAKYQRQIAEEEAARQRAEA---ERILK-----EKLAAISEATRLKTEAEI 2975
Cdd:pfam05557 375 SPQLLERIEEAEDMTQ------KMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQalrqqESLADPSYSKEEVDSLRR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2976 ALKEKEAENERLRRaaedeayQRKALEDEANQHK-----KEIEEKIVQLKKSSQAEMQRQKAMVDDTLkqrrvvEEEIRI 3050
Cdd:pfam05557 449 KLETLELERQRLRE-------QKNELEMELERRClqgdyDPKKTKVLHLSMNPAAEAYQQRKNQLEKL------QAEIER 515
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1838104091 3051 LKLNFEKAsSGKLDLELELNKLKNIAEETQQSKLRAE-EEAEK 3092
Cdd:pfam05557 516 LKRLLKKL-EDDLEQVLRLPETTSTMNFKEVLDLRKElESAEL 557
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2596-3180 |
2.08e-08 |
|
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: 61.28 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2596 LKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKalEDLENLKMQAEEAERKVKq 2675
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLK--EDHEKIQHLEEEYKKEIN- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2676 aqiEKEKQIQI--AHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQED---ALKAREEAEK 2750
Cdd:pfam05483 237 ---DKEKQVSLllIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmSLQRSMSTQK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2751 ELDKWRQKANEALrLRLQAEEEAHKKSLaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEKELERqrkvadsTAQQKL 2830
Cdd:pfam05483 314 ALEEDLQIATKTI-CQLTEEKEAQMEEL-------------NKAKAAHSFVVTEFEATTCSLEELLR-------TEQQRL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2831 TAEQELIRLraeFDNAEQQRSLLEDELYRLKNEviaaqqqrKQLE-DELAKMRSEMEILIQLKSRAEK--ETMSNTEKSK 2907
Cdd:pfam05483 373 EKNEDQLKI---ITMELQKKSSELEEMTKFKNN--------KEVElEELKKILAEDEKLLDEKKQFEKiaEELKGKEQEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2908 M-LLDAEASKMRDVaeeagKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLkteaeialkekeaENER 2986
Cdd:pfam05483 442 IfLLQAREKEIHDL-----EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------ENKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2987 LRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAM--VDDTLKQRR--------VVEEEIRILKLNFE 3056
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYEVL 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3057 KASSGKLDLELELNKLKNIAEETQQSklrAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLK 3136
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKN---IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1838104091 3137 KKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQ 3180
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE 704
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3350-3697 |
2.24e-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: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3350 EELLKVKLKIEKENQLLIKKdkdKAQQLLAEEAENMKRLAKEAAILSVESQEAsRLRQIAEEDLVQQRALAEKMLKEKMQ 3429
Cdd:pfam13868 13 SKLLAAKCNKERDAQIAEKK---RIKAEEKEEERRLDEMMEEERERALEEEEE-KEEERKEERKRYRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3430 AIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQK-SLEAERKRQLEIVAEAEKLKLQVSQLSVAQ 3508
Cdd:pfam13868 89 RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDERILEYLKEKAERE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3509 AKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEM 3588
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3589 ADAQMKQIEHEKTMLQQtfLTEKEMLLKKERLIEDEKKRlesqyeeeaKKAKALTDEQERQRKLMEEEKKklhatmdeal 3668
Cdd:pfam13868 249 ERRLAEEAEREEEEFER--MLRKQAEDEEIEQEEAEKRR---------MKRLEHRRELEKQIEEREEQRA---------- 307
|
330 340
....*....|....*....|....*....
gi 1838104091 3669 sKQKEAEREMLNKQKEMQELEKKRLEQEK 3697
Cdd:pfam13868 308 -AEREEELEEGERLREEEAERRERIEEER 335
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
3421-3740 |
2.28e-08 |
|
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: 60.93 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3421 EKMLKEKMQAIQEASRLKAEAE-----LLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAE 3495
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEkeatkDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3496 KLKLQVSQLSVAQAKAEEEAKRFKKQAdniAARLLETEIATKDKSTVMQ---QLEVERRNNSKEADDLRNAIANLETEK- 3571
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEA---LAEKLKEVINLAKQSEEEAappLLDAAPETPPKLPEHLDNVEEKVEKAQs 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3572 -ARLKKDAEELQNKSKEMADAQMKQIEHEKTmlqqTFLTEKEMLLK----------KERLIEDEKKRLESQYEEEAKKAK 3640
Cdd:pfam09731 241 lAKLVDQYKELVASERIVFQQELVSIFPDII----PVLKEDNLLSNddlnsliahaHREIDQLSKKLAELKKREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3641 ALTDEQERQRKLMEEEKKKLHATMDEALSK-QKEAEREMLNKQKEMQELEKKRLEQEKVLAEEnkKLRDQLQQLEEAQKE 3719
Cdd:pfam09731 317 ALEKQKEELDKLAEELSARLEEVRAADEAQlRLEFEREREEIRESYEEKLRTELERQAEAHEE--HLKDVLVEQEIELQR 394
|
330 340
....*....|....*....|.
gi 1838104091 3720 KNTQVISAAtVETTKNVYNGQ 3740
Cdd:pfam09731 395 EFLQDIKEK-VEEERAGRLLK 414
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2550-2899 |
2.72e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 60.29 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2550 SEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTL----NQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKqvi 2625
Cdd:pfam07888 39 CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRreleSRVAELKEELRQSREKHEELEEKYKELSASSEELSE--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2626 EETQKKRTAEEELKRKSEAEKEAAKQKQKALE---DLENLKMQAEEAERKVKQAQIEKeKQIQIAHVAAE---KSATAEL 2699
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2700 QSTQRSFVEKTSKLEESlkQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALR--------LRLQAEE 2771
Cdd:pfam07888 195 QELRNSLAQRDTQVLQL--QDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGeelssmaaQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2772 EAHKKSLAQEEAEKQKEEAE---REAKKRAKAEESALKQKEMAEK--------ELERQRKVADSTAQQKLTAEQELIRlr 2840
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASlalREGRARWAQERETLQQSAEADKdrieklsaELQRLEERLQEERMEREKLEVELGR-- 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 2841 aEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLedeLAKMRSEMEILIQLKSRAEKET 2899
Cdd:pfam07888 351 -EKDCNRVQLSESRRELQELKASLRVAQKEKEQL---QAEKQELLEYIRQLEQRLETVA 405
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2601-2750 |
3.19e-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: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2601 EKAAEAERLRKLAQEEAEKLHKQVIEETQK----KRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQA 2676
Cdd:TIGR02794 83 QRAAEQARQKELEQRAAAEKAAKQAEQAAKqaeeKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAA 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 2677 QIEKEKQIQIAHVAAEKSATAElqstqrsfVEKTSKLEESLKQEHGTVLQLQQEAAHlKKQQEDALKAREEAEK 2750
Cdd:TIGR02794 163 EAKKKAEEAKKKAEAEAKAKAE--------AEAKAKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAER 227
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2594-2828 |
3.53e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.89 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2594 TELKQLREKA-AEAERLRKLAQEEAEKlhkqviEETQKKRTAEEELKRKSEAEKEAAKQKQKAledlenlkmqaeEAERK 2672
Cdd:COG2268 195 AEIIRDARIAeAEAERETEIAIAQANR------EAEEAELEQEREIETARIAEAEAELAKKKA------------EERRE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2673 VKQAQIEKEKQIQIAHVAAEKSataelqstqrsfvektskleeslkqehgtvLQLQQEAAHLKKQQEDALKAREEAEKEL 2752
Cdd:COG2268 257 AETARAEAEAAYEIAEANAERE------------------------------VQRQLEIAEREREIELQEKEAEREEAEL 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 2753 DKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQkeeaerEAkKRAKAE-ESALKQKEMAEKELERQRKVADSTAQQ 2828
Cdd:COG2268 307 EADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEA------EG-KRALAEaWNKLGDAAILLMLIEKLPEIAEAAAKP 376
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
1270-1369 |
3.58e-08 |
|
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: 54.69 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1270 TAKEKLLCWSQRMTdgyQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQ-ENLEQAFNVAERDLGVTRLLD 1348
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQPvQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|.
gi 1838104091 1349 PEDVDVPHPDEKSIITYVSSL 1369
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQF 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
3266-3793 |
3.76e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.57 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3266 NAALEQKKKadaEMAKHKKLAEQTL------KQKFQVEQELTKVKLKLddtdkqkdlLDDELQRLKDEVDDAVKQRGQVE 3339
Cdd:pfam01576 91 SQQLQNEKK---KMQQHIQDLEEQLdeeeaaRQKLQLEKVTTEAKIKK---------LEEDILLLEDQNSKLSKERKLLE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3340 EELFKVKVQM-EELLKVK----LKIEKENQLLIKKDKDKAQQLLAEEAENMKRlAKEAAILSVESQEASRLRQIAEedLV 3414
Cdd:pfam01576 159 ERISEFTSNLaEEEEKAKslskLKNKHEAMISDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAE--LR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3415 QQRALAEKMLKEKMQAIQEASRLK---------AEAELLQRQKDLAQEQAQRLLEDKelmQKR-LDEETEeyqkSLEAER 3484
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKnnalkkireLEAQISELQEDLESERAARNKAEK---QRRdLGEELE----ALKTEL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3485 KRQLEIVAEAEKLKLQVSQ-LSVAQAKAEEEAKRFKKQADNIAARlleteiATKDKSTVMQQLEVERRNNskeaddlrna 3563
Cdd:pfam01576 309 EDTLDTTAAQQELRSKREQeVTELKKALEEETRSHEAQLQEMRQK------HTQALEELTEQLEQAKRNK---------- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3564 iANLETEKARLKKDAEELQNKSKEMADAQMKqiehektmlqqtfltekemllkkerlIEDEKKRLESQYEEEAKKAkalt 3643
Cdd:pfam01576 373 -ANLEKAKQALESENAELQAELRTLQQAKQD--------------------------SEHKRKKLEGQLQELQARL---- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3644 DEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKK-----------------L 3706
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQklnlstrlrqledernsL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3707 RDQLQQLEEAQK--EKNTQVISAATVETTKNVyngQNAGDVVDSVENKPDPLSfdgirdkvpasrlRDVGLLSKK----- 3779
Cdd:pfam01576 502 QEQLEEEEEAKRnvERQLSTLQAQLSDMKKKL---EEDAGTLEALEEGKKRLQ-------------RELEALTQQleeka 565
|
570
....*....|....*
gi 1838104091 3780 -EFDKLKKGKATVQQ 3793
Cdd:pfam01576 566 aAYDKLEKTKNRLQQ 580
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2361-3040 |
3.77e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.84 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2361 DSKTLKEQLSQEKKLLEEIENNKEN-VDEcqkyAKAYINSIKDYelqlvaynakADPHASPLKKNKMDSASDNIIQEYVT 2439
Cdd:TIGR01612 1119 DIKNLDQKIDHHIKALEEIKKKSENyIDE----IKAQINDLEDV----------ADKAISNDDPEEIEKKIENIVTKIDK 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2440 LRTRYSELMTLTSQyikfITETQRRLEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQmK 2519
Cdd:TIGR01612 1185 KKNIYDEIKKLLNE----IAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEK-S 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2520 QEVSKREVAALDAENQKKNIELELHELKKL-SEQQINDKSqlVDDALQSRTKIEEEIHII------RIQLETTLNQKSTA 2592
Cdd:TIGR01612 1260 PEIENEMGIEMDIKAEMETFNISHDDDKDHhIISKKHDEN--ISDIREKSLKIIEDFSEEsdindiKKELQKNLLDAQKH 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREKAAEAERLRKLAQEeaeklhKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLkmqaEEAERK 2672
Cdd:TIGR01612 1338 NSDINLYLNEIANIYNILKLNKI------KKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINL----EECKSK 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2673 VKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAH-LKKQQEDALKAREEAEKE 2751
Cdd:TIGR01612 1408 IESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHiLKIKKDNATNDHDFNINE 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2752 LDKWRQKANEAlrlrlqaeeeahkkslaqeeaekqkeeaEREAKKRAKAEESalkqkemaEKELERQRKVADSTAQQKLT 2831
Cdd:TIGR01612 1488 LKEHIDKSKGC----------------------------KDEADKNAKAIEK--------NKELFEQYKKDVTELLNKYS 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2832 AeqelIRLRAEFDNAEQQRSLLEDELYRLKNEVIAaqqQRKQLEDELAKMRSEmeiliqlKSRAEKETMSNTEKSKMLLD 2911
Cdd:TIGR01612 1532 A----LAIKNKFAKTKKDSEIIIKEIKDAHKKFIL---EAEKSEQKIKEIKKE-------KFRIEDDAAKNDKSNKAAID 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2912 AEASkmrdVAEEAGKLRAIAE-EAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEI--ALKEKEAENERLR 2988
Cdd:TIGR01612 1598 IQLS----LENFENKFLKISDiKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFleSLKDQKKNIEDKK 1673
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 2989 RAAEDEAYQRKALEDEANQHKKEIE----EKIVQLKKSSQAEMQRQKAMVDDTLKQ 3040
Cdd:TIGR01612 1674 KELDELDSEIEKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3253-3544 |
3.91e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 60.31 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3253 EAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVD 3329
Cdd:PRK11281 32 NGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3330 DAVKQR------GQVEEELFKVKVQMEEllkVKLKIEKENQLLIkkdkdkAQQLLAEEA-----ENMKRLAKEAAILSVE 3398
Cdd:PRK11281 112 EETRETlstlslRQLESRLAQTLDQLQN---AQNDLAEYNSQLV------SLQTQPERAqaalyANSQRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3399 SQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKaeaELLQRQKDLAQEQAQRLLEDKELMQ-----KRLD--E 3471
Cdd:PRK11281 183 KVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTlsE 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 3472 ET-EEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQ 3544
Cdd:PRK11281 260 KTvQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLK 333
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3118-3309 |
5.68e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3118 EKEAGRQRKIAQDELDRL-----KKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMmhKKLQ 3192
Cdd:PRK09510 94 QKQAAEQERLKQLEKERLaaqeqKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA--KKKA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3193 QEYEKakklakeaeaakekaekeavllRKQAEEAEsqkaaAEKEAAIQAKAQEDAErlrKEAEFEAAKRAQAE---NAAL 3269
Cdd:PRK09510 172 EAEAA----------------------KKAAAEAK-----KKAEAEAAAKAAAEAK---KKAEAEAKKKAAAEakkKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838104091 3270 EQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDD 3309
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2628-2890 |
6.15e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.32 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2628 TQKKRTAEEELKRKSEAEKEAAKQKQKaledlenlkmQAEEAERkvkQAQIEKEKQIQIAHVAAEKSATAELQStqrsfv 2707
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQ----------RAAEQAR---QKELEQRAAAEKAAKQAEQAAKQAEEK------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2708 ektskleeslkqehgtvlqlQQEAAHLKKQQEDALKAREEAEKEldkwRQKANEALRlrlQAEEEAHKKSLAQEEAEKQK 2787
Cdd:TIGR02794 118 --------------------QKQAEEAKAKQAAEAKAKAEAEAE----RKAKEEAAK---QAEEEAKAKAAAEAKKKAEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2788 EEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAA 2867
Cdd:TIGR02794 171 AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
250 260
....*....|....*....|...
gi 1838104091 2868 QQQRKQLEDELAKMRSEMEILIQ 2890
Cdd:TIGR02794 251 GARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5143-5179 |
6.27e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.71 E-value: 6.27e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1838104091 5143 IRLLEAQIATGGIIDPEKSHRLPVEVAYKRGFFDEEM 5179
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2582-2801 |
6.60e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.32 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2582 LETTLNQKSTAETELKQLREKAAEAERlrklAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEdlen 2661
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQ---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2662 lkmQAEEAERKVKQAQIEKEKQiqiahvAAEKSATAElqstqrsfVEKTSKLEESLKQehgtvlqlQQEAAHLKKQQEDA 2741
Cdd:TIGR02794 110 ---AAKQAEEKQKQAEEAKAKQ------AAEAKAKAE--------AEAERKAKEEAAK--------QAEEEAKAKAAAEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2742 LKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAE 2801
Cdd:TIGR02794 165 KKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAE 224
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2593-2996 |
6.63e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.58 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREKAAEAERLRKlAQEEAEKLHKQVIEETQKKRTAEEELkrkseaekeaakQKQKALEDLENLKMQAEEAERK 2672
Cdd:COG3096 835 EAELAALRQRRSELERELA-QHRAQEQQLRQQLDQLKEQLQLLNKL------------LPQANLLADETLADRLEELREE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2673 VKQAQiEKEKQIQIAHVAAEKSAT--AELQSTQRSFvektskleESLKQEHGTVLQLQQEAahlkKQQEDALK------- 2743
Cdd:COG3096 902 LDAAQ-EAQAFIQQHGKALAQLEPlvAVLQSDPEQF--------EQLQADYLQAKEQQRRL----KQQIFALSevvqrrp 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2744 --AREEAEKELDKwRQKANEALRLRL-QAEEEAhkkslaqeeaekqkeeaeREAKKRAKAeesALKQKEMAEKELERQRK 2820
Cdd:COG3096 969 hfSYEDAVGLLGE-NSDLNEKLRARLeQAEEAR------------------REAREQLRQ---AQAQYSQYNQVLASLKS 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2821 VADSTAQQKLTAEQEL--IRLRAEfDNAEQQRSLLEDELYrlkNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKE 2898
Cdd:COG3096 1027 SRDAKQQTLQELEQELeeLGVQAD-AEAEERARIRRDELH---EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2899 TmsnTEKSKMLLDAEASKMRdvaeeagkLRAIAEEAKYQRQIAEEEAARQRAeaerilkEKLAAISEatrlktEAEIALK 2978
Cdd:COG3096 1103 Y---KQEREQVVQAKAGWCA--------VLRLARDNDVERRLHRRELAYLSA-------DELRSMSD------KALGALR 1158
|
410 420
....*....|....*....|.
gi 1838104091 2979 EKEAENERLR---RAAEDEAY 2996
Cdd:COG3096 1159 LAVADNEHLRdalRLSEDPRR 1179
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
1145-1254 |
6.80e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 54.04 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1145 EDERDrvqKKTFTKWVNKHLIKRaesqhHVTDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHKLQNVQIALD 1219
Cdd:cd21299 1 ETSRE---ERCFRLWINSLGIDT-----YVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVK 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1838104091 1220 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1254
Cdd:cd21299 73 IGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2458-2683 |
7.42e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2458 ITETQRRLEDEEKAakilKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQevSKREVAALDAENQKk 2537
Cdd:COG4942 22 AAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--LEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2538 nIELELHELKKLSEQQI--------NDKSQLV---DDALQSRTKIEEEIHIIRIQLEttlnqkstaetELKQLREKAAEA 2606
Cdd:COG4942 95 -LRAELEAQKEELAELLralyrlgrQPPLALLlspEDFLDAVRRLQYLKYLAPARRE-----------QAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 2607 ERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQ 2683
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2434-3605 |
9.91e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2434 IQEYVTLRTRYSELMTLTSQYIkfitetqrrledeekAAKILKAEEQKKMADLQAeLDKQKKLAEAHaKAIAKAEKEADE 2513
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---------------AADYMRHANERRVHLEEA-LELRRELYTSR-RQLAAEQYRLVE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2514 LKhqmkqevskREVAALdaENQKKNIELELhelkklseQQINDKSQLVDDALQSRTKIEEeihiiriqlettlnqkstAE 2593
Cdd:PRK04863 312 MA---------RELAEL--NEAESDLEQDY--------QAASDHLNLVQTALRQQEKIER------------------YQ 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2594 TELKQLREKAAEAERLRKLAQEeaeklhkQVIEETQKKRTAEEELKR-KS----------EAEKEAA--KQKQKALE--- 2657
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADE-------QQEENEARAEAAEEEVDElKSqladyqqaldVQQTRAIqyQQAVQALErak 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2658 --------DLENLKMQAEEAERKVKQAQ---IEKEKQIQIAHVAAEKSATA-----------ELQSTQRSFVEKTSKLEE 2715
Cdd:PRK04863 428 qlcglpdlTADNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAAHSQFEQAyqlvrkiagevSRSEAWDVARELLRRLRE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2716 sLKQEHGTVLQLQQEAAHLKK---QQEDALKAREEAEKELDkwRQKANEALRLRLQAEEEAHKKSLAqeeaekqkeeaer 2792
Cdd:PRK04863 508 -QRHLAEQLQQLRMRLSELEQrlrQQQRAERLLAEFCKRLG--KNLDDEDELEQLQEELEARLESLS------------- 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2793 EAKKRAKAEESALKQKEmaeKELERQRKVADSTAQQKLTAEQELIRLR----AEFDNAEQQRSLLEDELYRLKN---EVI 2865
Cdd:PRK04863 572 ESVSEARERRMALRQQL---EQLQARIQRLAARAPAWLAAQDALARLReqsgEEFEDSQDVTEYMQQLLEREREltvERD 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2866 AAQQQRKQLEDELAKMR----SEMEILIQLKSRAEKETMSNtekskmLLDaeaskmrDVA-EEAGKLRAIAEEAKYQRQI 2940
Cdd:PRK04863 649 ELAARKQALDEEIERLSqpggSEDPRLNALAERFGGVLLSE------IYD-------DVSlEDAPYFSALYGPARHAIVV 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2941 AEEEAARQRAEAERILKEKL-------AAISEATRLKTEAEIALKEKEAENE-RLRRAAEDEAYQRKALEDEANQHKKEI 3012
Cdd:PRK04863 716 PDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQwRYSRFPEVPLFGRAAREKRIEQLRAER 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3013 EEKIVQLKKSS--QAEMQRQKAMVDDTLKQRRVV------EEEIRilKLNFEKAssgkldlELElNKLKNIAEETQQSKL 3084
Cdd:PRK04863 796 EELAERYATLSfdVQKLQRLHQAFSRFIGSHLAVafeadpEAELR--QLNRRRV-------ELE-RALADHESQEQQQRS 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3085 RAeeeaeKQRKLAMeeekrrreaeetvkkiTAAEKEAGRQRKIAQDELDrlkKKAEEARKQKDKAdsEAEKQIVAASQAA 3164
Cdd:PRK04863 866 QL-----EQAKEGL----------------SALNRLLPRLNLLADETLA---DRVEEIREQLDEA--EEAKRFVQQHGNA 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3165 LkcrtaeQQVQSVLAQQKEDSMMHKKLQQEYekakklakeaeaakekaekeavllrKQAEEAESQKaaaekeaaiqaKAQ 3244
Cdd:PRK04863 920 L------AQLEPIVSVLQSDPEQFEQLKQDY-------------------------QQAQQTQRDA-----------KQQ 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3245 EDA--ERLRKEAEF--EAAKRAQAENAALEQKKKADAEMAkhkklaeqtlkqkfqvEQELTKVKLKLDDTDKQKDLLDDE 3320
Cdd:PRK04863 958 AFAltEVVQRRAHFsyEDAAEMLAKNSDLNEKLRQRLEQA----------------EQERTRAREQLRQAQAQLAQYNQV 1021
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3321 LQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKE--NQLLIKKDKDKAQ---QLLAEEAEnMKRLAKeaail 3395
Cdd:PRK04863 1022 LASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDelHARLSANRSRRNQlekQLTFCEAE-MDNLTK----- 1095
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3396 svesqeasRLRQiAEEDLVQQRALAEKMLKekmqAIQEASRLKAEAELLQRqkdlaqeqaqrlLEDKELMQKRLDEETEE 3475
Cdd:PRK04863 1096 --------KLRK-LERDYHEMREQVVNAKA----GWCAVLRLVKDNGVERR------------LHRRELAYLSADELRSM 1150
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3476 YQKSLEAERKRqleiVAEAEKLKlQVSQLSVAQAKAEEEAKRFkkqadniaarlleteiatkdkSTVMQQLEVERRNNSK 3555
Cdd:PRK04863 1151 SDKALGALRLA----VADNEHLR-DVLRLSEDPKRPERKVQFY---------------------IAVYQHLRERIRQDII 1204
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 3556 EADDLRNAIANLETEKARLKKDAEELQNK----SKEMADAQMKQIEHEK---TMLQQ 3605
Cdd:PRK04863 1205 RTDDPVEAIEQMEIELSRLTEELTSREQKlaisSESVANIIRKTIQREQnriRMLNQ 1261
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2657-2999 |
1.13e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.62 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2657 EDLENLKMQAEEAE-RKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQE---HGTVLQLQQEAA 2732
Cdd:pfam13868 6 DELRELNSKLLAAKcNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEErkrYRQELEEQIEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2733 HLKKQQEdALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALK--QKEM 2810
Cdd:pfam13868 86 EQKRQEE-YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeyLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2811 AEKELERQRKVAdstaQQKLTAEQELIRLRAEFDNAEQQRslleDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQ 2890
Cdd:pfam13868 165 AEREEEREAERE----EIEEEKEREIARLRAQQEKAQDEK----AERDELRAKLYQEEQERKERQKEREEAEKKARQRQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2891 LKSRAEKETMsntEKSKMLldaEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEkLAAISEATRLK 2970
Cdd:pfam13868 237 LQQAREEQIE---LKERRL---AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ-IEEREEQRAAE 309
|
330 340
....*....|....*....|....*....
gi 1838104091 2971 TEAEIALKEKEAENERLRRAAEDEAYQRK 2999
Cdd:pfam13868 310 REEELEEGERLREEEAERRERIEEERQKK 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3130-3719 |
1.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3130 DELDRLKKKAEEARKQKdkadsEAEKQIVAASQAALKCRTAEQQVQSVLAQQKedsmmHKKLQQEYEkakklakeaeaak 3209
Cdd:COG4913 235 DDLERAHEALEDAREQI-----ELLEPIRELAERYAAARERLAELEYLRAALR-----LWFAQRRLE------------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3210 ekaekeavLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEfeaAKRAQAENAALEQKKKADAEMAKHKKLAEQT 3289
Cdd:COG4913 292 --------LLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDRLEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3290 LKQkfqVEQELTKVKLKLDDTDKQkdlLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLikk 3369
Cdd:COG4913 361 RAR---LEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3370 dkdKAQQLL--AEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRAlAEKML--------------KEKMQAIqE 3433
Cdd:COG4913 432 ---ERRKSNipARLLALRDALAEALGLDEAELPFVGELIEVRPEEERWRGA-IERVLggfaltllvppehyAAALRWV-N 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3434 ASRLKAEAELLQRQKDLAQEQAQRLLED-----------------KELMQKRLD-------EETEEYQKSL--------- 3480
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFDyvcvdspEELRRHPRAItragqvkgn 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3481 --------------------EAERKRQlEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIA--ARLLETEIATKD 3538
Cdd:COG4913 587 gtrhekddrrrirsryvlgfDNRAKLA-ALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3539 KSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMA--DAQMKQIEHEKTMLQQTfLTEKEMLLK 3616
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGrlEKELEQAEEELDELQDR-LEAAEDLAR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3617 KERLIE-DEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEK--KRL 3693
Cdd:COG4913 745 LELRALlEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllDRL 824
|
650 660
....*....|....*....|....*.
gi 1838104091 3694 EQEKvLAEENKKLRDQLQQLEEAQKE 3719
Cdd:COG4913 825 EEDG-LPEYEERFKELLNENSIEFVA 849
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2595-2834 |
1.14e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAAEA-----ERLRKLAQEEAEKL--HKQVIEETQKKRT-----AEEELKRKSEAEKEAAKQKQKALEDLENL 2662
Cdd:PRK05035 440 AIEQEKKKAEEAkarfeARQARLEREKAAREarHKKAAEARAAKDKdavaaALARVKAKKAAATQPIVIKAGARPDNSAV 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2663 KMQAEEAERKVKQAQIE---------KEKQIQ--IAHVAAEKSATAELQSTQRSFVE-KTSKLEESLkqehgtvlqlqqE 2730
Cdd:PRK05035 520 IAAREARKAQARARQAEkqaaaaadpKKAAVAaaIARAKAKKAAQQAANAEAEEEVDpKKAAVAAAI------------A 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2731 AAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEM 2810
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANA 667
|
250 260
....*....|....*....|....*...
gi 1838104091 2811 AEKELERQRKVADSTA----QQKLTAEQ 2834
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3550-3723 |
1.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3550 RRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLE 3629
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3630 SQYEEEAKKAKALTDEQERQRKLmEEEKKKLHATMDEALSKQKEAEREMLNK-QKEMQELEKKRLEQEKVLAEENKKLRD 3708
Cdd:COG4717 146 ERLEELEERLEELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*
gi 1838104091 3709 QLQQLEEAQKEKNTQ 3723
Cdd:COG4717 225 LEEELEQLENELEAA 239
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2586-3073 |
1.22e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 58.91 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2586 LNQKSTAETEL--KQLREKAAEAERLRKLAQEEaeklhkqVIEETQKKRTAEEElkRKSEAEKeaAKQKQKALEDLENLK 2663
Cdd:PRK10929 13 LSWGAYAATAPdeKQITQELEQAKAAKTPAQAE-------IVEALQSALNWLEE--RKGSLER--AKQYQQVIDNFPKLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2664 mqaeeaeRKVKQaQIEKEKQIQIAhvAAEKSATAELQstQRSFVEKTSKLEES--LKQEHGTVLQLQQEAAHLKKQQEDA 2741
Cdd:PRK10929 82 -------AELRQ-QLNNERDEPRS--VPPNMSTDALE--QEILQVSSQLLEKSrqAQQEQDRAREISDSLSQLPQQQTEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2742 LKAREEAEKEL---DKWRQKANEALRLRLQAEEEAHKkslaqeeaekqkeeaereakkrAKAEESALKQkemaekelerq 2818
Cdd:PRK10929 150 RRQLNEIERRLqtlGTPNTPLAQAQLTALQAESAALK----------------------ALVDELELAQ----------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2819 rkvadstaqqkLTA--EQELIRLRAEFdnaeqqrslledelyrlkneviaAQQQRKQLEDELAKMRSemeiliQLKSRAE 2896
Cdd:PRK10929 197 -----------LSAnnRQELARLRSEL-----------------------AKKRSQQLDAYLQALRN------QLNSQRQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2897 KETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAaiseatrLKTEAEIA 2976
Cdd:PRK10929 237 REAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------LNTLREQS 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2977 --LKEKEAENERLR----RAAEDEAYQRkaLEDEANQ---HKKEIEEkivQLKKSSQAEMQRQKAMVDDTLKQRRVVEEE 3047
Cdd:PRK10929 310 qwLGVSNALGEALRaqvaRLPEMPKPQQ--LDTEMAQlrvQRLRYED---LLNKQPQLRQIRQADGQPLTAEQNRILDAQ 384
|
490 500
....*....|....*....|....*.
gi 1838104091 3048 IRILKLNFEKASSGKLDLELELNKLK 3073
Cdd:PRK10929 385 LRTQRELLNSLLSGGDTLILELTKLK 410
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2595-2974 |
1.23e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAAEAERLRKLAQE---EAEKLHKQVIEETQKKRTAEEELkrksEAEKEAAK----------QKQKALE---- 2657
Cdd:COG3096 279 ERRELSERALELRRELFGARRqlaEEQYRLVEMARELEELSARESDL----EQDYQAASdhlnlvqtalRQQEKIEryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2658 DLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAE-----KSATAELQS------------------------------- 2701
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEevdslKSQLADYQQaldvqqtraiqyqqavqalekaralcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2702 TQRSFVEKTSKLEESLKQEHGTVLQLQQ-----EAAHlkKQQEDALKAREEAEKELDKWR--QKANEALR----LRLQAE 2770
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQklsvaDAAR--RQFEKAYELVCKIAGEVERSQawQTARELLRryrsQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2771 EEAHkkslaqeeaekqkeeaereakkrAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEfdnAEQQR 2850
Cdd:COG3096 513 RLQQ-----------------------LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE---LEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2851 SLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEK-ETMSNTEkskmLLDAEA--SKMRDVAEeagKL 2927
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERlREQSGEA----LADSQEvtAAMQQLLE---RE 639
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1838104091 2928 RaiaeeakyQRQIAEEEAARQRAEAERILKEKLAAI-SEATRLKTEAE 2974
Cdd:COG3096 640 R--------EATVERDELAARKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3459-3723 |
1.28e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.24 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3459 LEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQadniaarlLETEIATKD 3538
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQ--------EEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3539 KSTVMQQLEVErrnnskEADDLRNAIANLETEKARLK--KDAEELQNKSKEMADAQMKqIEHEKTMLQQTFLTEKEMLLK 3616
Cdd:pfam13868 100 REQMDEIVERI------QEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEER-EEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3617 KERLIEDEKKRLE----SQYEEEAKKAKALTDEQeRQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKR 3692
Cdd:pfam13868 173 AEREEIEEEKEREiarlRAQQEKAQDEKAERDEL-RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270
....*....|....*....|....*....|..
gi 1838104091 3693 LEQEKVLAE-ENKKLRDQLQQLEEAQKEKNTQ 3723
Cdd:pfam13868 252 LAEEAEREEeEFERMLRKQAEDEEIEQEEAEK 283
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2610-3081 |
1.46e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 58.12 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2610 RKLAQEEAEKLHKQVieetqkkrtaeEELKRKSEAekeAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAH- 2688
Cdd:pfam05701 37 RKLVELELEKVQEEI-----------PEYKKQSEA---AEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSEl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2689 -----------VAAEKS--ATAELQSTQRSFVEKTSKLeESLKQEHGTvlqLQQEAAHLKKQQEDALKAREEAEKELDKW 2755
Cdd:pfam05701 103 aklrveemeqgIADEASvaAKAQLEVAKARHAAAVAEL-KSVKEELES---LRKEYASLVSERDIAIKRAEEAVSASKEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2756 RQKANEalrlrLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKE--MAEKELERQRKVADSTA--QQKL- 2830
Cdd:pfam05701 179 EKTVEE-----LTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKElkQAEEELQRLNQQLLSAKdlKSKLe 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2831 TAEQELIRLRAEFdnAEQQRSLLEDELYRLKNEVI-------AAQQQRKQLED---ELAKMRSEMEIL----IQLKSRAE 2896
Cdd:pfam05701 254 TASALLLDLKAEL--AAYMESKLKEEADGEGNEKKtstsiqaALASAKKELEEvkaNIEKAKDEVNCLrvaaASLRSELE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2897 KE-----------TMSNTEKSKmlLDAEAS------------------KMRDVAEEAGKLRAIAEEAKYQRQIAEEEAAR 2947
Cdd:pfam05701 332 KEkaelaslrqreGMASIAVSS--LEAELNrtkseialvqakekeareKMVELPKQLQQAAQEAEEAKSLAQAAREELRK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2948 QRAEAER--------------ILKEKLAAIsEATRLKTEAEIALKEKEAENERLRRAA----------EDEAYQRKALED 3003
Cdd:pfam05701 410 AKEEAEQakaaastvesrleaVLKEIEAAK-ASEKLALAAIKALQESESSAESTNQEDsprgvtlsleEYYELSKRAHEA 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3004 EANQHKKeIEEKIVQLKKSSQAEMqRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKniAEETQQ 3081
Cdd:pfam05701 489 EELANKR-VAEAVSQIEEAKESEL-RSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRKWR--AEHEQR 562
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2363-3048 |
1.47e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2363 KTLKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQLvaynakadphasplkKNKMDSASDNIIQEYVTLRT 2442
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDL---------------NDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2443 RYSELMTLTSQYIKfitetqrrLEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADEL---KHQMK 2519
Cdd:TIGR04523 108 INSEIKNDKEQKNK--------LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELeneLNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2520 QEVSKREVAALDAENQKKNIELELHELKKLSEQQINDKSQLVDDALQsRTKIEEEIHIIRIQLETTLNQKSTAETELKQL 2599
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2600 REKAAEAERLRKLAQEEAEKLHKQVIEET---QKKRTAEEELKRKSEAE-----KEAAKQKQKALEDLENLKMQAEEAER 2671
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEkqlNQLKSEISDLNNQKEQDwnkelKSELKNQEKKLEEIQNQISQNNKIIS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2672 KVKQ--AQIEKEKqiqiahvaaeKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQeaahLKKQQEDaLKAREEAE 2749
Cdd:TIGR04523 339 QLNEqiSQLKKEL----------TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN----LESQIND-LESKIQNQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2750 KELDKWRQKANEALRLRLQAEEEAHKKSLAQEEaekqkeeaerEAKKRAKAEESALKQKEMAEKELERQRkvaDSTAQQK 2829
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETII----------KNNSEIKDLTNQDSVKELIIKNLDNTR---ESLETQL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2830 LTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMS-NTEKSKM 2908
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDlEDELNKD 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2909 LLDAEASKMRDVAEEagklraiaeeakYQRQIAEeeaarqraeaeriLKEklaAISEATRLKTEAEIALKEKEAENERLR 2988
Cdd:TIGR04523 551 DFELKKENLEKEIDE------------KNKEIEE-------------LKQ---TQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 2989 RAAEDEAYQRKALEDEANQHKKEiEEKIVQLKK---SSQAEMQRQKAMVDDTLKQRRVVEEEI 3048
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKnikSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2438-2761 |
1.50e-07 |
|
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: 58.10 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2438 VTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQKKMADLQAEL---DKQKKLAEAHAKaiAKAEKEADEL 2514
Cdd:NF033838 87 VALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKkvaEATKKVEEAEKK--AKDQKEEDRR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2515 KH-QMKQEVSKREVAALDAENQKKNIELELHELKK-LSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLEttlNQKSTA 2592
Cdd:NF033838 165 NYpTNTYKTLELEIAESDVEVKKAELELVKEEAKEpRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEE---EAKRRA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREK---AAEAERLRKLA--------------QEEAEKLHKQVIEET-------QKKRTAEEElKRKSEAEKEA 2648
Cdd:NF033838 242 DAKLKEAVEKnvaTSEQDKPKRRAkrgvlgepatpdkkENDAKSSDSSVGEETlpspslkPEKKVAEAE-KKVEEAKKKA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2649 AKQKQkalEDLEN--------LKMQAEEAERKVKQAQIEKEKQiqiahvaaeksataelqstqrsfVEKTSKLEESLKQE 2720
Cdd:NF033838 321 KDQKE---EDRRNyptntyktLELEIAESDVKVKEAELELVKE-----------------------EAKEPRNEEKIKQA 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1838104091 2721 HGTVLQLQQEAAHLKKQQEDALKAREEAEK---ELDKWRQKANE 2761
Cdd:NF033838 375 KAKVESKKAEATRLEKIKTDRKKAEEEAKRkaaEEDKVKEKPAE 418
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
3570-3714 |
1.51e-07 |
|
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: 56.91 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3570 EKARLKKDAEELQNKSKEmADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRlesqyEEEAKKAKALTDEQERQ 3649
Cdd:pfam02841 156 ERDKLEAKYNQVPRKGVK-AEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAK-----AEAAEAEQELLREKQKE 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3650 RKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQeLEKKRLEQEKVLAE----ENKKLRDQLQQLE 3714
Cdd:pfam02841 230 EEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERM-LEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2497-2751 |
1.60e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2497 AEAHAKAIAKAEKEADELKHQMKQEVSKREvaalDAENQKKNIELELHELkklsEQQINDKSQLVDDALQSRTKieeeih 2576
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAA------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2577 iIRIQLETTLNQKSTAETELKQLREKAAEAER-LRKLAQEEAEK--LHKQVIEETQKKRTAeeeLKRKSEAEKEAAKQKQ 2653
Cdd:COG4942 81 -LEAELAELEKEIAELRAELEAQKEELAELLRaLYRLGRQPPLAllLSPEDFLDAVRRLQY---LKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2654 KALEDLENLKMQAEEAERKVKQAQIEKEKQIQiahvaaeksataELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAH 2733
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 1838104091 2734 LKKQQEDALKAREEAEKE 2751
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
3242-3694 |
1.70e-07 |
|
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: 57.83 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAE-----MAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDL 3316
Cdd:pfam05557 18 KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkrirlLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3317 LDDELQRLKDEVDDAVKQRGQveeELFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAIls 3396
Cdd:pfam05557 98 QLADAREVISCLKNELSELRR---QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3397 vesQEASRLRQIAEEDlvqqrALAEKMLKEKMQAIQEASRLkaeaelLQRQKDlAQEQAQRLLEDKELmqkrLDEETEEY 3476
Cdd:pfam05557 173 ---KELEFEIQSQEQD-----SEIVKNSKSELARIPELEKE------LERLRE-HNKHLNENIENKLL----LKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3477 QKSLEAERKRQLEIVA-EAEKLKLQ--------VSQLSVAQAKAEEEAKRFKKQadniaarLLETEIATKD-KSTVMQQL 3546
Cdd:pfam05557 234 KRKLEREEKYREEAATlELEKEKLEqelqswvkLAQDTGLNLRSPEDLSRRIEQ-------LQQREIVLKEeNSSLTSSA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3547 EVERRNNSKEADDLRNAIANLETEKARLKKD---AEELQNK----SKEMA---------DAQMKQIEHEKTMLQQTFLTE 3610
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKRHkalVRRLQRRvlllTKERDgyrailesyDKELTMSNYSPQLLERIEEAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3611 kEMLLKKERLIEDEKKRLE-SQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALS-KQK----EAEREMLNKQKE 3684
Cdd:pfam05557 387 -DMTQKMQAHNEEMEAQLSvAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSlRRKletlELERQRLREQKN 465
|
490
....*....|
gi 1838104091 3685 MQELEKKRLE 3694
Cdd:pfam05557 466 ELEMELERRC 475
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1275-1369 |
1.79e-07 |
|
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: 53.46 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1275 LLCWSQRMTDGYqNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQ-----------------------ENLE 1331
Cdd:cd21224 5 LLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSGLS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1332 QAFNVAER-----------DLG-VTRLLDPEDVDVPHPDEKSIITYVSSL 1369
Cdd:cd21224 84 SELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
1154-1251 |
1.97e-07 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 52.34 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1154 KTFTKWVNkHLIKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMrfhkLQNVQIALDFLRHRQVK 1227
Cdd:cd21286 3 KIYTDWAN-HYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVN 77
|
90 100
....*....|....*....|....
gi 1838104091 1228 LVNIRNDDIADGNPKLTLGLIWTI 1251
Cdd:cd21286 78 VQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1267-1367 |
1.98e-07 |
|
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: 52.86 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1267 EDMTAKEKLLCWSQ-RMTDgyqnIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQ-ENLEQAFNVAERDLGVT 1344
Cdd:cd21315 13 KGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDAvKNAKEAMDLAEDWLDVP 88
|
90 100
....*....|....*....|...
gi 1838104091 1345 RLLDPEDVDVPHPDEKSIITYVS 1367
Cdd:cd21315 89 QLIKPEEMVNPKVDELSMMTYLS 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2665-2901 |
2.22e-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: 56.70 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2665 QAEEAERKVKQAQiekeKQIQiahvaAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKA 2744
Cdd:COG4942 21 AAAEAEAELEQLQ----QEIA-----ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADS 2824
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 2825 TAQQKLTAEQELIRLRAEFDNAEQQRsllEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMS 2901
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
1266-1369 |
2.28e-07 |
|
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: 52.40 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1266 SEDMTAKEKLLCWSQrmtDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLI-DMGRVYQQSNQENLEQAFNVAERDLGVT 1344
Cdd:cd21313 4 AKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVP 80
|
90 100
....*....|....*....|....*
gi 1838104091 1345 RLLDPEDVDVPHPDEKSIITYVSSL 1369
Cdd:cd21313 81 QVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2701-3184 |
2.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2701 STQRSFVEktSKLEESLKQEHGTVLQLQ-QEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEE-EAHKKSL 2778
Cdd:COG4717 37 STLLAFIR--AMLLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEElEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2779 AQEeaekqkeeaeREAKKRAKAEESALKQKEMAEKEL----------ERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQ 2848
Cdd:COG4717 115 REE----------LEKLEKLLQLLPLYQELEALEAELaelperleelEERLEELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2849 QRSL-LEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSK---------------MLLDA 2912
Cdd:COG4717 185 QLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2913 EASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLrRAAE 2992
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL-LELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2993 DEAYQRKALEDEANQHKKEIEekIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKlnfEKASSGKLDLELELNKL 3072
Cdd:COG4717 344 DRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK---EELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3073 KNIAEETQQSKLRAEEEAEKQRklameeekrrreaeetVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSE 3152
Cdd:COG4717 419 EELLEALDEEELEEELEELEEE----------------LEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
490 500 510
....*....|....*....|....*....|..
gi 1838104091 3153 AEKQIVAASQAALkcRTAEQQVQSVLAQQKED 3184
Cdd:COG4717 483 AELRELAEEWAAL--KLALELLEEAREEYREE 512
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2251-2755 |
3.19e-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: 57.29 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2251 AKLKKMRAEAeGEQPVFDSLEEELQKATTVSEKMSRVHSERDIELDHFRQNVSGLQDRWKAVFTQMEIRHRELEQLGRQL 2330
Cdd:TIGR00618 400 KELDILQREQ-ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2331 GYYHESYdwlihwiTDAKERQEKIQAVSITDSKTLKEQLS---QEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQL 2407
Cdd:TIGR00618 479 EQIHLQE-------TRKKAVVLARLLELQEEPCPLCGSCIhpnPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2408 VAYNAKADPHasplkKNKMDSASDNiIQEYVTLRTRYSELMTLTSQYIKfitETQRRLEDEEKAAKILKAEEQKKMADLQ 2487
Cdd:TIGR00618 552 TSERKQRASL-----KEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITV---RLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2488 AELDKQKKLaeAHAKAIAKAEKEADELKHQMKQEVSKREVaaldaenqkKNIELELHELKKLSEQQIndksQLVDDALQS 2567
Cdd:TIGR00618 623 PEQDLQDVR--LHLQQCSQELALKLTALHALQLTLTQERV---------REHALSIRVLPKELLASR----QLALQKMQS 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2568 RTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKR-----TAEEELKRKS 2642
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQArtvlkARTEAHFNNN 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2643 EAEKEAAKQKQKALEDLENLKMQAEEAERKVKQ-AQIEKEKQIQIAHVAAEKSATAELQSTQRsfvEKTSKLEESLKQEH 2721
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLlKTLEAEIGQEIPSDEDILNLQCETLVQEE---EQFLSRLEEKSATL 844
|
490 500 510
....*....|....*....|....*....|....
gi 1838104091 2722 GTVLQLQQEAAHLKKQQEDALKAREEAEKELDKW 2755
Cdd:TIGR00618 845 GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
1118-1262 |
3.61e-07 |
|
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: 52.74 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1118 GSPGASSDEEWDHSLDEPEektwphfiederdrvqKKTFTKWVNKHLIKRAESQHHV------TDLYEDLRDGHNLISLL 1191
Cdd:cd21323 7 GGTSAISSEGTQHSYSEEE----------------KVAFVNWINKALEGDPDCKHVVpmnptdESLFKSLADGILLCKMI 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 1192 EVLSGDTLPR----EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 1262
Cdd:cd21323 71 NLSQPDTIDErainKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2795-3194 |
4.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2795 KKRAKAEESALKQKEMAEKELERQRKVADSTAQ---QKLTAEQELIRLRAEFDNAEQQRSLLED--ELYRLKNEVIAAQQ 2869
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAElqeELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2870 QRKQLEDELAKMRSEMEILIQLKSRAEKetmsntekskmlLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQR 2949
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEE------------LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2950 AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRA---------------AEDEAYQRKALEDEANQHKKEIEE 3014
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3015 KIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKasSGKLDLELELNKLKNIAEetQQSKLRAEEEAEKQR 3094
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGL--PPDLSPEELLELLDRIEE--LQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3095 KLAmeeeKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALkcrtaEQQV 3174
Cdd:COG4717 364 QLE----ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL-----EEEL 434
|
410 420
....*....|....*....|
gi 1838104091 3175 QSVLAQQKEDSMMHKKLQQE 3194
Cdd:COG4717 435 EELEEELEELEEELEELREE 454
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
3244-3740 |
5.17e-07 |
|
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: 56.37 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3244 QEDAERLRKEAEFEAakRAQAENAALEQKKKadaEMAKHKklaeQTLKQKFQVEQELTKVKL----------KLDDTDKQ 3313
Cdd:pfam10174 178 EEDWERTRRIAEAEM--QLGHLEVLLDQKEK---ENIHLR----EELHRRNQLQPDPAKTKAlqtviemkdtKISSLERN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3314 KDLLDDELQRLKDEVDDAVKQRgqvEEELFKVKVQMEELLKVKLKIEKENQLLIKKDkdkaQQLLAEEAEnmkrlakeaa 3393
Cdd:pfam10174 249 IRDLEDEVQMLKTNGLLHTEDR---EEEIKQMEVYKSHSKFMKNKIDQLKQELSKKE----SELLALQTK---------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3394 iLSVESQEASRLRQIAEedlvqqralaekMLKEKMQAI-QEASRLKAEAELLQrqkdLAQEQAQRLLEDKelmQKRLDEE 3472
Cdd:pfam10174 312 -LETLTNQNSDCKQHIE------------VLKESLTAKeQRAAILQTEVDALR----LRLEEKESFLNKK---TKQLQDL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3473 TEEyqKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAkaEEEAKRFKKQADNIAARL----------------LETEIAT 3536
Cdd:pfam10174 372 TEE--KSTLAGEIRDLKDMLDVKERKINVLQKKIENL--QEQLRDKDKQLAGLKERVkslqtdssntdtalttLEEALSE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3537 KDK--STVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEE-------LQNKSKEMADAQMKQIEHEKTMlqqtf 3607
Cdd:pfam10174 448 KERiiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEkesslidLKEHASSLASSGLKKDSKLKSL----- 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3608 ltEKEMLLKKERLIEDEKKRLESQYEEEAKKAKA-LTD-----EQERQRKlmEEEKKKLHATMDEALSKQKEAEREMLNK 3681
Cdd:pfam10174 523 --EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPeINDrirllEQEVARY--KEESGKAQAEVERLLGILREVENEKNDK 598
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3682 QKEMQELEKKRLEQEKvlaEENKKLRdQLQQLEEAQKEKNTQVISAATVETTKNVYNGQ 3740
Cdd:pfam10174 599 DKKIAELESLTLRQMK---EQNKKVA-NIKHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5246-5274 |
5.91e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.86 E-value: 5.91e-07
10 20
....*....|....*....|....*....
gi 1838104091 5246 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 5274
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
1147-1257 |
6.41e-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: 51.92 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1147 ERDRVQKKTFTKWVNKHLIkraesQHHVTDLYEDLRDGHNLISLLEVL-------SGDTLPREKGRMRFHKLQNVQIALD 1219
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-----NPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVE 92
|
90 100 110
....*....|....*....|....*....|....*....
gi 1838104091 1220 FLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1257
Cdd:cd21331 93 LGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3244-3520 |
7.49e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.53 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3244 QEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQ--TLKQKF-QVEQELTKVKLKLDDTDKQKDLLDDE 3320
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEaqELREKRdELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3321 LQRLKDEVDDAVKQRGQVEeelfKVKVQMEELLK----VKLKIEKENQLlIKKDKDKAQQLlaEEAENMKRLAKEAAILS 3396
Cdd:COG1340 94 LDELRKELAELNKAGGSID----KLRKEIERLEWrqqtEVLSPEEEKEL-VEKIKELEKEL--EKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3397 VESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLdeetEEY 3476
Cdd:COG1340 167 AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL----REL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1838104091 3477 QKSLEAERKRQLEIVAEAEKlklqvsqlSVAQAKAEEEAKRFKK 3520
Cdd:COG1340 243 RKELKKLRKKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
3256-3627 |
9.82e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 55.68 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3256 FEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQEL------TKVKLKLDDTDKQKDLLDDELQRLKDEVD 3329
Cdd:PLN02939 31 LAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLentslrTVMELPQKSTSSDDDHNRASMQRDEAIAA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3330 DAVKQRGQVEEELFKVKVQMEELLKVKLKIEKeNQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIA 3409
Cdd:PLN02939 111 IDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEK-NILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3410 EEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDE--ETEEYQKSLEAERK-- 3485
Cdd:PLN02939 190 AQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEvaETEERVFKLEKERSll 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3486 ----RQLE---IVAEAEKLKLQVSQLSVAQAKAEEEA---KRFKKQADNiAARLLETEIATKDKSTVMQQlEVERRNNSK 3555
Cdd:PLN02939 270 daslRELEskfIVAQEDVSKLSPLQYDCWWEKVENLQdllDRATNQVEK-AALVLDQNQDLRDKVDKLEA-SLKEANVSK 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3556 EADDLrnaianLETEKARLKKDAEELQNKSKEMadaqmkqieHEKTMLQQTFLTEKEMLLKKerLIEDEKKR 3627
Cdd:PLN02939 348 FSSYK------VELLQQKLKLLEERLQASDHEI---------HSYIQLYQESIKEFQDTLSK--LKEESKKR 402
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3220-3496 |
1.10e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.51 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3220 RKQAEEAESQKAAAEKEAAIQAKAQE--------DAERLRKEAEFEAAKRAQAENAALEQKKkadaeMAKHKKLAEQTLK 3291
Cdd:pfam17380 315 RRKLEEAEKARQAEMDRQAAIYAEQErmamererELERIRQEERKRELERIRQEEIAMEISR-----MRELERLQMERQQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3292 QKFQVEQELTKV-KLKLDDTDKQKDLLDD--ELQRLKDEVDDAVKQRGQVEEElfKVKVQMEELLKVKLKIEKENQLLIK 3368
Cdd:pfam17380 390 KNERVRQELEAArKVKILEEERQRKIQQQkvEMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQQQVERLRQ 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3369 KDKDKAQQLLAEEAENMKR-LAKEAAILSVESQEASRLRQIAEEDlvQQRALAEKMLKEKMQAI-QEASRLKAEAEllqr 3446
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRkRAEEQRRKILEKELEERKQAMIEEE--RKRKLLEKEMEERQKAIyEEERRREAEEE---- 541
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3447 qkdlaqEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQ-LEIVAEAEK 3496
Cdd:pfam17380 542 ------RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREmMRQIVESEK 586
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2235-2999 |
1.16e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.61 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2235 EVHTVPSDAKEVESYRAKLKKMRAEAEGEQPVFDSLEEELQkaTTVSEKMSRVHSERD---IELDHFRQNVSGLQDRWKA 2311
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ--ETSAELNQLLRTLDDqwkEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2312 VFTQMEI---RHRELEQLGrqLGYYHESYDWLIHWITDAKERQEKIQAvsITDSKTLKEQLSQEKKLLEEIENNKENVDE 2388
Cdd:pfam12128 320 DRSELEAledQHGAFLDAD--IETAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2389 CQKYAKAYinsiKDYELQLVAYNAKADPHASPLKkNKMDSASDNIIQEYVTLRTRYSELMTLTSQyikfITETQRRLED- 2467
Cdd:pfam12128 396 KDKLAKIR----EARDRQLAVAEDDLQALESELR-EQLEAGKLEFNEEEYRLKSRLGELKLRLNQ----ATATPELLLQl 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2468 EEKAAKILKAEEQ-----KKMADLQAELDKQKKL----AEAHAKAIAKAEKEADELKHQMKQEVSK--------REVAAL 2530
Cdd:pfam12128 467 ENFDERIERAREEqeaanAEVERLQSELRQARKRrdqaSEALRQASRRLEERQSALDELELQLFPQagtllhflRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2531 DAENQKKNIELELHELKKL----SEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQkstAETELKQLREKAAEA 2606
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLdpevWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDK---AEEALQSAREKQAAA 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2607 ERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDlenLKMQAEEAERKVKQAQIEKEKQIQi 2686
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE---RKDSANERLNSLEAQLKQLDKKHQ- 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2687 ahvaaeksatAELQSTQRSFVEKTSKLEESLKQEHGTvlqlqqeaahlKKQQEDALKAREEAEKELDKWRQKAnealrlr 2766
Cdd:pfam12128 700 ----------AWLEEQKEQKREARTEKQAYWQVVEGA-----------LDAQLALLKAAIAARRSGAKAELKA------- 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2767 lqAEEEAHkkslaqeeaekqkeeaeREAKKRAKAEESALKqkemaekeLERQRKVADSTAQQKLTAEQELirlrAEFDNA 2846
Cdd:pfam12128 752 --LETWYK-----------------RDLASLGVDPDVIAK--------LKREIRTLERKIERIAVRRQEV----LRYFDW 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2847 EQQRSLLEDElyRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQlksRAEKETMSNtEKSKMLLDAEASKMRDVAEEAGK 2926
Cdd:pfam12128 801 YQETWLQRRP--RLATQLSNIERAISELQQQLARLIADTKLRRA---KLEMERKAS-EKQQVRLSENLRGLRCEMSKLAT 874
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 2927 LRAIAEEAKYQRQIAEEEAARQRaeaeriLKEKLAAISEATRLKTE---AEIALKEKEAENERLRRAAEDEAYQRK 2999
Cdd:pfam12128 875 LKEDANSEQAQGSIGERLAQLED------LKLKRDYLSESVKKYVEhfkNVIADHSGSGLAETWESLREEDHYQND 944
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2792-3000 |
1.18e-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: 54.38 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2792 REAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELyrlkNEVIAAQQQR 2871
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL----AELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2872 KQledelakmRSEMEILiqLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQ-----IAEEEAA 2946
Cdd:COG4942 117 GR--------QPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAelealLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 2947 RQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN--ERLRRAAEDEAYQRKA 3000
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEEleALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2632-3170 |
1.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2632 RTAEEELKRKSEAEKEA--AKQKQKALEDLENLKMQAEEAERKVKQAQIEKEK-QIQIAHVAAE--KSATAELQSTQRSF 2706
Cdd:COG4913 228 DALVEHFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLEllEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2707 VEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAR-EEAEKELDKWRQKANEALRL--RLQAEEEAHKKSLaqeea 2783
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERERRRARLEALlaALGLPLPASAEEF----- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2784 ekqkeeaeREAKKRAKAeesalkQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELyrlkne 2863
Cdd:COG4913 383 --------AALRAEAAA------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL------ 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2864 viaaQQQRKQLEDELAKMRSEMEI---LIQLKSRAEK-----ETMSNTEKSKMLLDAE--ASKMRDVAEEAGKLRAIAEE 2933
Cdd:COG4913 443 ----LALRDALAEALGLDEAELPFvgeLIEVRPEEERwrgaiERVLGGFALTLLVPPEhyAAALRWVNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2934 AKYQRQIAEEEAARQRAEAERI----------LKEKLAAISEATRLKTEAEI-----------------ALKEKE----- 2981
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCVDSPEELrrhpraitragqvkgngTRHEKDdrrri 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2982 -------AENERLRRAAEDEayqRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQK-AMVDDTLKQRRVVEEEIRILKL 3053
Cdd:COG4913 599 rsryvlgFDNRAKLAALEAE---LAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3054 NFEKASSGKLDLElelnKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAG-RQRKIAQDEL 3132
Cdd:COG4913 676 ELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALL 751
|
570 580 590
....*....|....*....|....*....|....*...
gi 1838104091 3133 DRLKKKAEEARKQKDKADSeAEKQIVAASQAALKCRTA 3170
Cdd:COG4913 752 EERFAAALGDAVERELREN-LEERIDALRARLNRAEEE 788
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2476-3027 |
1.46e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2476 KAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEK--EADELKHQMKQ-EVSKREVAALDAENQKKNIELELHELKKLSE- 2551
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELEskEEQLSSYEDKLfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGa 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2552 --------QQINDKSQ----LVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEK 2619
Cdd:TIGR00606 662 tavysqfiTQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2620 LHKQVIEETQKKRTAEEELKRKSE-------------AEKEAAKQKQKALEDLENLKMQAEEAERKVKQAqiekekqiqi 2686
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNdieeqetllgtimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQ---------- 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2687 ahvaaeksaTAELQStqrsfvektSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLR 2766
Cdd:TIGR00606 812 ---------AAKLQG---------SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2767 LQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNA 2846
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2847 EQQRSLLEDELYRLKNEviaaqqQRKQLEDELAKMRSEMEILIQLKSRAEKETmsntekSKMLLDAEASKMRD-VAEEAG 2925
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDD------YLKQKETELNTVNAQLEECEKHQEKINEDM------RLMRQDIDTQKIQErWLQDNL 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2926 KLRAIAEEAKyqrqiaeeeaarqraEAERILKEKLAAISEATRLKTEAEialKEKEAENERLRRAAEDEAY-QRKALEDE 3004
Cdd:TIGR00606 1022 TLRKRENELK---------------EVEEELKQHLKEMGQMQVLQMKQE---HQKLEENIDLIKRNHVLALgRQKGYEKE 1083
|
570 580
....*....|....*....|...
gi 1838104091 3005 ANQHKKEIEEKIVQLKKSSQAEM 3027
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEKYREM 1106
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4831-4864 |
1.47e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.86 E-value: 1.47e-06
10 20 30
....*....|....*....|....*....|....
gi 1838104091 4831 LLEAQAATGFIVDPVNNETLTVDEAVRKGVVGPE 4864
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2853-3500 |
1.54e-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: 55.12 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2853 LEDELYRLKNEVIAAQQQRKQLEDElakMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEE-AGKLRAIA 2931
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQLEALKSE---SQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSiQSQLEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2932 EEAK-----YQRQIAEEEAA-----RQRAEAERILKEKLA--------AISEATRLKTEAEIALKEKEAENERLRRAAED 2993
Cdd:pfam15921 306 EQARnqnsmYMRQLSDLESTvsqlrSELREAKRMYEDKIEelekqlvlANSELTEARTERDQFSQESGNLDDQLQKLLAD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2994 EAYQRKALEDEANQHKK---------------------------EIEEKIVQLKKSSQAEMQRQKAMVDDTLKqrrvvee 3046
Cdd:pfam15921 386 LHKREKELSLEKEQNKRlwdrdtgnsitidhlrrelddrnmevqRLEALLKAMKSECQGQMERQMAAIQGKNE------- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3047 eirilklNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEaekqrklameeekrrreaEETVKKITAAEKEAGRQRK 3126
Cdd:pfam15921 459 -------SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS------------------ERTVSDLTASLQEKERAIE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3127 IAQDELDRLKKKAEEARKQKDKADSEAEK-QIVAASQAALKCRTAEQ-QVQSVLAQQKEDsmMHKKLQQEyekakklake 3204
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGDHlRNVQTECEALKLQMAEKdKVIEILRQQIEN--MTQLVGQH---------- 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3205 aeaakeKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAerlrKEAEFEAakraqaenaaleqkKKADAEMAKHKK 3284
Cdd:pfam15921 582 ------GRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA----KIRELEA--------------RVSDLELEKVKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3285 LAEQTlkqkfqveQELTKVKlkldDTDKQKDLLDDELQRLKDEVDdAVKQRGQVEEELFKVKVQMEELLKVKLKIE-KEN 3363
Cdd:pfam15921 638 VNAGS--------ERLRAVK----DIKQERDQLLNEVKTSRNELN-SLSEDYEVLKRNFRNKSEEMETTTNKLKMQlKSA 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3364 QLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLR---QIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAE 3440
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQskiQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3441 AELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVaeaeKLKLQ 3500
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV----RLKLQ 840
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2730-3164 |
1.59e-06 |
|
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: 55.02 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2730 EAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQK- 2808
Cdd:NF033838 56 QKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTl 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2809 EMAEKELERQRKVADstAQQKLTAEQElirlraefdnaEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKmrsemeil 2888
Cdd:NF033838 136 EPGKKVAEATKKVEE--AEKKAKDQKE-----------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVK-------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2889 iqlksrAEKETMSNTEKSKmllDAEAsKMRDVAEEAGKLraiaEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATR 2968
Cdd:NF033838 195 ------EEAKEPRDEEKIK---QAKA-KVESKKAEATRL----EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2969 LKteaeialkekeaenERLRRAAEDEAYQRKALEDEANQHKKEIEEKIV---QLKKSSQ-AEMQRQKAMVDDTLKQRRvv 3044
Cdd:NF033838 261 PK--------------RRAKRGVLGEPATPDKKENDAKSSDSSVGEETLpspSLKPEKKvAEAEKKVEEAKKKAKDQK-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3045 EEEIRILKLNFEKASS---GKLDLELELNKLKNIAEETQQSKlraEEEAEKQRKlameeekrrreaeetvKKITAAEKEA 3121
Cdd:NF033838 325 EEDRRNYPTNTYKTLEleiAESDVKVKEAELELVKEEAKEPR---NEEKIKQAK----------------AKVESKKAEA 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1838104091 3122 GRQRKIAQDeldrlKKKAEEARKQKDKADSEAEKQIVAASQAA 3164
Cdd:NF033838 386 TRLEKIKTD-----RKKAEEEAKRKAAEEDKVKEKPAEQPQPA 423
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2727-3302 |
1.64e-06 |
|
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: 54.65 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2727 LQQEAAHLKKQQEDALKAREEAEKELDKWRqKANEALRLRL---QAEEEAHKKSLaqeeaeKQKEEAEREAKKRAKAEES 2803
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLeraQTEEAQAKQDS------ELAKLRVEEMEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2804 ALKQKEMaekELERQRKVAdstaqqkltAEQELIRLRAEFDNAEQQRSLLEDE----LYRLKNEVIAAQQQRKQLED--- 2876
Cdd:pfam05701 120 VAAKAQL---EVAKARHAA---------AVAELKSVKEELESLRKEYASLVSErdiaIKRAEEAVSASKEIEKTVEElti 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2877 ELAKMRSEMEIliqlkSRAEKetmsntekskmlLDAEASKMRDV-AEEAGKLRaiaeeakYQRQI--AEEEAARQRAE-- 2951
Cdd:pfam05701 188 ELIATKESLES-----AHAAH------------LEAEEHRIGAAlAREQDKLN-------WEKELkqAEEELQRLNQQll 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2952 AERILKEKLAAISEA-TRLKTE----AEIALKEKEAENERLRRAAEDE----AYQRKALED-EANQHKKEIEEKIVQLKK 3021
Cdd:pfam05701 244 SAKDLKSKLETASALlLDLKAElaayMESKLKEEADGEGNEKKTSTSIqaalASAKKELEEvKANIEKAKDEVNCLRVAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3022 SS-QAEMQRQKAMVdDTLKQRRvveeeirilklnfEKASSGKLDLELELNKLKniaEETQQSKLRAEEEAEKQRKLAmee 3100
Cdd:pfam05701 324 ASlRSELEKEKAEL-ASLRQRE-------------GMASIAVSSLEAELNRTK---SEIALVQAKEKEAREKMVELP--- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3101 ekrrreaeetvKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADS------EAEKQIVAASQA---ALKCRTA- 3170
Cdd:pfam05701 384 -----------KQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTvesrleAVLKEIEAAKASeklALAAIKAl 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3171 EQQVQSVLAQQKEDSMMHKKLQ-QEYEKakklakeaeaakekaekeavlLRKQAEEAESQKAAAEKEAAIQAKAQEDAE- 3248
Cdd:pfam05701 453 QESESSAESTNQEDSPRGVTLSlEEYYE---------------------LSKRAHEAEELANKRVAEAVSQIEEAKESEl 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3249 ----RLrKEAEFEAAKRAQAENAALEQkkkadAEMAKHKKLAeqtlkqkfqVEQELTK 3302
Cdd:pfam05701 512 rsleKL-EEVNREMEERKEALKIALEK-----AEKAKEGKLA---------AEQELRK 554
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
1118-1262 |
1.81e-06 |
|
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: 50.74 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1118 GSPGASSDEEWDHSLDEPEektwphfiederdrvqKKTFTKWVNKHLIKRAESQHHV------TDLYEDLRDGHNLISLL 1191
Cdd:cd21292 7 GGTSEASSEGTTHSYSEEE----------------KVAFVNWINKNLGDDPDCKHLLpmdpntDDLFEKVKDGILLCKMI 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 1192 EVLSGDTLPR----EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 1262
Cdd:cd21292 71 NLSVPDTIDErainKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
|
|
| PspC_relate_1 |
NF033840 |
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ... |
365-682 |
1.84e-06 |
|
PspC-related protein choline-binding protein 1; Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
Pssm-ID: 411409 [Multi-domain] Cd Length: 648 Bit Score: 54.70 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 365 TMVHAKNTTSVLTETAPPF---ITTPANKDVKEKKTNNVFVEPAKPADVEATPEKASDDKKAQVVITTSAAQETSELTPV 441
Cdd:NF033840 37 SFVHAASTIRYIKDDTRPVgsnVLTESDGEDGIKKITTTYDLNEKTGEVTVKENTTTIEKKAQDIIYKVAAQDKIQEKTI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 442 NIDVKKEKPKGEKVDKEPIKptevtpvgciIDQEKAKITAKVT--VTQETTKPPPDSTASEPVLSTDAVKEISKVKVVQE 519
Cdd:NF033840 117 NHKTRFEKDENKERSENPVT----------IDGEDGKVVTTTTydVSPETGTVTENVTIEKKEPTDTVIKVPAKSKVERE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 520 PIDTKVTK--TDESHQQTT-IVTNSIHEVKTTITTTHLFETTassqattplkgNATVTEMITTEKHtavKETPQVKKdvt 596
Cdd:NF033840 187 VLPTSVIRfeKDETKDRSEnPETIDGEDGYVTTTRTYDVDTE-----------TGEVTEKVTTDRT---EPTDTVIK--- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 597 fvaeevlqVSCSPQLSQNVAPMQVAietqqavegsskskrkkkksPGEKSKSFDAEELPESKGGKEKTAKNT----LKPE 672
Cdd:NF033840 250 --------VPAKSKVERRVLPTSVI--------------------RFEKDETKDRSENPVTIDGEDGYVTTTrtydVNPE 301
|
330
....*....|
gi 1838104091 673 TVMTSETLTV 682
Cdd:NF033840 302 TGKVTEKVTV 311
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2711-3035 |
1.87e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.13 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2711 SKLEESLkQEHGTVLQLQQEAahlkkqQEDALKAREEAEKELDKWRQKANEaLRLRLQAEEEAHKKSLAQEEAEKQKEEA 2790
Cdd:pfam07888 34 NRLEECL-QERAELLQAQEAA------NRQREKEKERYKRDREQWERQRRE-LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2791 EREAKKRAKAEESAL-KQKEMAE---KELERQRKvadSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIA 2866
Cdd:pfam07888 106 LSASSEELSEEKDALlAQRAAHEariRELEEDIK---TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2867 AQQQRKQLEDELAKMRSEME----ILIQLKSRAEKETMSNTEKSKMLLDAEASK--MRDVAEEAGKLRAIAEEAKyqRQI 2940
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2941 AEEEAARQRAEAEriLKEKLAAISEATRLKTEAEIALKEkeaenERLRRAAEDEAYQRKALEDEanQHKKEIEEKIVQLK 3020
Cdd:pfam07888 261 SSMAAQRDRTQAE--LHQARLQAAQLTLQLADASLALRE-----GRARWAQERETLQQSAEADK--DRIEKLSAELQRLE 331
|
330
....*....|....*.
gi 1838104091 3021 KSSQAE-MQRQKAMVD 3035
Cdd:pfam07888 332 ERLQEErMEREKLEVE 347
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2581-2776 |
1.90e-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: 54.00 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2581 QLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKA-LEDL 2659
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2660 ENLKMQAEEAERKVKQAQIEKE-KQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQ 2738
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838104091 2739 EDALKAREEAEKELDKWRQKANEALRL--RLQAEEEAHKK 2776
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2595-2958 |
1.95e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAAEAERLRKLAQEEAEKlhkQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKaledlENLKMQAEEAERKVK 2674
Cdd:pfam13868 7 ELRELNSKLLAAKCNKERDAQIAEK---KRIKAEEKEEERRLDEMMEEERERALEEEEEK-----EEERKEERKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2675 QAQI-EKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQehgtVLQLQQEAAHLKKQQEDALKAREEAEKELD 2753
Cdd:pfam13868 79 EEQIeEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK----QRQLREEIDEFNEEQAEWKELEKEEEREED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2754 kwrQKANEALRLRLQAEEEahkkslaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQ-QKLTA 2832
Cdd:pfam13868 155 ---ERILEYLKEKAEREEE-------------------REAEREEIEEEKEREIARLRAQQEKAQDEKAERDELrAKLYQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2833 EQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMeILIQLKSRAEKETMSNTEKSKMLLDA 2912
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFER-MLRKQAEDEEIEQEEAEKRRMKRLEH 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2913 EASKMRDVAE-EAGKLRAIAEEAKYQRQIAEEEAARQR---AEAERILKE 2958
Cdd:pfam13868 292 RRELEKQIEErEEQRAAEREEELEEGERLREEEAERRErieEERQKKLKE 341
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3463-3725 |
2.06e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3463 ELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLsVAQAKAE-EEAKRFKKQADNIAARlleteiatkdkst 3541
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDEL-NAQVKELrEEAQELREKRDELNEK------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3542 vMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQ------IEHEKTMLQQtfLTEKEMLL 3615
Cdd:COG1340 73 -VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQqtevlsPEEEKELVEK--IKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3616 KKERLIEDEKKrlesQYEEEAKKAKALTDEQERQRKLMEE---EKKKLHATMDEALSK----QKEAE---REMLNKQKEM 3685
Cdd:COG1340 150 EKAKKALEKNE----KLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIELYKEadelRKEADelhKEIVEAQEKA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1838104091 3686 QELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVI 3725
Cdd:COG1340 226 DELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEEL 265
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2460-2680 |
2.12e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.70 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2460 ETQRRLEDEEKAAKILKAEEQKKMADL--QAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEvskrEVAALDAENQKK 2537
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2538 NIElelhELKKLSEQQINDKSQLVddalqsrtkieeeihiiriqlettlNQKSTAETELKQLREKAAEAERLRKLAQEEA 2617
Cdd:TIGR02794 144 AKE----EAAKQAEEEAKAKAAAE-------------------------AKKKAEEAKKKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 2618 EKlhkqviEETQKKRTAEEELKRKSEAEKEAAKQ---KQKALEDLENLKMQAEEAERKVKQAQIEK 2680
Cdd:TIGR02794 195 KA------KAEAAKAKAAAEAAAKAEAEAAAAAAaeaERKADEAELGDIFGLASGSNAEKQGGARG 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2589-2751 |
2.29e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2589 KSTAETELKQLREKA--------AEAERLRKL----AQEEAEKLHKQVIEETQKKRT-----------AEEELKRKSEA- 2644
Cdd:PRK12704 26 KKIAEAKIKEAEEEAkrileeakKEAEAIKKEalleAKEEIHKLRNEFEKELRERRNelqklekrllqKEENLDRKLELl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2645 ---EKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKqiqIAHVAAEksataelqstqrsfvEKTSKLEESLKQEh 2721
Cdd:PRK12704 106 ekrEEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER---ISGLTAE---------------EAKEILLEKVEEE- 166
|
170 180 190
....*....|....*....|....*....|
gi 1838104091 2722 gtvlqLQQEAAHLKKQQEDalKAREEAEKE 2751
Cdd:PRK12704 167 -----ARHEAAVLIKEIEE--EAKEEADKK 189
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
3266-3717 |
2.52e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 53.96 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3266 NAALEQK----KKADAEMAKHKKLAEQTLKQKFQVEQELTKVKlklddtdkqkdllDDELQRLKDEVDDAVKQRGQVEEE 3341
Cdd:pfam03528 3 DEDLQQRvaelEKENAEFYRLKQQLEAEFNQKRAKFKELYLAK-------------EEDLKRQNAVLQEAQVELDALQNQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3342 LFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEaailsVESQEASRLRQiAEEDLVQQRALAE 3421
Cdd:pfam03528 70 LALARAEMENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVRE-----YEVQFHRRLEQ-ERAQWNQYRESAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3422 KMLKEKMQAIQEASrlkaEAELLQRQKDLAQEQAQRLLEDKELMQKRLDE------ETEEYQKSLEAERKRQLEIVAEAE 3495
Cdd:pfam03528 144 REIADLRRRLSEGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3496 KlklqvsqlsvaqakaeeeakrfkkqadniAARlleteiatkdkstvmqqleverrnnskeaDDLRNAIANLETEKARLK 3575
Cdd:pfam03528 220 K-----------------------------SCR-----------------------------TDLEMYVAVLNTQKSVLQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3576 KDAEELQNKSKEMADaQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESqyeeeakkakALTDEQERQrklMEE 3655
Cdd:pfam03528 242 EDAEKLRKELHEVCH-LLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMES----------VLTSEQLRQ---VEE 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3656 EKKKlhatmDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQ 3717
Cdd:pfam03528 308 IKKK-----DQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAH 364
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3242-3586 |
2.53e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDEL 3321
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3322 QRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLikkdKDKAQQLLAEEAENMKRLAKEAAILSVESQE 3401
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL----EAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3402 ASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLE 3481
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3482 AERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLR 3561
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|....*
gi 1838104091 3562 NAIANLETEKARLKKDAEELQNKSK 3586
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGL 350
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2595-2981 |
2.64e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.75 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAAEAERLRKLAQEEAEKlhKQVIEETQKKRTAEEELKRKseaEKEAAKQKQKALEDLENLKMQAEEAERKVK 2674
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAAN--RQREKEKERYKRDREQWERQ---RRELESRVAELKEELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2675 QAQIEKEKqiqiahVAAEKSAtaeLQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKEldk 2754
Cdd:pfam07888 105 ELSASSEE------LSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2755 wrqkaNEALRLRLQAEEEaHKKSLAQEEAEKQKEEAEREAK-KRAKAEESALKQKEMAEkelerQRKVADSTAqqkltAE 2833
Cdd:pfam07888 173 -----RKQLQAKLQQTEE-ELRSLSKEFQELRNSLAQRDTQvLQLQDTITTLTQKLTTA-----HRKEAENEA-----LL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2834 QELIRLRAEFDNAEQQRSLLEDELyrlknEVIAAQQQRKQLEDELAKMRS-EMEILIQLKSRAEKETMSN--TEKSKMLL 2910
Cdd:pfam07888 237 EELRSLQERLNASERKVEGLGEEL-----SSMAAQRDRTQAELHQARLQAaQLTLQLADASLALREGRARwaQERETLQQ 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 2911 DAEASKMR--DVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEKE 2981
Cdd:pfam07888 312 SAEADKDRieKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSE---SRRELQELKASLRVAQKEKE 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2908-3155 |
2.67e-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: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2908 MLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEeAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERL 2987
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2988 RRaaedeayQRKALEDEANQHKKEIEEKIVQLKKSSQ-------------AEMQRQKAMVDDTLKQRRvveEEIRILKLN 3054
Cdd:COG4942 89 EK-------EIAELRAELEAQKEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKYLAPARR---EQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3055 FEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAmeeekrrREAEETVKKITAAEKEAGRQRKIAQDELDR 3134
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|.
gi 1838104091 3135 LKKKAEEARKQKDKADSEAEK 3155
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3377-3599 |
2.84e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3377 LLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDlvQQRALAEKMLKEKMQAIQEASRL--KAEAELLQRQKDLAQEQ 3454
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALK--KEEKALLKQLAALERRIAALARRirALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3455 AQRlledkELMQKRLDEETEEYqksleAERKRQLEIVAEAEKLKLQVSQLSVAQAKA------------EEEAKRFKKQA 3522
Cdd:COG4942 90 KEI-----AELRAELEAQKEEL-----AELLRALYRLGRQPPLALLLSPEDFLDAVRrlqylkylaparREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 3523 DNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMaDAQMKQIEHE 3599
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-EALIARLEAE 235
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2478-2872 |
2.98e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2478 EEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADElkhQMKQEvskrevaaldaenQKKNIELELHELKKLSEQQINDK 2557
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDE---MMEEE-------------RERALEEEEEKEEERKEERKRYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2558 SQLVDdalqsrtkieeeihiiriQLETTLNQKSTAETElkQLREKAAEAERLRKLAQEEAEKLhkqviEETQKKRTAEEE 2637
Cdd:pfam13868 76 QELEE------------------QIEEREQKRQEEYEE--KLQEREQMDEIVERIQEEDQAEA-----EEKLEKQRQLRE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2638 LKRKSEAEKEAAKQKQKALEDLENLK-------MQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQrsfvekt 2710
Cdd:pfam13868 131 EIDEFNEEQAEWKELEKEEEREEDERileylkeKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2711 skleESLKQEHgtvLQLQQEAAHLKKQQEDALKaREEAEKELDKWRQKANEALRLRLQAEEEAHKkslaqeeaekqkeea 2790
Cdd:pfam13868 204 ----DELRAKL---YQEEQERKERQKEREEAEK-KARQRQELQQAREEQIELKERRLAEEAEREE--------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2791 erEAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRlkNEVIAAQQQ 2870
Cdd:pfam13868 261 --EEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAER--RERIEEERQ 336
|
..
gi 1838104091 2871 RK 2872
Cdd:pfam13868 337 KK 338
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2563-2995 |
3.56e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 53.37 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2563 DALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKS 2642
Cdd:COG5278 93 AELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2643 EAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHG 2722
Cdd:COG5278 173 AALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2723 TVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEE 2802
Cdd:COG5278 253 LLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2803 SALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDElyRLKNEVIAAQQQRKQLEDELAKMR 2882
Cdd:COG5278 333 LATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE--AVELEVLAIAAAAAAAAAEAAAAA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2883 SEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAA 2962
Cdd:COG5278 411 AAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAA 490
|
410 420 430
....*....|....*....|....*....|...
gi 1838104091 2963 ISEATRLKTEAEIALKEKEAENERLRRAAEDEA 2995
Cdd:COG5278 491 AALAAAAALSLALALAALLLAAAEAALAAALAA 523
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2793-3049 |
3.59e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2793 EAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRaefdnaeQQRSLLEDELYRLKNEVIAAQQQRK 2872
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK-------ELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2873 QLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSkmlldAEASKMRDVAEEAgklRAIAEEAKYQRqiaeEEAARQRAEA 2952
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ-----AEEEAKAKAAAEA---KKKAEEAKKKA----EAEAKAKAEA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2953 ERILK-EKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQK 3031
Cdd:TIGR02794 186 EAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYA 265
|
250
....*....|....*...
gi 1838104091 3032 AMVDDTLKQRRVVEEEIR 3049
Cdd:TIGR02794 266 AIIQQAIQQNLYDDPSFR 283
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3453-3656 |
3.88e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3453 EQAQRLLE----DKELMQ-----KRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQAD 3523
Cdd:COG1579 4 EDLRALLDlqelDSELDRlehrlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3524 NIaarlleteiatkdkstvmqqleverrNNSKEADDLRNAIANLETEKARLKKDAEELqnkskemadaqMKQIEHEKTML 3603
Cdd:COG1579 84 NV--------------------------RNNKEYEALQKEIESLKRRISDLEDEILEL-----------MERIEELEEEL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3604 QQTflteKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEE 3656
Cdd:COG1579 127 AEL----EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2244-2767 |
4.06e-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: 53.58 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2244 KEVESYRAKLKKMRAEAEGEQPVFDSLEEELQKATTVS-EKMSRVHSERdielDHFRQNVSGLQDRWKAVFTQMEIRHRE 2322
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAnSELTEARTER----DQFSQESGNLDDQLQKLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2323 L----EQLGRQLGYYHESYDWLIHWITDAKERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNKENVDECQKYAkAYIN 2398
Cdd:pfam15921 393 LslekEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT-AQLE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2399 SIKDYELQLV-AYNAK-----------ADPHASPLKKNKMDSASDniiQEYVTLRTRYsELMTLTSQYIKFITETQRRLE 2466
Cdd:pfam15921 472 STKEMLRKVVeELTAKkmtlessertvSDLTASLQEKERAIEATN---AEITKLRSRV-DLKLQELQHLKNEGDHLRNVQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2467 DEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEadelKHQMKQEVSKREVAALDAENQKKNIELELHEL 2546
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE----KAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2547 K-KLSEQQInDKSQLVdDALQSRTKIEEEIHIIRIQLettLNQKSTAETELKQLREKAAEAERLRKLAQEEAE----KLH 2621
Cdd:pfam15921 624 EaRVSDLEL-EKVKLV-NAGSERLRAVKDIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2622 KQVIEETQKKRTAEEELKRKSEAEKEAAK-----QKQKALE--DLENLKMQAEEAERKVKQAQIEK-----EKQI---QI 2686
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKvamgmQKQITAKrgQIDALQSKIQFLEEAMTNANKEKhflkeEKNKlsqEL 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2687 AHVAAEKSATAE----LQSTQRSFVEKTSKLEESLKQehgTVLQLQQEAAHLKKQQEDALKAREEAE---KELDKWRQKA 2759
Cdd:pfam15921 779 STVATEKNKMAGelevLRSQERRLKEKVANMEVALDK---ASLQFAECQDIIQRQEQESVRLKLQHTldvKELQGPGYTS 855
|
....*...
gi 1838104091 2760 NEALRLRL 2767
Cdd:pfam15921 856 NSSMKPRL 863
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2477-2660 |
4.17e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2477 AEEQKKMADLQA---ELDKQKKLAEAHAKAIAKAEKEADELKhqmkQEVSKREVAALDAENQKKNIELELHEL----KKL 2549
Cdd:COG1579 3 PEDLRALLDLQEldsELDRLEHRLKELPAELAELEDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEVeariKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2550 SEQQINDKSQLVDDALQSrtkieeeihiiriQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQ 2629
Cdd:COG1579 79 EEQLGNVRNNKEYEALQK-------------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190
....*....|....*....|....*....|.
gi 1838104091 2630 KKRTAEEELKRKseaEKEAAKQKQKALEDLE 2660
Cdd:COG1579 146 ELDEELAELEAE---LEELEAEREELAAKIP 173
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2792-3227 |
4.52e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 53.37 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2792 REAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQR 2871
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2872 KQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAE 2951
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2952 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQK 3031
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3032 AMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETV 3111
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3112 KKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKL 3191
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1838104091 3192 QQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAE 3227
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAAL 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2591-2956 |
4.64e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2591 TAETELKQLREKAAEAERLRKLAQEEAEKLhKQVIEETQKKRTAEEELKRKSEAEKEAAkQKQKALEDLENLKMQAEEAE 2670
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEAL-EAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2671 RKVKQAQIEKEKqiqiahvaaeksATAELQstqrsfvektsKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEK 2750
Cdd:COG4913 685 DDLAALEEQLEE------------LEAELE-----------ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2751 ELDKWRQKANEALRLRLQAEEeahkkslaqeeaekQKEEAEREAKKRAKAEESALKQkemAEKELERQRK---------V 2821
Cdd:COG4913 742 LARLELRALLEERFAAALGDA--------------VERELRENLEERIDALRARLNR---AEEELERAMRafnrewpaeT 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2822 ADSTA--------QQKLT--AEQELIRLRAEFDNAEQQRS--LLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILI 2889
Cdd:COG4913 805 ADLDAdleslpeyLALLDrlEEDGLPEYEERFKELLNENSieFVADLLSKLRRAIREIKERIDPLNDSLKRIPFGPGRYL 884
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 2890 QLKSRAEKetmsntekskmllDAEA----SKMRDVAEEAGKLRAIAEEAKYQR------QIAEEEAARQRAEAERIL 2956
Cdd:COG4913 885 RLEARPRP-------------DPEVrefrQELRAVTSGASLFDEELSEARFAAlkrlieRLRSEEEESDRRWRARVL 948
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2743-3053 |
5.72e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.23 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2743 KAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVA 2822
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2823 DSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYR--LKNEVIAAQQQRKQLEDELAKMRSEMEIliqlksRAEKEtm 2900
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEeeREEDERILEYLKEKAEREEEREAEREEI------EEEKE-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2901 snteKSKMLLDAEASKMRDVAEEAGKLRA--IAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALK 2978
Cdd:pfam13868 184 ----REIARLRAQQEKAQDEKAERDELRAklYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAERE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2979 EKEAENERLRRAAEDEAYQRKALEDEAN--QHKKEIEEKIV---QLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKL 3053
Cdd:pfam13868 260 EEEFERMLRKQAEDEEIEQEEAEKRRMKrlEHRRELEKQIEereEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2462-2697 |
5.84e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.03 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2462 QRRLEDEEKAakilKAEEQKKMAdlqAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKNIEL 2541
Cdd:PRK05035 459 QARLEREKAA----REARHKKAA---EARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQAR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2542 ELHELKKLSEqQINDKSQLVDDALQsRTKieeeihiiriqLETTLNQKSTAETELKQLREKAAEAERL-----RKLAQEE 2616
Cdd:PRK05035 532 ARQAEKQAAA-AADPKKAAVAAAIA-RAK-----------AKKAAQQAANAEAEEEVDPKKAAVAAAIarakaKKAAQQA 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2617 AEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLK--MQAEEAERKVKQAQIEKEKQIQIAHVAAEKS 2694
Cdd:PRK05035 599 ASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKaaVAAAIARAKARKAAQQQANAEPEEAEDPKKA 678
|
...
gi 1838104091 2695 ATA 2697
Cdd:PRK05035 679 AVA 681
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3351-3698 |
6.33e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3351 ELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRlAKEAaiLSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQA 3430
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKR-DREQ--WERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3431 IQEASRLKAEAELLQRQKDLAQEQAQRLLED-KELMQKRLDEETE-----EYQKSLEAERKRQlEIVAEAEKLKLQVSQL 3504
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDiKTLTQRVLERETElermkERAKKAGAQRKEE-EAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3505 SVAQAKAE-EEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQN 3583
Cdd:pfam07888 186 ELRSLSKEfQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3584 K------------------SKEMADAQMKQIE------HEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKA 3639
Cdd:pfam07888 266 QrdrtqaelhqarlqaaqlTLQLADASLALREgrarwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLE 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3640 KALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKV 3698
Cdd:pfam07888 346 VELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2456-2661 |
6.52e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2456 KFITETQRRLEDEEKAakiLKAEEQKKMADLQA--ELDKQKKLAEAHAKAIAKAEKEADElkhqmkqEVSKREVAALDAE 2533
Cdd:PRK09510 95 KQAAEQERLKQLEKER---LAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEA-------EAKRAAAAAKKAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2534 NQKKNIELELHELKKLSEQQindksqlvddalqsrtkieeeihiirIQLETTLNQKSTAETELKQLREKAAEAERLRKlA 2613
Cdd:PRK09510 165 AEAKKKAEAEAAKKAAAEAK--------------------------KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-K 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838104091 2614 QEEAEKLHKQVIEETQKKRTAEEELKRKSeAEKEAAKQKQKALEDLEN 2661
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAKAAAEKAAAAKA-AEKAAAAKAAAEVDDLFG 264
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2618-3072 |
6.68e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2618 EKLHKQVIEETQKK------RTAEEE---LKRKSEAEKE-AAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIA 2687
Cdd:COG3096 255 RDLFKHLITEATNYvaadymRHANERrelSERALELRRElFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2688 HVAAEKSATAELQSTQRsFVEKTSKLEESLKQEHGTVLQLQQeaahlkkQQEDALKAREEAEKELDKWR-QKANealrlR 2766
Cdd:COG3096 335 HLNLVQTALRQQEKIER-YQEDLEELTERLEEQEEVVEEAAE-------QLAEAEARLEAAEEEVDSLKsQLAD-----Y 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2767 LQAEEEAHKkslaqeeaekqkeeaereakkRAKAEESALKQKEMAEKELErqrkVADSTAQQkltAEQELIRLRAEFDNA 2846
Cdd:COG3096 402 QQALDVQQT---------------------RAIQYQQAVQALEKARALCG----LPDLTPEN---AEDYLAAFRAKEQQA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2847 EQQRSLLEDelyRLKNEVIAAQQQRKQLEdELAKMRSEMEiliqlKSRAeketmsntekskmlldaeASKMRDVAEEAGK 2926
Cdd:COG3096 454 TEEVLELEQ---KLSVADAARRQFEKAYE-LVCKIAGEVE-----RSQA------------------WQTARELLRRYRS 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2927 LRAIAE-EAKYQRQIAE-EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEde 3004
Cdd:COG3096 507 QQALAQrLQQLRAQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR-- 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3005 anQHKKEIEEKIVQLKKS------SQAEMQRQKAMVDDTLKQR--------RVVEEEiRILKLNFEKASSGKLDLELELN 3070
Cdd:COG3096 585 --QQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSqevtaamqQLLERE-REATVERDELAARKQALESQIE 661
|
..
gi 1838104091 3071 KL 3072
Cdd:COG3096 662 RL 663
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
3459-3714 |
6.92e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 51.49 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3459 LEDKELMQKR---LDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIaarlleteia 3535
Cdd:pfam09728 17 EEKLAALCKKyaeLLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKL---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3536 tKDKSTVMQQLEVERRNNSKEA-----DDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTE 3610
Cdd:pfam09728 87 -KEESKKLAKEEEEKRKELSEKfqstlKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTKELEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3611 KEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEE------EK-KKLHATMDEALSKQKEAEREMLNKQK 3683
Cdd:pfam09728 166 QLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREqlnlyvEKfEEFQDTLNKSNEVFTTFKKEMEKMSK 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1838104091 3684 EMQELEKKRL-----------------EQEKVLAEENKKLRDQLQQLE 3714
Cdd:pfam09728 246 KIKKLEKENLtwkrkweksnkallemaEERQKLKEELEKLQKKLEKLE 293
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3173-3489 |
7.18e-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: 51.84 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3173 QVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRK 3252
Cdd:pfam13868 19 KCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3253 EAEF--EAAKRAQAENAALEQKK--KADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEV 3328
Cdd:pfam13868 99 EREQmdEIVERIQEEDQAEAEEKleKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3329 DDAVKQRGQ-VEEELFKVKVQMEELLKVKLKIEKENQLliKKDKDKAQQLlAEEAENMKRLAKEAAILSVESQEASRLRQ 3407
Cdd:pfam13868 179 EEEKEREIArLRAQQEKAQDEKAERDELRAKLYQEEQE--RKERQKEREE-AEKKARQRQELQQAREEQIELKERRLAEE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3408 IAEEDLVQQRALAEKML---KEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAER 3484
Cdd:pfam13868 256 AEREEEEFERMLRKQAEdeeIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
....*
gi 1838104091 3485 KRQLE 3489
Cdd:pfam13868 336 QKKLK 340
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2669-2832 |
7.29e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.18 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2669 AERKVKQAQIEKEKQIQIAhVAAEKSATAELQStqrsfvektskleeslKQEHGTVLQLQQEAAHLKKQQE---DALKAR 2745
Cdd:COG2268 199 RDARIAEAEAERETEIAIA-QANREAEEAELEQ----------------EREIETARIAEAEAELAKKKAEerrEAETAR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2746 EEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADST 2825
Cdd:COG2268 262 AEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341
|
....*..
gi 1838104091 2826 AQQKLTA 2832
Cdd:COG2268 342 GKRALAE 348
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2841-3292 |
7.35e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2841 AEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKE---TMSNTEKSKMLLDAeaskM 2917
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMDE----I 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2918 RDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQ 2997
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2998 RKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE 3077
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3078 ETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQI 3157
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3158 VAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEA 3237
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 3238 AIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQ 3292
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3544-3715 |
7.44e-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: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3544 QQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEmADAQMKQIEHEktmlqqtfltekemLLKKERLIED 3623
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELE--------------IEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3624 EKKRLESQyeEEAKKAKALTDE---QERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLA 3700
Cdd:COG1579 78 YEEQLGNV--RNNKEYEALQKEiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*
gi 1838104091 3701 EENKKLRDQLQQLEE 3715
Cdd:COG1579 156 AELEELEAEREELAA 170
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
1152-1263 |
7.58e-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: 49.29 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1152 QKKTFTKWVNKHLIKRAESQH------HVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 1221
Cdd:cd21325 25 EKYAFVNWINKALENDPDCRHvipmnpNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1838104091 1222 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQIN 1263
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2844-3538 |
8.59e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2844 DNAEQQrslLEDELYRLKNEVIAAQQQRKQLEDELAKmrsEMEILIQLKSRAEK-ETMSNTEKSKmlLDAEASKMRDVAE 2922
Cdd:TIGR04523 32 DTEEKQ---LEKKLKTIKNELKNKEKELKNLDKNLNK---DEEKINNSNNKIKIlEQQIKDLNDK--LKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2923 EAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRaaedeayQRKALE 3002
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKK-------QKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3003 DEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNfEKASSGKLDLEL---ELNKLKNIAEET 3079
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK-KQNNQLKDNIEKkqqEINEKTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3080 QQSKLRAEEEAEKQRKlamEEEKRRREAEETVKKITAAEKeagrQRKIAQDELDRLKKKAE--------EARKQKDKADS 3151
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKK---QLSEKQKELEQNNKKIKELEK----QLNQLKSEISDLNNQKEqdwnkelkSELKNQEKKLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3152 EAEKQIvaaSQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKa 3231
Cdd:TIGR04523 325 EIQNQI---SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3232 aaekeaaiqakaqEDAERLRKEAEfEAAKRAQAENAALEQKkkadaemakHKKLAEQTLKQKFQV---EQELTKVKLKLD 3308
Cdd:TIGR04523 401 -------------QNQEKLNQQKD-EQIKKLQQEKELLEKE---------IERLKETIIKNNSEIkdlTNQDSVKELIIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3309 DTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKdkdkaqqlLAEEAENMKRL 3388
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK--------ISSLKEKIEKL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3389 AKEaaILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEasrLKAEAELLQRqkdlAQEQAQRLLEDKELMQKR 3468
Cdd:TIGR04523 530 ESE--KKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKK----KQEEKQELIDQKEKEKKD 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3469 LDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKD 3538
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2472-2772 |
8.65e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2472 AKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEAdelkhqmKQEVSKREVAALDAENQKKNIELELhelKKLSE 2551
Cdd:pfam02029 47 DSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQ-------KEFDPTIADEKESVAERKENNEEEE---NSSWE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2552 QQINDKSQLVDDALQsrtkieeeihiiriqlETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVI-EETQK 2630
Cdd:pfam02029 117 KEEKRDSRLGRYKEE----------------ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFaKEEVK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2631 KRTAEEELKRKSE------AEKEAAKQKQKALEDlENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKsataELQSTQR 2704
Cdd:pfam02029 181 DEKIKKEKKVKYEskvfldQKRGHPEVKSQNGEE-EVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ----KLEELRR 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 2705 SFVEKTSKLEESLKQEhgtvlqlQQEAA----HLKKQQEDALKAREEAE---KELDKWRQKANEALRLRLQAEEE 2772
Cdd:pfam02029 256 RRQEKESEEFEKLRQK-------QQEAEleleELKKKREERRKLLEEEEqrrKQEEAERKLREEEEKRRMKEEIE 323
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
3308-3715 |
8.80e-06 |
|
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: 52.32 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3308 DDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQ------MEELLKVKLKIEKENQLLIKKDKDKAQQLLAEE 3381
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSdikteyLYELNVLKEKSEAELTSKTKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3382 AENMKRLAKEAAILSVESQEASRLRQiaEEDLVQQRALAEKMLKEKMqAIQEASRLKAEAELLQRQKDLAQE-----QAQ 3456
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELEI-AESDVEVKKAELELVKEEAKEPRDeekikQAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3457 RLLEDKELMQKRLDEeteeyqksLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADniaarllETEIAT 3536
Cdd:NF033838 211 AKVESKKAEATRLEK--------IKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGV-------LGEPAT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3537 KDKstvmqqleveRRNNSKEADD------LRNAIANLETEKARLKKDAEELQNKSKEMADAQ--------MKQIEHEKTM 3602
Cdd:NF033838 276 PDK----------KENDAKSSDSsvgeetLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDrrnyptntYKTLELEIAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3603 LQQTfLTEKEMLLKKERLIE--DEKKRLESQYEEEAKKAKALTDEQ-ERQRKLMEEEKKKLHATMDEAlsKQKEAEReml 3679
Cdd:NF033838 346 SDVK-VKEAELELVKEEAKEprNEEKIKQAKAKVESKKAEATRLEKiKTDRKKAEEEAKRKAAEEDKV--KEKPAEQ--- 419
|
410 420 430
....*....|....*....|....*....|....*.
gi 1838104091 3680 nKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEE 3715
Cdd:NF033838 420 -PQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAEE 454
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
3398-3719 |
8.88e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3398 ESQEASR-LRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDkelMQKRldeeTEEY 3476
Cdd:pfam02029 3 DEEEAAReRRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---TAKR----EERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3477 QKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQL-EVERRNNSK 3555
Cdd:pfam02029 76 QKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWsTEVRQAEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3556 EADDLRNAIANLETEKARLKKDAEELQNKSKEMA-DAQMKQIEHEK------------TMLQQTFLTEKEMLLKKERLIE 3622
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvKYESKVFLDQKrghpevksqngeEEVTKLKVTTKRRQGGLSQSQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3623 DEKKRlESQYEEEAKKakaltDEQERQR-KLMEEEKKKLhatmdealsKQKEAEREMlnkqkEMQELEKKRLEQEKVLAE 3701
Cdd:pfam02029 236 REEEA-EVFLEAEQKL-----EELRRRRqEKESEEFEKL---------RQKQQEAEL-----ELEELKKKREERRKLLEE 295
|
330
....*....|....*...
gi 1838104091 3702 ENKKlRDQLQQLEEAQKE 3719
Cdd:pfam02029 296 EEQR-RKQEEAERKLREE 312
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1732-1824 |
9.01e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1732 HAFISASTKELMWLNDKEEEEVNFDWSDKNPNMTAKKDNYSGLMRELELREKKVNDLQAMGERLVRDGHPGKKTVEDFTA 1811
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1838104091 1812 ALQTQWSWILQLC 1824
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3544-3706 |
9.19e-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: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3544 QQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEmADAQMKQIEHEKTMlqQTFLTEKEMLLKKERLIED 3623
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNKEY--EALQKEIESLKRRISDLED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3624 EKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLhatmDEALSKQkeaeremlnkQKEMQELEKKRLEQEKVLAEEN 3703
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAEL----DEELAEL----------EAELEELEAEREELAAKIPPEL 176
|
...
gi 1838104091 3704 KKL 3706
Cdd:COG1579 177 LAL 179
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
1152-1262 |
9.37e-06 |
|
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: 48.85 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1152 QKKTFTKWVNKHLIKRAESQH------HVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 1221
Cdd:cd21324 25 EKYAFVNWINKALENDPDCKHvipmnpNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1838104091 1222 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 1262
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
3556-3674 |
1.01e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 52.39 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3556 EADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKkerlIEDEKKRLESQYEEE 3635
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3636 AKKAKALTDEQERQR----------------------------KLMEEEKKKLhATMDEALSK----QKEA 3674
Cdd:COG0542 488 PELEKELAELEEELAelapllreevteediaevvsrwtgipvgKLLEGEREKL-LNLEEELHErvigQDEA 557
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2419-2928 |
1.05e-05 |
|
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: 52.13 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2419 SPLKKNKMDSASDNIIQ---EYVTLRTRyseLMTLTSQYikfitetqrrlEDEEKAAKILK----AEEQKKmADLQAELD 2491
Cdd:pfam10174 284 SKFMKNKIDQLKQELSKkesELLALQTK---LETLTNQN-----------SDCKQHIEVLKesltAKEQRA-AILQTEVD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2492 KQKKLAEAHAKAIAKAEKEADELK----------HQMKQ--EVSKREVAALdaenQKKnielelheLKKLSEQQINDKSQ 2559
Cdd:pfam10174 349 ALRLRLEEKESFLNKKTKQLQDLTeekstlageiRDLKDmlDVKERKINVL----QKK--------IENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2560 LvdDALQSRTKIeeeihiiriqLETtlnQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELK 2639
Cdd:pfam10174 417 L--AGLKERVKS----------LQT---DSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2640 RKSEAEKEAAKQKQKALEDLENlkMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSAT-AELQSTQRSFVEKTSKLEESLK 2718
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKE--HASSLASSGLKKDSKLKSLEIAVEQKKEECSKLeNQLKKAHNAEEAVRTNPEINDR 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2719 qehgtVLQLQQEAAHLKkqqEDALKAREEAEKELDKWRQKANEalrlrlQAEEEAHKKSLAQEEAEKQKEEAEREAKKRA 2798
Cdd:pfam10174 560 -----IRLLEQEVARYK---EESGKAQAEVERLLGILREVENE------KNDKDKKIAELESLTLRQMKEQNKKVANIKH 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2799 KAEESALKQKEMAEKELERQRKVADSTAQQKLTaeqeliRLRAEFDNAEQqrslledELYRLKNEVIAAQQQRKQLEDEL 2878
Cdd:pfam10174 626 GQQEMKKKGAQLLEEARRREDNLADNSQQLQLE------ELMGALEKTRQ-------ELDATKARLSSTQQSLAEKDGHL 692
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 2879 AKMRSE----MEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLR 2928
Cdd:pfam10174 693 TNLRAErrkqLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2591-2947 |
1.07e-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: 51.46 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2591 TAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEetqkkrtaEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAE 2670
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEE--------EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2671 RKVKQAQIEKEKQIQiahvaAEKSATAELQSTQRsfvektskleESLKQEHGTVLQLQQEAAHLKKQQEDALKAR-EEAE 2749
Cdd:pfam13868 97 LQEREQMDEIVERIQ-----EEDQAEAEEKLEKQ----------RQLREEIDEFNEEQAEWKELEKEEEREEDERiLEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2750 KELDKwRQKANEALRLRLQAEEEAHKKSLAQEEaekqkeeaerEAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQK 2829
Cdd:pfam13868 162 KEKAE-REEEREAEREEIEEEKEREIARLRAQQ----------EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2830 LTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRkqlEDELAKMRSEMEILIQLKSRAEKEtmsnteksKML 2909
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAE---DEEIEQEEAEKRRMKRLEHRRELE--------KQI 299
|
330 340 350
....*....|....*....|....*....|....*...
gi 1838104091 2910 LDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAAR 2947
Cdd:pfam13868 300 EEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5031-5069 |
1.12e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.12e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1838104091 5031 YLVGTSCIAGVLLESSKERLSVYQAMKKNLIRPGTAFEL 5069
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2466-2705 |
1.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2466 EDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQevSKREVAALDAENQKKNIELElhe 2545
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--LQAEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2546 lKKLSEQQIN--------------------DKSQLVDDALQSRTKIEEEIHIIRIQLEttlNQKSTAETELKQLREKAAE 2605
Cdd:COG3883 90 -ERARALYRSggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELE---AKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2606 AERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQ 2685
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260
....*....|....*....|
gi 1838104091 2686 IAHVAAEKSATAELQSTQRS 2705
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGAA 265
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
3411-3677 |
1.20e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3411 EDLVQQRALAE--KMLKEKMQAIQEasrlkaEAELLQRQKDLAQEQA---QRLLEDkelMQKRLDEETEEYQKSLEAERK 3485
Cdd:PHA02562 157 EDLLDISVLSEmdKLNKDKIRELNQ------QIQTLDMKIDHIQQQIktyNKNIEE---QRKKNGENIARKQNKYDELVE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3486 RQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFkkqadNIAARLLETEIATKDK-----------STVMQQLEverrnns 3554
Cdd:PHA02562 228 EAKTIKAEIEELTDELLNLVMDIEDPSAALNKL-----NTAAAKIKSKIEQFQKvikmyekggvcPTCTQQIS------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3555 kEADDLrnaIANLETEKARLKKDAEELQNKSKEMadaqmKQIEHEKTMLQQTFLTEKEMLLKKERLIedekkrleSQYEE 3634
Cdd:PHA02562 296 -EGPDR---ITKIKDKLKELQHSLEKLDTAIDEL-----EEIMDEFNEQSKKLLELKNKISTNKQSL--------ITLVD 358
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1838104091 3635 EAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAERE 3677
Cdd:PHA02562 359 KAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2863-3000 |
1.21e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.41 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2863 EVIAAQQQRKQledELAKMRSEMEILIQLKSRAEKETmsntEKSKMLLDAEASKMRDVAEEAGKLRAI---------AEE 2933
Cdd:COG2268 213 EIAIAQANREA---EEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEI 285
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 2934 AKYQRQI--AEEEAARQRAEAERILKEKLAAisEATRLKTEAeialkEKEAENERLRRAAEDEAYQRKA 3000
Cdd:COG2268 286 AEREREIelQEKEAEREEAELEADVRKPAEA--EKQAAEAEA-----EAEAEAIRAKGLAEAEGKRALA 347
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2867-3092 |
1.21e-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: 51.38 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2867 AQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLL-DAEASKMRDVAEEAGKLRAI----AEEAKYQRqiA 2941
Cdd:TIGR02794 52 ANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEqRAAAEKAAKQAEQAAKQAEEkqkqAEEAKAKQ--A 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2942 EEEAARQRAEAERILKEKLAAISEATRLKTEAEIAlkEKEAENERLRRAAEDEAyqrkaledeanqhKKEIEEKIVQLKK 3021
Cdd:TIGR02794 130 AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKA-------------KAEAEAKAKAEEA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3022 SSQAEMQRQKAMVDDTLKQRRvvEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEK 3092
Cdd:TIGR02794 195 KAKAEAAKAKAAAEAAAKAEA--EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3567-3731 |
1.35e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3567 LETEKARLKKDAE------ELQnkskemadAQMKQIEHEKTMLQ-QTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKA 3639
Cdd:COG1196 198 LERQLEPLERQAEkaeryrELK--------EELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3640 KALTDEQERQRKLMEEEKKKLHATMDEA--LSKQKEAEREML-NKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEA 3716
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELarLEQDIARLEERRrELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170
....*....|....*
gi 1838104091 3717 QKEKNTQVISAATVE 3731
Cdd:COG1196 350 EEELEEAEAELAEAE 364
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
3594-3712 |
1.43e-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: 50.65 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3594 KQIEHEKTMlqQTFLTEKEM-----------LLKKERLIEDEKKRlesqyEEEAKKAKALTDEQERQRKLMEEEKKKLHA 3662
Cdd:cd16269 164 KGVKAEEVL--QEFLQSKEAeaeailqadqaLTEKEKEIEAERAK-----AEAAEQERKLLEEQQRELEQKLEDQERSYE 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3663 TMDEALSKQKEAEREMLNKQKEmQELEKKRLEQEKVLAEENKKLRDQLQQ 3712
Cdd:cd16269 237 EHLRQLKEKMEEERENLLKEQE-RALESKLKEQEALLEEGFKEQAELLQE 285
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2273-2696 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2273 ELQKATTVSEKMSRVHSERDIELDHFRQNVSGLQdrwkavftQMEIRHRELEQLGRQLGYYHESYDWLIHwitdAKERQE 2352
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDE--------KLLDEKKQFEKIAEELKGKEQELIFLLQ----AREKEI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2353 KIQAVSITDSKTLKEQLSQE-KKLLEEIENNK-------ENVDECQKYAKAYINSIKDYELQLvaYNAKADPHASPLKKN 2424
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEvEDLKTELEKEKlknieltAHCDKLLLENKELTQEASDMTLEL--KKHQEDIINCKKQEE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2425 KMDSASDNIIQEYVTLRtrySELMTLTSQYIKFITETQRRLEDEEKAAKILKAE---EQKKMADLQAELDKQKKLAEAHA 2501
Cdd:pfam05483 531 RMLKQIENLEEKEMNLR---DELESVREEFIQKGDEVKCKLDKSEENARSIEYEvlkKEKQMKILENKCNNLKKQIENKN 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2502 KAIAKAEKEADELKHQmkqevSKREVAALDAENQKKN-IELELHELKKLSEQQINDKSQLVDDALQSRTKIeeeihiiri 2580
Cdd:pfam05483 608 KNIEELHQENKALKKK-----GSAENKQLNAYEIKVNkLELELASAKQKFEEIIDNYQKEIEDKKISEEKL--------- 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2581 qLETTLNQKSTAETELKQLREKAAEAErlRKLAQEEA--EKlHKQVIEETQKKRTAEEELKRKSEAEKEAAKqkqKALE- 2657
Cdd:pfam05483 674 -LEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVAlmEK-HKHQYDKIIEERDSELGLYKNKEQEQSSAK---AALEi 746
|
410 420 430
....*....|....*....|....*....|....*....
gi 1838104091 2658 DLENLKMQAEEAErkvKQAQIEKEKQIQIAHVAAEKSAT 2696
Cdd:pfam05483 747 ELSNIKAELLSLK---KQLEIEKEEKEKLKMEAKENTAI 782
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3368-3534 |
1.50e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3368 KKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEA---ELL 3444
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3445 QRQKDLAQEQAQRLLEDKElMQKRLDEEteeyqksLEAERKRQLEIvAEAEKLKLQvSQLSVAQAKAEEEAKRfKKQADN 3524
Cdd:pfam15709 434 ELQRKKQQEEAERAEAEKQ-RQKELEMQ-------LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEE-RRQKEE 502
|
170
....*....|
gi 1838104091 3525 IAARLLETEI 3534
Cdd:pfam15709 503 EAARLALEEA 512
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2904-3153 |
1.55e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 51.68 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2904 EKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKyqrqiaeEEAARQRAEAERiLKEKLAAisEATRLKTEAEIALKEKEAE 2983
Cdd:COG1193 503 ERARELLGEESIDVEKLIEELERERRELEEER-------EEAERLREELEK-LREELEE--KLEELEEEKEEILEKAREE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2984 NERLRRAAEDEAYQ--RKALEDEANQHK-KEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVE-EEIRILKLN----- 3054
Cdd:COG1193 573 AEEILREARKEAEEliRELREAQAEEEElKEARKKLEELKQELEEKLEKPKKKAKPAKPPEELKVgDRVRVLSLGqkgev 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3055 FEKASSGKLDLELELNKLKniaeeTQQSKLRAEEEAEKQRKlameeekrrreaeetvKKITAAEKEAGRQRKIAQDELDR 3134
Cdd:COG1193 653 LEIPKGGEAEVQVGILKMT-----VKLSDLEKVEKKKPKKP----------------KKRPAGVSVSVSKASTVSPELDL 711
|
250
....*....|....*....
gi 1838104091 3135 LKKKAEEARKQKDKADSEA 3153
Cdd:COG1193 712 RGMRVEEALPELDKYLDDA 730
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4498-4531 |
1.62e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.62e-05
10 20 30
....*....|....*....|....*....|....
gi 1838104091 4498 LLEAQAATGFLVDPVRNQFLTVDEAVKSGLVGPE 4531
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2802-3141 |
1.91e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2802 ESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKM 2881
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2882 RSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKyqrQIAEEEAARQRAEAERILKEKLA 2961
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA---ALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2962 AISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQR 3041
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3042 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEA 3121
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1838104091 3122 GRQRKIAQDELDRLKKKAEE 3141
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
3289-3736 |
1.92e-05 |
|
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: 51.36 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3289 TLKQKFQ-VEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDdAVKQRGQV-EEELFKVKVQMEEllKVKLKIEKENQLL 3366
Cdd:pfam10174 293 QLKQELSkKESELLALQTKLETLTNQNSDCKQHIEVLKESLT-AKEQRAAIlQTEVDALRLRLEE--KESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3367 ikkDKDKAQQLLAEEAENMKRL--AKEAAILSVESQEASRLRQIAEEDlvqqRALAEkmLKEKMQAIQEASRlkaeaell 3444
Cdd:pfam10174 370 ---DLTEEKSTLAGEIRDLKDMldVKERKINVLQKKIENLQEQLRDKD----KQLAG--LKERVKSLQTDSS-------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3445 qrQKDLAQEQAQRLLEDKELMQKRLDE--ETEEYQKSLEAERKRQleivaEAEKLKLQVSQLSVAQAKAEEEAKRFKKQA 3522
Cdd:pfam10174 433 --NTDTALTTLEEALSEKERIIERLKEqrEREDRERLEELESLKK-----ENKDLKEKVSALQPELTEKESSLIDLKEHA 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3523 DNIAARL---------LETEIATKDKSTVMQQLEVERRNNSKEAD----DLRNAIANLETEKARLKKDAEELQNKSKEMA 3589
Cdd:pfam10174 506 SSLASSGlkkdsklksLEIAVEQKKEECSKLENQLKKAHNAEEAVrtnpEINDRIRLLEQEVARYKEESGKAQAEVERLL 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3590 DAqMKQIEHEKtmlqqtfltekemlLKKERLIEDEKKRLESQYEEEAKKAKALTD-EQERQRK---LMEEEKKKLHATMD 3665
Cdd:pfam10174 586 GI-LREVENEK--------------NDKDKKIAELESLTLRQMKEQNKKVANIKHgQQEMKKKgaqLLEEARRREDNLAD 650
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3666 EALSKQKEAEREMLNKQKEMQELEKKRLEQ-EKVLAEENKKL----RDQLQQLEEAQKEKNtQVISAATVETTKNV 3736
Cdd:pfam10174 651 NSQQLQLEELMGALEKTRQELDATKARLSStQQSLAEKDGHLtnlrAERRKQLEEILEMKQ-EALLAAISEKDANI 725
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2593-2693 |
1.92e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREKAAEAERLRKlaqeEAEKLHKQVieETQKKRTAEEELKRKSEAEKEAAKQ----KQKALEDLENLKMQAEE 2668
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEEL--EEKKEKLQEEEDKLLEEAEKEAQQAikeaKKEADEIIKELRQLQKG 599
|
90 100
....*....|....*....|....*.
gi 1838104091 2669 AERKVK-QAQIEKEKQIQIAHVAAEK 2693
Cdd:PRK00409 600 GYASVKaHELIEARKRLNKANEKKEK 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2833-3016 |
1.97e-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: 49.54 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2833 EQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSntekskmllda 2912
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2913 eASKMRDvaeeagkLRAIaeeakyQRQIaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAE 2992
Cdd:COG1579 85 -VRNNKE-------YEAL------QKEI--ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....
gi 1838104091 2993 DEAYQRKALEDEANQHKKEIEEKI 3016
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKI 172
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
3242-3486 |
1.97e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.30 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEM-------AKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQK 3314
Cdd:pfam00038 79 NLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATlarvdleAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3315 dllddelqrlkdEVDDAVKQ---------RGQVEEELFKVKVQMEELLKVKLKiekENQLLIKKDKDKAQQLLAEEAENM 3385
Cdd:pfam00038 159 ------------EMDAARKLdltsalaeiRAQYEEIAAKNREEAEEWYQSKLE---ELQQAAARNGDALRSAKEEITELR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3386 KRL-AKEAAILSVESQEASRLRQIAEedlVQQR-ALAEKMLKEKMQAIQEAsrlkaeaelLQRQKdlaQEQAQRLLEDKE 3463
Cdd:pfam00038 224 RTIqSLEIELQSLKKQKASLERQLAE---TEERyELQLADYQELISELEAE---------LQETR---QEMARQLREYQE 288
|
250 260
....*....|....*....|....*
gi 1838104091 3464 LM--QKRLDEETEEYQKSLEAERKR 3486
Cdd:pfam00038 289 LLnvKLALDIEIATYRKLLEGEECR 313
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2239-2399 |
2.04e-05 |
|
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: 48.98 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2239 VPSDAKEVESYRAKLKKMRAEAEGEQPVFDSLEEElqkattvSEKMSRVHSErdiELDHFRQNVSGLQDRWKAVFTQMEI 2318
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHP---DAEEIQERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2319 RHRELEQLGRQLGYYHESYDwLIHWITDAKERQEKIQAVSitDSKTLKEQLSQEKKLLEEIENNKENVDECQKYAKAYIN 2398
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
.
gi 1838104091 2399 S 2399
Cdd:cd00176 175 E 175
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
3260-3729 |
2.08e-05 |
|
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: 51.01 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3260 KRAQAENAALEQKKKA------DAEMAKHKKLAE--------QTLKQKFQ--VEQELTKVKLKLDDTDkqkDLLDD-ELQ 3322
Cdd:pfam06160 6 KKIYKEIDELEERKNElmnlpvQEELSKVKKLNLtgetqekfEEWRKKWDdiVTKSLPDIEELLFEAE---ELNDKyRFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3323 RLKDEVDDAVKQRGQVEEELFKVKVQMEELLKvklkIEKENQLLIKKDKDKAQQLlaeeaenMKRLAKEAAILSVesqea 3402
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLE----SEEKNREEVEELKDKYREL-------RKTLLANRFSYGP----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3403 srlrqiAEEDLvqqralaEKMLKEKMQAIQEASRLKAEAELLQrqkdlAQEQAQRLLEDKELMQKRLdEETEEYQKSLEA 3482
Cdd:pfam06160 147 ------AIDEL-------EKQLAEIEEEFSQFEELTESGDYLE-----AREVLEKLEEETDALEELM-EDIPPLYEELKT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3483 ERKRQLEIVAEAEKlKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIatKDKSTVMQQLEverrnnsKEADDLRN 3562
Cdd:pfam06160 208 ELPDQLEELKEGYR-EMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLEL--DEAEEALEEIE-------ERIDQLYD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3563 AianLETEKaRLKKDAEELQNKSKEM---ADAQMKQIEHEKTMLQQTF-LTEKEmlLKKERLIEDEKKRLESQYEEE--- 3635
Cdd:pfam06160 278 L---LEKEV-DAKKYVEKNLPEIEDYlehAEEQNKELKEELERVQQSYtLNENE--LERVRGLEKQLEELEKRYDEIver 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3636 -AKKAKALTDEQERQRKLM------EEEKKKLHATMDEALSKQKEAEREMLNKQKEMQE----LEKKRL--------EQE 3696
Cdd:pfam06160 352 lEEKEVAYSELQEELEEILeqleeiEEEQEEFKESLQSLRKDELEAREKLDEFKLELREikrlVEKSNLpglpesylDYF 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3697 KVLAEENKKLRDQL-----------QQLEEAQ------KEKNTQVISAAT 3729
Cdd:pfam06160 432 FDVSDEIEDLADELnevplnmdevnRLLDEAQddvdtlYEKTEELIDNAT 481
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2838-3718 |
2.13e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2838 RLRAEFDNAEQQRSLLEDELYRLKNEvIAAQQQRkqledeLAKMRSEMEILIQLKSRAEKETMSntekskmlldaeASKM 2917
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQ-LAAEQYR------LVEMARELAELNEAESDLEQDYQA------------ASDH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2918 RDVAEEAgkLRAIAEEAKYQRQIAEEEAArqraeaeriLKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAED---- 2993
Cdd:PRK04863 337 LNLVQTA--LRQQEKIERYQADLEELEER---------LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADyqqa 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2994 -EAYQRKALedeANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRIL--KLNFEKASSGKLDLELELn 3070
Cdd:PRK04863 406 lDVQQTRAI---QYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLeqKLSVAQAAHSQFEQAYQL- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3071 kLKNIA-----EETQQSKLRAEEEAEKQRKLAmeeekrrreaeETVKKITAAEKEAgRQRKIAQDELDRLKKKAEEARKQ 3145
Cdd:PRK04863 482 -VRKIAgevsrSEAWDVARELLRRLREQRHLA-----------EQLQQLRMRLSEL-EQRLRQQQRAERLLAEFCKRLGK 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3146 KDKADSEAEkQIVAASQAALKcrTAEQQVQSVLAQQKEDSMMHKKLQQEYEKakklakeaeaakekaekeavlLRKQAEE 3225
Cdd:PRK04863 549 NLDDEDELE-QLQEELEARLE--SLSESVSEARERRMALRQQLEQLQARIQR---------------------LAARAPA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3226 AESQKAAAEKEAAIQAKAQEDAER--------LRKEAEFE------AAKRAQAENAALEQKKKADAEMAKHKKLAEQ--- 3288
Cdd:PRK04863 605 WLAAQDALARLREQSGEEFEDSQDvteymqqlLERERELTverdelAARKQALDEEIERLSQPGGSEDPRLNALAERfgg 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3289 ----------TLKQK--FQ----------VEQELTKVKLKLddtDKQKDLLDD------ELQRLKDEVDDAvkqrgqveE 3340
Cdd:PRK04863 685 vllseiyddvSLEDApyFSalygparhaiVVPDLSDAAEQL---AGLEDCPEDlyliegDPDSFDDSVFSV--------E 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3341 ELFK-VKVQMEEllkVKLKIEK--ENQLLIKKDKDKAQQLLAEEAEnmkRLAKEAAILSVESQEASRLRQIAEEDLVQQR 3417
Cdd:PRK04863 754 ELEKaVVVKIAD---RQWRYSRfpEVPLFGRAAREKRIEQLRAERE---ELAERYATLSFDVQKLQRLHQAFSRFIGSHL 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3418 ALA-----EKMLKEKMQAIQEASRLKA---EAELLQRQK-DLAQEQAQRL--------LEDKELMQKRLDEETEEYQKSL 3480
Cdd:PRK04863 828 AVAfeadpEAELRQLNRRRVELERALAdheSQEQQQRSQlEQAKEGLSALnrllprlnLLADETLADRVEEIREQLDEAE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3481 EAER--KRQLEIVAEAEKL--KLQVSQLSVAQAKAE-EEAKRFKKQADNiAARLLeTEIatkdkstvmqqleVERRNN-- 3553
Cdd:PRK04863 908 EAKRfvQQHGNALAQLEPIvsVLQSDPEQFEQLKQDyQQAQQTQRDAKQ-QAFAL-TEV-------------VQRRAHfs 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3554 -SKEADDLRNAIANLETEKARLKKdAEELQNKSKEM---ADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDekkrLE 3629
Cdd:PRK04863 973 yEDAAEMLAKNSDLNEKLRQRLEQ-AEQERTRAREQlrqAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQD----LG 1047
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3630 SQYEEEAkkakaltDEQERQRklmeeeKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKrleqekvLAEENKKLRDQ 3709
Cdd:PRK04863 1048 VPADSGA-------EERARAR------RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK-------LRKLERDYHEM 1107
|
....*....
gi 1838104091 3710 LQQLEEAQK 3718
Cdd:PRK04863 1108 REQVVNAKA 1116
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2846-3038 |
2.22e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2846 AEQQRSLLEDELYRLKNEVIAAQQQR-KQLEDElakmrsemeiliQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEA 2924
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERlKQLEKE------------RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2925 GKLRAIAEEAKyqrqiAEEEAARQRAEAERILKEKLAAISEA-TRLKTEAEIALK-----EKEAENERLRRAAEDE---- 2994
Cdd:PRK09510 145 AKAKAEAEAKR-----AAAAAKKAAAEAKKKAEAEAAKKAAAeAKKKAEAEAAAKaaaeaKKKAEAEAKKKAAAEAkkka 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1838104091 2995 AYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTL 3038
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5239-5267 |
2.70e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.70e-05
10 20
....*....|....*....|....*....
gi 1838104091 5239 VRKRRVVIVDPETGKEMTVYEAYRKGLID 5267
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2593-2754 |
2.71e-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: 49.15 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLK-------MQ 2665
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyeaLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2666 AEEAERKVKQAQIEKEkqiQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKqehgtvlQLQQEAAHLKKQQEDALKAR 2745
Cdd:COG1579 96 KEIESLKRRISDLEDE---ILELMERIEELEEELAELEAELAELEAELEEKKA-------ELDEELAELEAELEELEAER 165
|
....*....
gi 1838104091 2746 EEAEKELDK 2754
Cdd:COG1579 166 EELAAKIPP 174
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4535-4569 |
2.78e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.78e-05
10 20 30
....*....|....*....|....*....|....*
gi 1838104091 4535 KLLSAEKAVTGYKDPYTGNTISLFEALQKGLIPKE 4569
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2666-3038 |
2.87e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2666 AEEAERKVKQ-AQIEKEKQIQIAHVAAEKSATAELQStqRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKA 2744
Cdd:pfam02029 4 EEEAARERRRrAREERRRQKEEEEPSGQVTESVEPNE--HNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKeeaereaKKRAKAEESALKQKEMAEKELERQRKVADS 2824
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR-------LGRYKEEETEIREKEYQENKWSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2825 TAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKmrsemeiliqlksRAEKETMSNTE 2904
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ-------------NGEEEVTKLKV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2905 KSKMLLDAEASKMRDVAEEAGKLRA--IAEEAKYQRQIAEEEaarqraEAERILKEKLAAISEATRLKTEAEIALKEKEA 2982
Cdd:pfam02029 222 TTKRRQGGLSQSQEREEEAEVFLEAeqKLEELRRRRQEKESE------EFEKLRQKQQEAELELEELKKKREERRKLLEE 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 2983 EnERLRRAAEDEayQRKALEDEANQHKKEIEekivqlKKSSQAEMQRQKaMVDDTL 3038
Cdd:pfam02029 296 E-EQRRKQEEAE--RKLREEEEKRRMKEEIE------RRRAEAAEKRQK-LPEDSS 341
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3360-3566 |
2.90e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3360 EKENQLLIKKDKDKAQQLLAEEAENMKRLAKEaailsvesQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKA 3439
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKE--------RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3440 EAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETeeyQKSLEAERKRQLEIVAE--AEKLKLQVSQlSVAQAKAEEEAKR 3517
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKkkAEAEAKKKAA-AEAKKKAAAEAKA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838104091 3518 FKKQADNIAARLLETEIATKDKStvmqqlEVERRNNSKEADDLRNAIAN 3566
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAE------KAAAAKAAAEVDDLFGGLDS 268
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2811-3150 |
3.25e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2811 AEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQ 2890
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2891 LKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAK-YQRQIAEEEAARQRAEAERILKEKLAAISEATRL 2969
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKeLEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2970 KTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIR 3049
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3050 ILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQ 3129
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|.
gi 1838104091 3130 DELDRLKKKAEEARKQKDKAD 3150
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVAD 369
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2450-2664 |
3.40e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2450 LTSQYIKFITETQRRledeekaAKILKAEEQKKMADLQAELDKQKKLAEAHAKA------IAKAEKEADELKHQMKQEVS 2523
Cdd:COG2268 186 LDALGRRKIAEIIRD-------ARIAEAEAERETEIAIAQANREAEEAELEQEReietarIAEAEAELAKKKAEERREAE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2524 KREVAA-----LDAENQKKNIELELHELKKLSEQQINDKSQLVDDAlqsrtkieeeihiiriQLETTLNQKSTAETELKQ 2598
Cdd:COG2268 259 TARAEAeaayeIAEANAEREVQRQLEIAEREREIELQEKEAEREEA----------------ELEADVRKPAEAEKQAAE 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 2599 LREKA-AEAERLRKLAQEEAeklhKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKM 2664
Cdd:COG2268 323 AEAEAeAEAIRAKGLAEAEG----KRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2462-2767 |
3.46e-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: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2462 QRRLEDEEKAAKILKAEEQKKMADLQAElDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKNIEL 2541
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEK-EEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2542 ELHELKKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETE-----LKQLREKAAEAERLRKLAQEE 2616
Cdd:pfam13868 115 QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREeereaEREEIEEEKEREIARLRAQQE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2617 AEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSAT 2696
Cdd:pfam13868 195 KAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 2697 AELQstqrsfveKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKARE-EAEKELDKWRQKANEALRLRL 2767
Cdd:pfam13868 275 EIEQ--------EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEgERLREEEAERRERIEEERQKK 338
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2465-3025 |
3.76e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2465 LEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQ------EVSKREVAALDAENQKKN 2538
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNElssledMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2539 IELELHELKKLSEQQindkSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKaaeaerLRKLaqEEAE 2618
Cdd:PRK01156 268 ELEKNNYYKELEERH----MKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAI------IKKL--SVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2619 KLHKQVIEETQKKrtaeEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAE------ 2692
Cdd:PRK01156 336 KDYNDYIKKKSRY----DDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDaikkel 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2693 ----------KSATAELQSTQRSFVEKTSKLEESLKQEH--------GTVLQlQQEAAHLKKQQEDALKAREEAEKELDK 2754
Cdd:PRK01156 412 neinvklqdiSSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcGTTLG-EEKSNHIINHYNEKKSRLEEKIREIEI 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2755 WRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADStaqqkltaeQ 2834
Cdd:PRK01156 491 EVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL---------E 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2835 ELIRLRAEFDNAEQQRSLLEDELYRLKNEVIaaQQQRKQLEDELAKMRSEMEiliqlksraekETMSNTEKSKMLLDAEA 2914
Cdd:PRK01156 562 DLDSKRTSWLNALAVISLIDIETNRSRSNEI--KKQLNDLESRLQEIEIGFP-----------DDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2915 SKMRDVAEEAGKLRAIAEEAK-----YQRQIAEEEaarqraEAERILKEKLAAISEA-TRLK------TEAEIALKEKEA 2982
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRgkidnYKKQIAEID------SIIPDLKEITSRINDIeDNLKksrkalDDAKANRARLES 702
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1838104091 2983 ENERLRRAAEdEAYQRKALEDEANQHKKEIEEKIVQLKKSSQA 3025
Cdd:PRK01156 703 TIEILRTRIN-ELSDRINDINETLESMKKIKKAIGDLKRLREA 744
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3392-3719 |
3.84e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3392 AAILSVESQEASRLRQIAEEDLVQqralaEKMLKEKMQAIQEASRLKAEAELLQrqKDLaqEQAQRLLEDKElmqkRLDE 3471
Cdd:PRK11281 14 AFLFLLLCLSSAFARAASNGDLPT-----EADVQAQLDALNKQKLLEAEDKLVQ--QDL--EQTLALLDKID----RQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3472 ETEEYQKSLEAERKRQLEIVAEAEKLKlqvsqlsvaQAKAEEEAKRFKKQA-DNIAARLLET---------EIATKDKST 3541
Cdd:PRK11281 81 ETEQLKQQLAQAPAKLRQAQAELEALK---------DDNDEETRETLSTLSlRQLESRLAQTldqlqnaqnDLAEYNSQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3542 VMQQLEVER-----RNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQiehEKTMLQ-QTFLTEkemLL 3615
Cdd:PRK11281 152 VSLQTQPERaqaalYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDL---QRKSLEgNTQLQD---LL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3616 KKER-LIEDEKKRLESQyeeeakkakaLTDEQE--RQRKLMEEEKkklhaTMDEALSkQKEAEREMLNK--QKEMQ---E 3687
Cdd:PRK11281 226 QKQRdYLTARIQRLEHQ----------LQLLQEaiNSKRLTLSEK-----TVQEAQS-QDEAARIQANPlvAQELEinlQ 289
|
330 340 350
....*....|....*....|....*....|....*...
gi 1838104091 3688 LEKKRLEQ-EK--VLAEENKKLR---DQLQQLEEAQKE 3719
Cdd:PRK11281 290 LSQRLLKAtEKlnTLTQQNLRVKnwlDRLTQSERNIKE 327
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2583-2828 |
3.88e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2583 ETTLNQKSTAETELKQLREKAAEAERLrklaqeEAEKLHKqviEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLEnL 2662
Cdd:pfam15709 322 KALLEKREQEKASRDRLRAERAEMRRL------EVERKRR---EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIR-L 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2663 KMQAEEAERkvkQAQIEKEKQIQIAHVAAEKSATAELQSTQRsfvektskleeslkqehgTVLQLQQeaahlKKQQEDAL 2742
Cdd:pfam15709 392 RKQRLEEER---QRQEEEERKQRLQLQAAQERARQQQEEFRR------------------KLQELQR-----KKQQEEAE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2743 KAREEAEKELDKWRQKANEALRLRLQAEEEahkkslaqeEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVA 2822
Cdd:pfam15709 446 RAEAEKQRQKELEMQLAEEQKRLMEMAEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQA 516
|
....*.
gi 1838104091 2823 DSTAQQ 2828
Cdd:pfam15709 517 QEQARQ 522
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3320-3564 |
3.92e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.46 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3320 ELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEllkvklKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAailsvES 3399
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK-----QK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3400 QEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEEtEEYQKS 3479
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE-EAKAKA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3480 LEAERKRQLEIVAEAEKLKlqvsqlsvaQAKAEEEAKRfKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNsKEADD 3559
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEA---------AAAAAAEAER-KADEAELGDIFGLASGSNAEKQGGARGAAAGSEVD-KYAAI 267
|
....*
gi 1838104091 3560 LRNAI 3564
Cdd:TIGR02794 268 IQQAI 272
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2591-2834 |
4.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2591 TAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELkrkseaekEAAKQKQKALEDlenlkmQAEEAE 2670
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------EALQAEIDKLQA------EIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2671 RKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSF------VEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKA 2744
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDVLLGSESFsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2745 REEAEKELDKWRQKANEAlrlrlQAEEEAHKKSLaqeeaekQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADS 2824
Cdd:COG3883 159 LEALKAELEAAKAELEAQ-----QAEQEALLAQL-------SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|
gi 1838104091 2825 TAQQKLTAEQ 2834
Cdd:COG3883 227 AAAAAAAAAA 236
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5030-5066 |
4.21e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 4.21e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1838104091 5030 RYLVGTSCIAGVLLESSKERLSVYQAMKKNLIRPGTA 5066
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5106-5137 |
4.33e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 4.33e-05
10 20 30
....*....|....*....|....*....|..
gi 1838104091 5106 KLLSAERAVTGYRDPYSGKTISLFQAMQKGLI 5137
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2540-2876 |
4.40e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2540 ELELHELKKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEaerlrklAQEEAEK 2619
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-------LEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2620 LHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAEL 2699
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2700 QSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLA 2779
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2780 QEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYR 2859
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*..
gi 1838104091 2860 LKNEVIAAQQQRKQLED 2876
Cdd:COG4372 325 AKKLELALAILLAELAD 341
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3429-3741 |
4.48e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3429 QAIQEASRLKAEAELLQRQKDLAQEQAQRL---LEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLS 3505
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3506 VAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARlkkdaEELQNKS 3585
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE-----QALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3586 KEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMD 3665
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3666 EALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVETTKNVYNGQN 3741
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
3042-3286 |
4.58e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3042 RVVEEEIRILKLNFEKASSGKLDLELelnKLKNIAEETQQSKLRAEEEAEKqRKLAMEEEKRRREAEETVKKITAAEKEA 3121
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEA---RQARLEREKAAREARHKKAAEA-RAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3122 GRQRK-------IAQDELDRLKKKAEEARKQKDKADsEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHK-KLQQ 3193
Cdd:PRK05035 508 IKAGArpdnsavIAAREARKAQARARQAEKQAAAAA-DPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAvAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3194 EYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKK 3273
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQAN 666
|
250
....*....|...
gi 1838104091 3274 KADAEMAKHKKLA 3286
Cdd:PRK05035 667 AEPEEAEDPKKAA 679
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2596-2751 |
4.70e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.71 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2596 LKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAE------------EELKRKSEAEKEAAKQKQKALEDLENLK 2663
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRErnqqrqearrerEELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2664 MQAEEAERKVKQAQ---IEKEKQIqiahvaaeksataelqstQRSFVEKTSKLEESLKQEHGTVLQ--LQQEAAHLKKQQ 2738
Cdd:PRK12705 105 NQLEEREKALSARElelEELEKQL------------------DNELYRVAGLTPEQARKLLLKLLDaeLEEEKAQRVKKI 166
|
170
....*....|...
gi 1838104091 2739 EDalKAREEAEKE 2751
Cdd:PRK12705 167 EE--EADLEAERK 177
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2739-2976 |
4.84e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2739 EDALKAREEAEKELDKWRQKANealrlRLQAEEEAhkkslaqeeaekqkeEAEREAKKRAKAEESALKQKEMAEKELERQ 2818
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQAN-----REAEEAEL---------------EQEREIETARIAEAEAELAKKKAEERREAE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2819 RKvadstaqqKLTAEQELIrlraefdnaeqqrslledelyrlknevIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKE 2898
Cdd:COG2268 259 TA--------RAEAEAAYE---------------------------IAEANAEREVQRQLEIAEREREIELQEKEAEREE 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 2899 tmsNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKyqrqiAEEEAARQRAEAERILKEklAAISEAtRLKTEAEIA 2976
Cdd:COG2268 304 ---AELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGD--AAILLM-LIEKLPEIA 370
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2792-3098 |
5.09e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2792 REAKKRAKAEESALKQKEM-AEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAE----------------QQRSLLE 2854
Cdd:pfam15709 197 REGKVHGEAEAAVGKSRESkAEKKSELISKGKKTGAKRKRTQKERNLEVAAELSGPDvinsketedasergafSSDSVVE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2855 DELYRLKNE------VIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVaeeagklr 2928
Cdd:pfam15709 277 DPWLSSKYDaeesqvSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL-------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2929 aiaeEAKYQRQIAEEEAARQRAEAERilKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAED--EAYQRKALEDEAN 3006
Cdd:pfam15709 349 ----EVERKRREQEEQRRLQQEQLER--AEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEErkQRLQLQAAQERAR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3007 QHKKEIEEKIVQL-KKSSQAEMQRQKAmvddtlKQRRVVEEEIRilklnfekassgkldLELELNKLKNIAEETQQSKLR 3085
Cdd:pfam15709 423 QQQEEFRRKLQELqRKKQQEEAERAEA------EKQRQKELEMQ---------------LAEEQKRLMEMAEEERLEYQR 481
|
330
....*....|...
gi 1838104091 3086 AEEEAEKQRKLAM 3098
Cdd:pfam15709 482 QKQEAEEKARLEA 494
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3258-3457 |
5.17e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3258 AAKRAQAENAA---LEQKKKADAEMAKhkklAEQTLkQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQ 3334
Cdd:COG3206 167 ELRREEARKALeflEEQLPELRKELEE----AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3335 RGQVEEELFKVKVQMEELLK-----------VKLKIEKENQLLIKKDKD-KAQQLLAEEAENMKRLAKEAAILSVESQEA 3402
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspviqqlraqlAELEAELAELSARYTPNHpDVIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3403 SRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAE--------LLQRQKDLAQEQAQR 3457
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvarelyesLLQRLEEARLAEALT 384
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
3397-3709 |
6.51e-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: 49.63 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3397 VESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEY 3476
Cdd:NF033838 40 VRGGNNPTVTSSGNESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3477 QKSLEA-------ERKRQLEIVAEAEKlklqvsQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEV- 3548
Cdd:NF033838 120 KKELDAafeqfkkDTLEPGKKVAEATK------KVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELv 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3549 -ERRNNSKEADDLRNAIANLETEKARLKKdaeelqnkskemadaqMKQIEhektmlqqtflTEKEMllkkerlIEDEKKR 3627
Cdd:NF033838 194 kEEAKEPRDEEKIKQAKAKVESKKAEATR----------------LEKIK-----------TDREK-------AEEEAKR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3628 LESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQEL--EKKRLEQEKVLAEENKK 3705
Cdd:NF033838 240 RADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSLkpEKKVAEAEKKVEEAKKK 319
|
....
gi 1838104091 3706 LRDQ 3709
Cdd:NF033838 320 AKDQ 323
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
3442-3727 |
6.51e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 48.91 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3442 ELLQRQKDLAQEQAQRLLEDKELMQKRLDEE------TEEYQKSLEAERKRQLEIVAEAEKLKLQVS-QLSVAQAK---A 3511
Cdd:pfam15742 45 DLKQHNSLLQEENIKIKAELKQAQQKLLDSTkmcsslTAEWKHCQQKIRELELEVLKQAQSIKSQNSlQEKLAQEKsrvA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3512 EEEAKRFKKQADNIAA---RLLETEIATKdkstvmQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEM 3588
Cdd:pfam15742 125 DAEEKILELQQKLEHAhkvCLTDTCILEK------KQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3589 ADaqmKQIEHEKTMLQQTF-LTEKEMLLKKerlIEDEKKRLESQ---YEEEAKKAKALTDEQERQRKLMEE--------- 3655
Cdd:pfam15742 199 QD---KEAQLEMTNSQQQLrIQQQEAQLKQ---LENEKRKSDEHlksNQELSEKLSSLQQEKEALQEELQQvlkqldvhv 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3656 ---------EKKKLHATMDEALS---------KQKEAEREMLNKQKE-MQELEKKRLEQEKVLAEENKKLRDQLQQLEEA 3716
Cdd:pfam15742 273 rkynekhhhHKAKLRRAKDRLVHeveqrderiKQLENEIGILQQQSEkEKAFQKQVTAQNEILLLEKRKLLEQLTEQEEL 352
|
330
....*....|.
gi 1838104091 3717 QKeKNTQVISA 3727
Cdd:pfam15742 353 IK-NNKRTISS 362
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2687-2907 |
7.23e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2687 AHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQK--ANEALR 2764
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2765 LRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA---------EKELERQRKVADSTAQQKLTAEQE 2835
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 2836 LIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSK 2907
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2825-3048 |
7.29e-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: 49.26 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2825 TAQQKLTAEQELIRLRAEFDNAEQQrslLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILI----QLKSRAEKETM 2900
Cdd:pfam05667 301 THTEKLQFTNEAPAATSSPPTKVET---EEELQQQREEELEELQEQLEDLESSIQELEKEIKKLEssikQVEEELEELKE 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2901 SNTEKSK----------MLLDAEA--SKM-RDVAEEAGKLRAIAEE---------AKYQRqiAEEEAARQRAEAERI--- 2955
Cdd:pfam05667 378 QNEELEKqykvkkktldLLPDAEEniAKLqALVDASAQRLVELAGQwekhrvpliEEYRA--LKEAKSNKEDESQRKlee 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2956 ---LKEKLAAISEATRLKTEaeiALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIE-EKIVQLKKSSQAEMQRQK 3031
Cdd:pfam05667 456 ikeLREKIKEVAEEAKQKEE---LYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEINSLT 532
|
250
....*....|....*..
gi 1838104091 3032 AMVDDTLKqrrVVEEEI 3048
Cdd:pfam05667 533 GKLDRTFT---VTDELV 546
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1285-1371 |
7.32e-05 |
|
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: 45.37 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1285 GYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLID---MGRVYQQSN-QENLEQAFNVAERdLGVTRLLDPEDVDVPHPDEk 1360
Cdd:cd21218 27 GPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelVLEVLSEEDlEKRAEKVLQAAEK-LGCKYFLTPEDIVSGNPRL- 104
|
90
....*....|.
gi 1838104091 1361 sIITYVSSLYD 1371
Cdd:cd21218 105 -NLAFVATLFN 114
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3123-3475 |
7.52e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3123 RQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAAlkcRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLA 3202
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL---RQSREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3203 KEAEAAKEKAEKEAVLL--RKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAkraQAENAALeqkkkaDAEMA 3280
Cdd:pfam07888 125 AAHEARIRELEEDIKTLtqRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT---EEELRSL------SKEFQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3281 KHKKLAEQTLKQKFQVEQELTKVKLKLDDTDK---QKDLLDDELQR--------------LKDEVDDAVKQRGQVEEELF 3343
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaENEALLEELRSlqerlnaserkvegLGEELSSMAAQRDRTQAELH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3344 KVKVQMEE----LLKVKLKIeKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRAL 3419
Cdd:pfam07888 276 QARLQAAQltlqLADASLAL-REGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDC 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3420 AEKMLKEKMQAIQEasrLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEE 3475
Cdd:pfam07888 355 NRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
3245-3805 |
7.53e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3245 EDAERLRKEAEFEAAKRAQAENAALEQKKKAD--AEMAKHKKLAEQTLKQKFQVEQELTKVKL-KLDDTDKQKDLLDDEL 3321
Cdd:TIGR01612 1166 DDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNeiAEIEKDKTSLEEVKGINLSYGKNLGKLFLeKIDEEKKKSEHMIKAM 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3322 QRLKDEVDDAVKQRGQVEEELfkvkvqmeellKVKLKIEKE-NQLLIKKDKDKAQQLLAEEA-ENMKRLAKEAAILSVES 3399
Cdd:TIGR01612 1246 EAYIEDLDEIKEKSPEIENEM-----------GIEMDIKAEmETFNISHDDDKDHHIISKKHdENISDIREKSLKIIEDF 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3400 QEASRLRQIAEEdLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQK--DLAQEQAQRLLEDKELMQKRLDEETEEYQ 3477
Cdd:TIGR01612 1315 SEESDINDIKKE-LQKNLLDAQKHNSDINLYLNEIANIYNILKLNKIKKiiDEVKEYTKEIEENNKNIKDELDKSEKLIK 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3478 K-----SLEaERKRQLEIVAEAEKLKLQVSQLSVAQA---KAEEEAKRFKKQAD--NIAARLLETEIATKDKSTvmQQLE 3547
Cdd:TIGR01612 1394 KikddiNLE-ECKSKIESTLDDKDIDECIKKIKELKNhilSEESNIDTYFKNADenNENVLLLFKNIEMADNKS--QHIL 1470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3548 VERRNNSKEADDLrnaiaNLETEKARLKKdaeelQNKSKEMADAQMKQIEHEKTMLQQtFLTEKEMLLKKERLIE----- 3622
Cdd:TIGR01612 1471 KIKKDNATNDHDF-----NINELKEHIDK-----SKGCKDEADKNAKAIEKNKELFEQ-YKKDVTELLNKYSALAiknkf 1539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3623 DEKKRLESQYEEEAKKA-KALTDEQERQRKLMEEEKKKLHATMDEAlSKQKEAEREMLNKQKEMQELEKKRLEqekvLAE 3701
Cdd:TIGR01612 1540 AKTKKDSEIIIKEIKDAhKKFILEAEKSEQKIKEIKKEKFRIEDDA-AKNDKSNKAAIDIQLSLENFENKFLK----ISD 1614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3702 ENKKLRDQLQQLEEAQKEKNTQVISAATVETTKNVYNGQNAGDVVDSVENKPdplsfDGIRDKvpasrlrdvgllsKKEF 3781
Cdd:TIGR01612 1615 IKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQK-----KNIEDK-------------KKEL 1676
|
570 580 590
....*....|....*....|....*....|....
gi 1838104091 3782 D----KLKKGKATVQQ------LGETEKLKLILK 3805
Cdd:TIGR01612 1677 DeldsEIEKIEIDVDQhkknyeIGIIEKIKEIAI 1710
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1158-1251 |
9.79e-05 |
|
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: 44.98 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1158 KWVNKHLIKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM---RFHKLQNVQIALDFLrhRQVKLVN-IRN 1233
Cdd:cd21218 17 RWVNYHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1838104091 1234 DDIADGNPKLTLGLIWTI 1251
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
1140-1251 |
9.95e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 45.34 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1140 WPHFIEDERDrvqKKTFTKWVNKHLikrAESQHH--VTDLYEDLRDGHNLISLLEVLSGDTLPREKG--RMRFHKLQNVQ 1215
Cdd:cd21285 2 KSWEAENGFD---KQIYTDWANHYL---AKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENID 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 1838104091 1216 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 1251
Cdd:cd21285 76 ACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2464-2679 |
1.00e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2464 RLEDEEKAAKiLKAEEQKKMADLQAELDKQKKLAEAHA-KAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKnIELE 2542
Cdd:PRK09510 66 RQQQQQKSAK-RAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA-KAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2543 LHELKKLSEQQindksqlvddALQSRTKIEEEIHIIRIQLEttlnQKSTAETELKqlreKAAEAERLRKLAQEEAEKlhk 2622
Cdd:PRK09510 144 AAKAKAEAEAK----------RAAAAAKKAAAEAKKKAEAE----AAKKAAAEAK----KKAEAEAAAKAAAEAKKK--- 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 2623 qviEETQKKRTAEEELKRKSEAEK----EAAKQKQKALEDLENLKMQAEEAERKVKQAQIE 2679
Cdd:PRK09510 203 ---AEAEAKKKAAAEAKKKAAAEAkaaaAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3400-3600 |
1.02e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3400 QEASRLRQiaeedlvQQRALAEKMLKEKMQAIQEASRLKAE-AELLQRQKDLAQEQAQRLLEDKELMQKRldEETEEYQK 3478
Cdd:PRK09510 62 EQYNRQQQ-------QQKSAKRAEEQRKKKEQQQAEELQQKqAAEQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3479 SLEAERKRQLEivAEAEKLKLQVSQLSVAQAKAEEEAkrfKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEAD 3558
Cdd:PRK09510 133 QAEEAAAKAAA--AAKAKAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838104091 3559 DLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEK 3600
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3277-3496 |
1.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3277 AEMAKHKKLAE-QTL-KQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKvqmeellk 3354
Cdd:COG1579 1 AMPEDLRALLDlQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3355 vklkiekenqllIKKDKDKAQQLLAEEAENMKRLAKEaailsVESQEAsrlrqiaeedlvqQRALAEKMLKEKMQAIQEa 3434
Cdd:COG1579 73 ------------ARIKKYEEQLGNVRNNKEYEALQKE-----IESLKR-------------RISDLEDEILELMERIEE- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3435 srlkAEAELLQRQKDLAQEQAQrlLEDKelmQKRLDEETEEYQKSLEAERKRQLEIVAEAEK 3496
Cdd:COG1579 122 ----LEEELAELEAELAELEAE--LEEK---KAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2226-2713 |
1.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2226 LKQYEDCLREVHTVPSDAKEVESYRAKLKKMRAEAEgeqpvfdSLEEELQKATTVSEKMSRVHSERDI--ELDHFRQNVS 2303
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEKLEKLLQLLPLyqELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2304 GLQDRWKavftQMEIRHRELEQLGRQLgyyhesydwlIHWITDAKERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNK 2383
Cdd:COG4717 143 ELPERLE----ELEERLEELRELEEEL----------EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2384 ENVDECQKYAKAYINSIKDyELQLVAYNAKADPHASPLKKNKMDSASDNIIqeyVTLRTRYSELMTLTSQYIKFIT---- 2459
Cdd:COG4717 209 AELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLFlvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2460 -----ETQRRLEDEEKAAKILKAEEQKKMADLQAEldKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSK-REVAALDAE 2533
Cdd:COG4717 285 llallFLLLAREKASLGKEAEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELlREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2534 NQKKNIELELHELkkLSEQQINDKSQLVDDALQSRtkieeeihiiriQLETTLNQKSTAETELKQLREkaaeaERLRKLA 2613
Cdd:COG4717 363 LQLEELEQEIAAL--LAEAGVEDEEELRAALEQAE------------EYQELKEELEELEEQLEELLG-----ELEELLE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2614 QEEAEKLHKQVIEETQKKRTAEEELKRKSEaEKEAAKQKQKALED---LENLKMQAEEAERKVKQAqIEKEKQIQIAHVA 2690
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELRE-ELAELEAELEQLEEdgeLAELLQELEELKAELREL-AEEWAALKLALEL 501
|
490 500
....*....|....*....|...
gi 1838104091 2691 AEKSATAELQSTQRSFVEKTSKL 2713
Cdd:COG4717 502 LEEAREEYREERLPPVLERASEY 524
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2529-2776 |
1.13e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.54 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2529 ALDAENQKKNIELELHELKKLSEQQINDKSQLVDDaLQSRTKIEEEIHIIRIQLETTLNQKSTAETEL----KQLREKAA 2604
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQ-LKKQEEAISQASRKLRETQNTLNQLNKQIDELnasiAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2605 EAERLrkLAQE------EAEKLHKQVI---EETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQ 2675
Cdd:PRK11637 121 AQERL--LAAQldaafrQGEHTGLQLIlsgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2676 AQIEKEKQ---IQIAHVAAEKSATAelqstqrsfvektskLEESLKQEHGTVLQLQQEAAHLKKQ---QEDALKAReeAE 2749
Cdd:PRK11637 199 LLYEQQAQqqkLEQARNERKKTLTG---------------LESSLQKDQQQLSELRANESRLRDSiarAEREAKAR--AE 261
|
250 260
....*....|....*....|....*..
gi 1838104091 2750 KEldkwrqkANEALRLRlQAEEEAHKK 2776
Cdd:PRK11637 262 RE-------AREAARVR-DKQKQAKRK 280
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3219-3581 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3219 LRKQAE---EAESQKAAAEKEAAIQAKAQEDAERLRKEAEF------EAAKRAQAENAALEQKKKAdaEMAKHKKLAEQT 3289
Cdd:pfam07888 40 LQERAEllqAQEAANRQREKEKERYKRDREQWERQRRELESrvaelkEELRQSREKHEELEEKYKE--LSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3290 ---LKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEElfkvkvqmEELLKVKLKIEKENQLL 3366
Cdd:pfam07888 118 dalLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3367 IKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKM---------LKEKMQAIQeASRL 3437
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLnaserkvegLGEELSSMA-AQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3438 KAEAELLQRQKDLAQEQAQrlLEDKELM----QKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKlqvsqlsvaQAKAEE 3513
Cdd:pfam07888 269 RTQAELHQARLQAAQLTLQ--LADASLAlregRARWAQERETLQQSAEADKDRIEKLSAELQRLE---------ERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3514 EAKRFKkqadniaarlLETEIATKDKSTVMQQLEVERrnnskEADDLRNAIANLETEKARLKKDAEEL 3581
Cdd:pfam07888 338 RMEREK----------LEVELGREKDCNRVQLSESRR-----ELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3242-3457 |
1.17e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKE---AEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLD 3318
Cdd:COG4942 24 EAEAELEQLQQEiaeLEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3319 DELQRLKdevdDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKEnqlLIKKDKDKAQQL---LAEEAENMKRLAKEAAIL 3395
Cdd:COG4942 104 EELAELL----RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY---LAPARREQAEELradLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3396 SVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQ-KDLAQEQAQR 3457
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAAA 239
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2505-2700 |
1.18e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2505 AKAEKEADELKHQMK------QEVSKREVAAldAENQKKNIELELHELKKLSEQQINDKsqlvddALQSRTKIEEEIHII 2578
Cdd:TIGR02794 46 GAVAQQANRIQQQKKpaakkeQERQKKLEQQ--AEEAEKQRAAEQARQKELEQRAAAEK------AAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2579 RIQLEttlNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRtAEEELKRKSEAEKEA-AKQKQKAle 2657
Cdd:TIGR02794 118 QKQAE---EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA-EEAKKKAEAEAKAKAeAEAKAKA-- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1838104091 2658 dlENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQ 2700
Cdd:TIGR02794 192 --EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEA 232
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
1147-1258 |
1.20e-04 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 44.98 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1147 ERDRVQKKTFTKWVNKHLIkraesQHHVTDLYEDLRDGHNLISLLEV---------LSGDTLPREKGRMRfhKLQNVQIA 1217
Cdd:cd21329 2 EGESSEERTFRNWMNSLGV-----NPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1838104091 1218 LDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1258
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2590-2886 |
1.20e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 48.14 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2590 STAETELKQLREKAAEAERLRKLAQEEAEKLhKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEdLENLKMQaeea 2669
Cdd:pfam15742 30 TSAEKELRYERGKNLDLKQHNSLLQEENIKI-KAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELE-LEVLKQA---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2670 eRKVKQAQIEKEKqiqiahVAAEKSATAELQstqrsfvEKTSKLEESLKQEHGtvLQLQQEAAHLKKQQEDALKAREEAE 2749
Cdd:pfam15742 104 -QSIKSQNSLQEK------LAQEKSRVADAE-------EKILELQQKLEHAHK--VCLTDTCILEKKQLEERIKEASENE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2750 KELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQK 2829
Cdd:pfam15742 168 AKLKQQYQEEQQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKL 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 2830 LTAEQELIRLRAEFDNAEQQ-----------RSLLEDELYRLKNEVIAAQQQR----KQLEDELAKMRSEME 2886
Cdd:pfam15742 248 SSLQQEKEALQEELQQVLKQldvhvrkynekHHHHKAKLRRAKDRLVHEVEQRderiKQLENEIGILQQQSE 319
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2403-2882 |
1.37e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 48.43 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2403 YELQLVAYNAKADPHASPLKKNKMDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKILKAEEQKK 2482
Cdd:COG4995 6 LLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2483 MADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKNIELELHELKKLSEQQINDKSQLVD 2562
Cdd:COG4995 86 ALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2563 DALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKS 2642
Cdd:COG4995 166 LALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2643 EAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHG 2722
Cdd:COG4995 246 AAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2723 TVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAhkkslaqeeaekqkeEAEREAKKRAKAEE 2802
Cdd:COG4995 326 LLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLA---------------LLLEALLLLLLALL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2803 SALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELY---RLKNEVIAaqqqrkQLEDELA 2879
Cdd:COG4995 391 AALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYafvQLYQLLIA------PIEAELP 464
|
...
gi 1838104091 2880 KMR 2882
Cdd:COG4995 465 GIK 467
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2923-3461 |
1.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2923 EAGK---LRAIaeeakyqRQIAEEEAARQRAEAERILKEKlaAISEATRLKtEAEIALKEKEAENERLRRAAEDEAYQRK 2999
Cdd:COG4717 33 EAGKstlLAFI-------RAMLLERLEKEADELFKPQGRK--PELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3000 ALEdEANQHKKEIEEKIVQLKKSSQAEmqrqkamvdDTLKQRRVVEEEIRILKLNFEKAssgkldleleLNKLKNIaEET 3079
Cdd:COG4717 103 ELE-ELEAELEELREELEKLEKLLQLL---------PLYQELEALEAELAELPERLEEL----------EERLEEL-REL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3080 QQSKLRAEEEAEKQRklameeekrrREAEETVKKITAAEKEAGRQrkiAQDELDRLKKKAEEARKQKDKAdsEAEKQIVA 3159
Cdd:COG4717 162 EEELEELEAELAELQ----------EELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEA--QEELEELE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3160 ASQAALKCRTAEQQVQSVLAQQKEDSMMH-------KKLQQEYEKAKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAA 3232
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3233 AEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQE--LTKVKLKLDDT 3310
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3311 DKQKDLLDDELQRLKDEVDDAvkqRGQVEEELFKVKVQMEELLKVKLKIEKENqllikkdkdkAQQLLAEEAENMKRLAK 3390
Cdd:COG4717 387 LRAALEQAEEYQELKEELEEL---EEQLEELLGELEELLEALDEEELEEELEE----------LEEELEELEEELEELRE 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3391 EAAILSvesqeaSRLRQIAEEDLVQQRALAEKMLKEKMQ-AIQEASRLKAEAELLQR-QKDLAQEQAQRLLED 3461
Cdd:COG4717 454 ELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALELLEEaREEYREERLPPVLER 520
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
3446-3591 |
1.52e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.47 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3446 RQKDLAQEQ-AQRLLEdkelMQKRLDEeteeyqksLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADN 3524
Cdd:PTZ00491 669 RHQAELLEQeARGRLE----RQKMHDK--------AKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAEAEV 736
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3525 IAARLLeteiATKDKstVMQQLEVERRNNSKEAD-DLRNAIANLETEKARLKKDAEelQNKSKEMADA 3591
Cdd:PTZ00491 737 EQAELR----AKALR--IEAEAELEKLRKRQELElEYEQAQNELEIAKAKELADIE--ATKFERIVEA 796
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3625-3723 |
1.52e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3625 KKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKkLHATmDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENK 3704
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90
....*....|....*....
gi 1838104091 3705 KLRDQLQQLEEAQKEKNTQ 3723
Cdd:PRK12704 104 LLEKREEELEKKEKELEQK 122
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2590-2832 |
1.55e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.05 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2590 STAETELKQLREKAAEaeRLRKLAQEE-AEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQK--QKALEDLENLKMQA 2666
Cdd:PRK07735 1 MDPEKDLEDLKKEAAR--RAKEEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRaaAAAKAKAAALAKQK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2667 EEAERKVKQAQIEKEKqiqiAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKARE 2746
Cdd:PRK07735 79 REGTEEVTEEEKAKAK----AKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2747 EAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKK-----RAKAEESAL-KQKEM-----AEKEL 2815
Cdd:PRK07735 155 EEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKakaaaAAKAKAAALaKQKASqgngdSGDED 234
|
250
....*....|....*..
gi 1838104091 2816 ERQRKVADSTAQQKLTA 2832
Cdd:PRK07735 235 AKAKAIAAAKAKAAAAA 251
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4204-4240 |
1.58e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.58e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1838104091 4204 KLLSAERAVTGYKDPYTGKTISLFQAMKKDLIPKEQG 4240
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2603-2778 |
1.61e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2603 AAEAERLRKLAqeeaeKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQ--AQIEK 2680
Cdd:COG1579 3 PEDLRALLDLQ-----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEveARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2681 EKQiQIAHVAAEKSATA---ELQSTQRsfveKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKwRQ 2757
Cdd:COG1579 78 YEE-QLGNVRNNKEYEAlqkEIESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE-EL 151
|
170 180
....*....|....*....|.
gi 1838104091 2758 KANEALRLRLQAEEEAHKKSL 2778
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
1145-1252 |
1.88e-04 |
|
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: 44.36 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1145 EDERdrvqkKTFTKWVNKHLIKRAESQHHV---TD---LYEDLRDGHNLISLLEVLSGDTL-------PREKGRM--RFH 1209
Cdd:cd21294 5 EDER-----REFTKHINAVLAGDPDVGSRLpfpTDtfqLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQ 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1838104091 1210 KLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1252
Cdd:cd21294 80 MIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2938-3095 |
1.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2938 RQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEkeaENERLRRAAEDEAYQRkalEDEANQHKKEIEEKIV 3017
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRER---RNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3018 QLKKSSQaEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSgKLDLELE--------------LNKLKN-----IAEE 3078
Cdd:PRK12704 97 NLDRKLE-LLEKREEELEKKEKELEQKQQELEKKEEELEELIE-EQLQELErisgltaeeakeilLEKVEEearheAAVL 174
|
170
....*....|....*..
gi 1838104091 3079 TQQSKLRAEEEAEKQRK 3095
Cdd:PRK12704 175 IKEIEEEAKEEADKKAK 191
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3242-3393 |
2.00e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKEAEFEAAKRAQAENAALEQKKKadaEMAKHKKLAEQTLKQKfqvEQELTKvklKLDDTDKQKDLLDDEL 3321
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELR---ERRNELQKLEKRLLQK---EENLDR---KLELLEKREEELEKKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3322 QRLKDEVDDAVKQRGQVEEelfKVKVQMEELLKV-KLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAA 3393
Cdd:PRK12704 117 KELEQKQQELEKKEEELEE---LIEEQLQELERIsGLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEA 186
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
1266-1369 |
2.15e-04 |
|
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: 44.03 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1266 SEDMTAKEKLLCWSQrmtDGYQNIRCDNFTTSWRDGKLFNAVIHKHHPRLIDMGRVYQQSNQ-ENLEQAFNVAERDLGVT 1344
Cdd:cd21312 8 AKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPvTNAREAMQQADDWLGIP 84
|
90 100
....*....|....*....|....*
gi 1838104091 1345 RLLDPEDVDVPHPDEKSIITYVSSL 1369
Cdd:cd21312 85 QVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
3271-3719 |
2.24e-04 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 47.93 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3271 QKKKADAEMAKHKKLAEQTLKQKF------QVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFK 3344
Cdd:pfam09730 8 KKVAADGESREESLLQESASKEAYyaqrilELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3345 VKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEA--ENMKRLAKEAAILSVESQEASRLRQIaeedlvqqralAEK 3422
Cdd:pfam09730 88 YKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGlkHEITRKEEETELLNSQLEEAIRLREI-----------AER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3423 MLKEKMQAIQEASRLKAEAellqrQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVS 3502
Cdd:pfam09730 157 QLDEALETLKTEREQKNSL-----RKELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3503 QLSVAQAKAEEEAKRFKKQADNIAARLLeTEIATKDKSTVMQQL-EVERrnnskeaddlrnaianletEKARLKKDAEEL 3581
Cdd:pfam09730 232 NSGLDNRTSTPRKSEVFPPAPSLVSDLL-SELNISEIQKLKQQLiQVER-------------------EKVSLLSTLQES 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3582 QnKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEeakkakalTDEQERQRKLMEEEKKKLH 3661
Cdd:pfam09730 292 Q-KQLEQAKGALSEQQEKVNRLTENLEAMRGLQASKERQDALDSEKDRDSHED--------GDYYEVDINGPEILECKYR 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3662 ATMDEA--LSKQKEAEREMLNKQKEMQELEKKRLEQEKvlaeenKKLRDQLQQLEEAQKE 3719
Cdd:pfam09730 363 VAVEEAgeLREELKALKARYNTLEERYKEEKTRWEAEA------QDLAEKIRQLEKASHQ 416
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2551-2877 |
2.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2551 EQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQK 2630
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2631 KRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKT 2710
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2711 SKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEA 2790
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2791 EREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQ 2870
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
....*..
gi 1838104091 2871 RKQLEDE 2877
Cdd:COG4372 364 EAGVADG 370
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2522-2698 |
2.28e-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: 47.69 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2522 VSKREVAALDAENQKK-NIELELHELKKLSEQQINDKSQLVDDALQsrtKIEEEIHIIRIQLETtlnQKSTAETELKQLR 2600
Cdd:pfam05262 178 SDKKVVEALREDNEKGvNFRRDMTDLKERESQEDAKRAQQLKEELD---KKQIDADKAQQKADF---AQDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2601 EKAAEAERLRKLAQEEAEKLHKQVIEEtqKKRTAEEELKRKSEAEKEAAKQKQKALEDL-ENLKMQAEEAERKVKQAQIE 2679
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAEN--QKREIEKAQIEIKKNDEEALKAKDHKAFDLkQESKASEKEAEDKELEAQKK 329
|
170 180
....*....|....*....|....
gi 1838104091 2680 KEK-----QIQIAHVAAEKSATAE 2698
Cdd:pfam05262 330 REPvaedlQKTKPQVEAQPTSLNE 353
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2589-2661 |
2.32e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 44.35 E-value: 2.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 2589 KSTAETELKQLREkaaEAERLRKLAQEEAEKLHKQVIEEtqkkrtAEEELKR-KSEAEKEAAKQKQKALEDLEN 2661
Cdd:cd06503 53 LAEYEEKLAEARA---EAQEIIEEARKEAEKIKEEILAE------AKEEAERiLEQAKAEIEQEKEKALAELRK 117
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3459-3677 |
2.33e-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: 47.64 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3459 LEDKELMQKRLDEETEEyQKSLEAERKRQleivAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARlleteiatkd 3538
Cdd:pfam15709 328 REQEKASRDRLRAERAE-MRRLEVERKRR----EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLR---------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3539 kstvMQQLEVERRNNSKEAddlRNAIANLETEKARLKKDAEELQNKSKEMaDAQMKQIEHEKTMLQQTFLTEKEMLLKKE 3618
Cdd:pfam15709 393 ----KQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRKLQEL-QRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3619 --RLIE-DEKKRLESQYEEEAKKAKALTDEQERQRKlmEEEKKKLhaTMDEALSKQKEAERE 3677
Cdd:pfam15709 465 qkRLMEmAEEERLEYQRQKQEAEEKARLEAEERRQK--EEEAARL--ALEEAMKQAQEQARQ 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2734-3071 |
2.48e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2734 LKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEK 2813
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2814 ELERqrkvadstaqqkltAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILiQLKS 2893
Cdd:COG4372 109 EAEE--------------LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL-EQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2894 RAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEA 2973
Cdd:COG4372 174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2974 EIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKL 3053
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
330
....*....|....*...
gi 1838104091 3054 NFEKASSGKLDLELELNK 3071
Cdd:COG4372 334 ILLAELADLLQLLLVGLL 351
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2581-2701 |
2.59e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2581 QLETTLNQKSTAETELKQLREKAAeaerlRKLAQEEAEKLhKQVIEETQKKRTAEEELKRKSEAEKEAAKQK-QKALEDL 2659
Cdd:COG2268 213 EIAIAQANREAEEAELEQEREIET-----ARIAEAEAELA-KKKAEERREAETARAEAEAAYEIAEANAEREvQRQLEIA 286
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1838104091 2660 E---NLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQS 2701
Cdd:COG2268 287 ErerEIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEA 331
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2471-2665 |
2.82e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 47.17 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2471 AAKILKAEEQKKMADLQAELDKQ--KKLAEAHAKAIAK-AEKEADELKHQMKQEVskREVAALDAENQKKNIELELHELK 2547
Cdd:PRK00106 23 SIKMKSAKEAAELTLLNAEQEAVnlRGKAERDAEHIKKtAKRESKALKKELLLEA--KEEARKYREEIEQEFKSERQELK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2548 KLsEQQINDKSQLVD---DALQSRTKIEEEIHIIRIQLETTLNQKstaETELKQL-REKAAEAERLRKLAQEEAEKLhkq 2623
Cdd:PRK00106 101 QI-ESRLTERATSLDrkdENLSSKEKTLESKEQSLTDKSKHIDER---EEQVEKLeEQKKAELERVAALSQAEAREI--- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838104091 2624 VIEETQKKRTaEEELKRKSEAEKEAAKQKQKALEDLENLKMQ 2665
Cdd:PRK00106 174 ILAETENKLT-HEIATRIREAEREVKDRSDKMAKDLLAQAMQ 214
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
3382-3687 |
2.84e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3382 AENMKRL-AKEAAILSVEsqeasrlRQIAEEDLVQQRALAEKMLKeKMQAIQEASR-LKAEAELLQRQKDLAQEQAQRLL 3459
Cdd:COG5022 806 LGSRKEYrSYLACIIKLQ-------KTIKREKKLRETEEVEFSLK-AEVLIQKFGRsLKAKKRFSLLKKETIYLQSAQRV 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3460 EDKELMQKRLDEETEE----YQKSLEAErKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRfKKQADNIAARLLETEia 3535
Cdd:COG5022 878 ELAERQLQELKIDVKSisslKLVNLELE-SEIIELKKSLSSDLIENLEFKTELIARLKKLLN-NIDLEEGPSIEYVKL-- 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3536 tkdksTVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMAdaqmkqieheKTMLQQTFLTEKEMLL 3615
Cdd:COG5022 954 -----PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA----------ELSKQYGALQESTKQL 1018
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3616 KKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKklHATMDEALSKQKEAEREMLnKQKEMQE 3687
Cdd:COG5022 1019 KELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQ--LQARYKALKLRRENSLLDD-KQLYQLE 1087
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
3495-3720 |
3.08e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3495 EKLKLQVSQLSVAQAKAEEEAKRFKKQADNiaarLLETEiatKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKARL 3574
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDE----LVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3575 KkdaeelqnkskemadAQMKQIEHEKTMLQ---------QTFLTEKEMLLKkerlIEDEKKRLESQYEEEAKkakALTDE 3645
Cdd:PHA02562 268 K---------------SKIEQFQKVIKMYEkggvcptctQQISEGPDRITK----IKDKLKELQHSLEKLDT---AIDEL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3646 QERQRKLMEEEKKKLhaTMDEALSKQKEA----EREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:PHA02562 326 EEIMDEFNEQSKKLL--ELKNKISTNKQSlitlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5069-5103 |
3.15e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.15e-04
10 20 30
....*....|....*....|....*....|....*
gi 1838104091 5069 LLEAQAATGYVIDPIKNLKLTVLEAVRMGIVGPEF 5103
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2472-2949 |
3.21e-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: 47.44 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2472 AKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKREVAAldaENQKKNIELELHELKKLSE 2551
Cdd:pfam09731 73 SAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKAL---EEVLKEAISKAESATAVAK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2552 QQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQlrekaaEAERLRKLAQEEAEKLHKQVIEETQKK 2631
Cdd:pfam09731 150 EAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLK------EVINLAKQSEEEAAPPLLDAAPETPPK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2632 RTAEEElkrKSEAEKEAAKQKQKALEDLENLkmqaEEAERKVKQAQIEKeKQIQIAHVAAEKSATaelqstqrsfveKTS 2711
Cdd:pfam09731 224 LPEHLD---NVEEKVEKAQSLAKLVDQYKEL----VASERIVFQQELVS-IFPDIIPVLKEDNLL------------SND 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2712 KLEESLKQEHGTVLQLQQEAAHLKKQ-QEDALKAREEAEKELDKwrqkANEALRLRLQAEEEAHKKSLaqeeaekqkeea 2790
Cdd:pfam09731 284 DLNSLIAHAHREIDQLSKKLAELKKReEKHIERALEKQKEELDK----LAEELSARLEEVRAADEAQL------------ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2791 erEAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKL-TAEQELIRLRAEF--DNAEQQRSLLE---DELYRLKNEV 2864
Cdd:pfam09731 348 --RLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLvEQEIELQREFLQDikEKVEEERAGRLlklNELLANLKGL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2865 IAAQQQRKQLEDELAKMRSemeilIQLKSRAEKETM--SNTEKSKMLLDAEASKMRDVAEEAGKLRAIAE---EAKYQRQ 2939
Cdd:pfam09731 426 EKATSSHSEVEDENRKAQQ-----LWLAVEALRSTLedGSADSRPRPLVRELKALKELASDDEVVKAALAslpEEAYQRG 500
|
490
....*....|
gi 1838104091 2940 IAEEEAARQR 2949
Cdd:pfam09731 501 VYTEAALRER 510
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2466-2684 |
3.31e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2466 EDEEKAAKILKAeeqkkMADLQAELDKQKKLAEAhAKAIAKAEKEADELKHQMKQevSKREVAALDAENQ----KKNIEL 2541
Cdd:COG3206 145 PDPELAAAVANA-----LAEAYLEQNLELRREEA-RKALEFLEEQLPELRKELEE--AEAALEEFRQKNGlvdlSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2542 ELHELKKLSEQQINDKSQLVD-----DALQSRTKIEEEIHIIRIQ---LETTLNQKSTAETELKQLRE---------KAA 2604
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEaearlAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSArytpnhpdvIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2605 EAER--LRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAER-------KVKQ 2675
Cdd:COG3206 297 RAQIaaLRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElyesllqRLEE 376
|
....*....
gi 1838104091 2676 AQIEKEKQI 2684
Cdd:COG3206 377 ARLAEALTV 385
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2601-2917 |
3.34e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2601 EKAAEAERLRKlAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLK---MQAEEAERKVKQAQ 2677
Cdd:pfam02029 4 EEEAARERRRR-AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLdrtAKREERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2678 IEKEKQIQIAHVAAEKS--------ATAELQSTQRsfvEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAE 2749
Cdd:pfam02029 83 LERQKEFDPTIADEKESvaerkennEEEENSSWEK---EEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2750 KELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAER----EAKKRAKAEESALKQKEMAEKELERQRKVADST 2825
Cdd:pfam02029 160 EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRghpeVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2826 AQQKLTAEQELIRLR--------AEFDNAEQQRSLLEDELYRLKNEviaAQQQRKQLEDELAKMRSEmeiliqlksRAEK 2897
Cdd:pfam02029 240 AEVFLEAEQKLEELRrrrqekesEEFEKLRQKQQEAELELEELKKK---REERRKLLEEEEQRRKQE---------EAER 307
|
330 340
....*....|....*....|
gi 1838104091 2898 ETMSNTEKSKMLLDAEASKM 2917
Cdd:pfam02029 308 KLREEEEKRRMKEEIERRRA 327
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
3059-3691 |
3.42e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3059 SSGKLDLELELNKLKNIAEETQQSKLRAEEEAE-KQRKLAMEEEKRRREAEETVKKITAAEK-EAGRQRKI-AQDELDRL 3135
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEkKASALKRQLDRESDRNQELQKRIRLLEKrEAEAEEALrEQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3136 KKKAEEA--RKQKDKADSEAEKQIVaasQAALKCRTAEQQVQSVLAQQKEDSMMHKK--LQQEYEkakklakeaeaakek 3211
Cdd:pfam05557 81 KKKYLEAlnKKLNEKESQLADAREV---ISCLKNELSELRRQIQRAELELQSTNSELeeLQERLD--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3212 aekeavLLRKQAEEAEsqkaAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAEnaalEQKKKADAEMAKHKKLaeQTLK 3291
Cdd:pfam05557 143 ------LLKAKASEAE----QLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS----EIVKNSKSELARIPEL--EKEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3292 QKFQVEQEltkvklKLDDTDKQKDLLDDELQRLKDEVDDAVKQRgqveEELFKVKVQMEEL---LKVKLKIEKENQLLIK 3368
Cdd:pfam05557 207 ERLREHNK------HLNENIENKLLLKEEVEDLKRKLEREEKYR----EEAATLELEKEKLeqeLQSWVKLAQDTGLNLR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3369 KDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKmqaiqeasRLKAEAELLQRQK 3448
Cdd:pfam05557 277 SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK--------RHKALVRRLQRRV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3449 DLAQEQAQRLLEDKELMQKRLDEETEEYQKSleaerKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADniaar 3528
Cdd:pfam05557 349 LLLTKERDGYRAILESYDKELTMSNYSPQLL-----ERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQ----- 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3529 LLETEIATKDKstvmQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQnkskemadaqmkqIEHEKTMLQQTFL 3608
Cdd:pfam05557 419 TLERELQALRQ----QESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELE-------------MELERRCLQGDYD 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3609 tekemlLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQEL 3688
Cdd:pfam05557 482 ------PKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESA 555
|
...
gi 1838104091 3689 EKK 3691
Cdd:pfam05557 556 ELK 558
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3353-3525 |
3.46e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3353 LKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQ 3432
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3433 EA-SRLKAEAELLQRQKDLAQEQAQRLLEDKEL--MQKRLDEETEEYQKSLEAERKRQ--------------------LE 3489
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQeelkvgdevkylslgqkgevLS 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1838104091 3490 IVAEAE--------KLKLQVSQLSVAQAKAEEEAKRFKKQADNI 3525
Cdd:PRK00409 657 IPDDKEaivqagimKMKVPLSDLEKIQKPKKKKKKKPKTVKPKP 700
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3419-3795 |
3.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3419 LAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEE---YQKSLEAERKRQLEIVAEAE 3495
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3496 KLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLleteiatkdkstvmQQLEVERRNNSKEADDLRNAIANLETEKARLK 3575
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL--------------EELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3576 KDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEE 3655
Cdd:COG4372 150 EELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3656 EKKKLHATMDEALSKQKEAER-EMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVETTK 3734
Cdd:COG4372 230 KLGLALSALLDALELEEDKEElLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3735 NVYNGQNAGDVVDSVENKPDPLSFDGIRDKVPASRLRDVGLLSKKEFDKLKKGKATVQQLG 3795
Cdd:COG4372 310 IGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
3299-3787 |
3.70e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3299 ELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAvkqrgqveEELFKVKVQMEELLKVKLKIE-----KENQLLIKKDKDK 3373
Cdd:TIGR01612 1356 KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKS--------EKLIKKIKDDINLEECKSKIEstlddKDIDECIKKIKEL 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3374 AQQLLAEEAeNMKRLAKEAAilsvESQEASRL--RQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLA 3451
Cdd:TIGR01612 1428 KNHILSEES-NIDTYFKNAD----ENNENVLLlfKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3452 QEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLE--------IVAEAEKLKlqvSQLSVAQAKAEEEAKRFKKQAD 3523
Cdd:TIGR01612 1503 DKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAktkkdseiIIKEIKDAH---KKFILEAEKSEQKIKEIKKEKF 1579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3524 NIaarllETEIATKDKST---VMQQLEVER-RNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKemaDAQMKQIEHE 3599
Cdd:TIGR01612 1580 RI-----EDDAAKNDKSNkaaIDIQLSLENfENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQ---DTELKENGDN 1651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3600 KTMLQqTFLtekEMLLKKERLIEDEKKRLESqyeeeakkakaLTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREML 3679
Cdd:TIGR01612 1652 LNSLQ-EFL---ESLKDQKKNIEDKKKELDE-----------LDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEI 1716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3680 NKQKEMQELEKKRL------------EQEKVLAEENKKLRDQLQQ-----------LEEAQKE-------KNTQVisAAT 3729
Cdd:TIGR01612 1717 ESIKELIEPTIENLissfntndlegiDPNEKLEEYNTEIGDIYEEfielyniiagcLETVSKEpitydeiKNTRI--NAQ 1794
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3730 VETTKNVYNGQNAGDVVDSVENKpdplSFDGIRDKVpASRLRDVGLLSKKEFDKLKKG 3787
Cdd:TIGR01612 1795 NEFLKIIEIEKKSKSYLDDIEAK----EFDRIINHF-KKKLDHVNDKFTKEYSKINEG 1847
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3309-3498 |
3.71e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3309 DTDKQKDLLDdeLQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLK--VKLKIEKENqllIKKDKDKAQQLLAEEAENMK 3386
Cdd:COG1579 2 MPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEArlEAAKTELED---LEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3387 RLakEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEAsrlkaeaellqrQKDLAQEQAQRlledkELMQ 3466
Cdd:COG1579 77 KY--EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEEL------------EEELAELEAEL-----AELE 137
|
170 180 190
....*....|....*....|....*....|..
gi 1838104091 3467 KRLDEETEEYQKSLEAERKRQLEIVAEAEKLK 3498
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3112-3494 |
3.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3112 KKITAAEKEAGRQRKIaQDELDRLKKKAEEARKQKDKADSEAEK--QIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHK 3189
Cdd:COG4717 78 EELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3190 KLQQEYEKAKKLAKEAEAAkekaekeavllrkQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEF--EAAKRAQAENA 3267
Cdd:COG4717 157 ELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEELQQRLAEleEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3268 ALEQKKKADAEMAKHKKLAEQTLKQKF--------------------------------------------QVEQELTKV 3303
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3304 KLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKvkvQMEELLKVKLKIEK-ENQLLIKKDKDKAQQLLA--- 3379
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD---RIEELQELLREAEElEEELQLEELEQEIAALLAeag 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3380 ----EEAENMKRLAKEAAILSVESQEAS-RLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAE--AELLQRQKDLAQ 3452
Cdd:COG4717 381 vedeEELRAALEQAEEYQELKEELEELEeQLEELLGELEELLEALDEEELEEELEELEEELEELEEelEELREELAELEA 460
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1838104091 3453 EQAQrLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEA 3494
Cdd:COG4717 461 ELEQ-LEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4168-4200 |
3.95e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.95e-04
10 20 30
....*....|....*....|....*....|...
gi 1838104091 4168 LEAQAGTGYVVDPVNNQKYTVDEAVKAGVVGPE 4200
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2581-2753 |
4.17e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2581 QLETTLNQKSTAETE-LKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAE-KEAAKQKQKALED 2658
Cdd:PRK09510 87 QQAEELQQKQAAEQErLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEaKRAAAAAKKAAAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2659 LEnlKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQ 2738
Cdd:PRK09510 167 AK--KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA 244
|
170
....*....|....*.
gi 1838104091 2739 EDALKA-REEAEKELD 2753
Cdd:PRK09510 245 KAAEKAaAAKAAAEVD 260
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2212-2678 |
4.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2212 VEMVIRNTQGA-EGVLKQYEDclrevhtvpsdaKEVESYRAKLKKMRAEAEGEQPVFDSLEEELQKATTVSEKMSRV--- 2287
Cdd:PRK02224 178 VERVLSDQRGSlDQLKAQIEE------------KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVlee 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2288 HSERDIELDHFRQNVSGLQDRWKAVFTQMEIRHRELEQLGRQLGYYHESYDWLIHW-------ITDAKERQEKIQAVSIT 2360
Cdd:PRK02224 246 HEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2361 DSKTLKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQLVAYNAKADPHAS-------------------PL 2421
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREeieeleeeieelrerfgdaPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2422 KKNKMDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRL------------EDEEKAAKILKAEEQKkmADLQAE 2489
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgqpvEGSPHVETIEEDRERV--EELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2490 L----DKQKKLAEAH--AKAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKNIElELHElkklseqqinDKSQLVDD 2563
Cdd:PRK02224 484 LedleEEVEEVEERLerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE-ELRE----------RAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2564 ALQSRTKIEEEIHIIRIQLET--TLNQKSTAETE----LKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEE 2637
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEvaELNSKLAELKEriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 2638 LKRKSEAE--------KEAAKQKQKALEDLENL--KMQAEEAERKVKQAQI 2678
Cdd:PRK02224 633 RERKRELEaefdeariEEAREDKERAEEYLEQVeeKLDELREERDDLQAEI 683
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2922-3166 |
4.49e-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: 46.43 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2922 EEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERI---LKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQR 2998
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQrreLESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2999 KALEDEANQHKKEIEEKIVQLKKSSQ---AEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNI 3075
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLereTELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3076 AEETQQSKLRAEEEAEK-QRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQdeldrLKKKAEEARKQKDKADSEAE 3154
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTlTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG-----LGEELSSMAAQRDRTQAELH 275
|
250
....*....|..
gi 1838104091 3155 KQIVAASQAALK 3166
Cdd:pfam07888 276 QARLQAAQLTLQ 287
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2890-3035 |
4.60e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.40 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2890 QLKSRAEKETmSNTEKSKMLLDAEASKMRDVAEEAgklraiAEEAKYQRQIAEEEA--------ARQRAEAERILKEKLA 2961
Cdd:COG2268 196 EIIRDARIAE-AEAERETEIAIAQANREAEEAELE------QEREIETARIAEAEAelakkkaeERREAETARAEAEAAY 268
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 2962 AISEAtrlKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVD 3035
Cdd:COG2268 269 EIAEA---NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3312-3722 |
4.80e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3312 KQKDLLDDELQRLKDEVDDAV----KQRGQVEEELFKVKVQMEELLKVK--LKIEKENQLLIKKDKDKAQQLLAEEAENM 3385
Cdd:PRK01156 124 ISKDVFLNSIFVGQGEMDSLIsgdpAQRKKILDEILEINSLERNYDKLKdvIDMLRAEISNIDYLEEKLKSSNLELENIK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3386 KRLAKEAAILSV---ESQEASRLRQIAEEDLVQqralAEKMLKEKMQAIQEASRLkaEAELLQRQKDLA----------- 3451
Cdd:PRK01156 204 KQIADDEKSHSItlkEIERLSIEYNNAMDDYNN----LKSALNELSSLEDMKNRY--ESEIKTAESDLSmeleknnyyke 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3452 -QEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEE--EAKRFKKQADNIAAR 3528
Cdd:PRK01156 278 lEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDyiKKKSRYDDLNNQILE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3529 LLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLeteKARLKKDAEELqNKSKEMADAQMKQIEHEKTMLQQTF- 3607
Cdd:PRK01156 358 LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI---LKIQEIDPDAI-KKELNEINVKLQDISSKVSSLNQRIr 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3608 -LTEKEMLLKKE---------------RLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLhATMDEALSKQ 3671
Cdd:PRK01156 434 aLRENLDELSRNmemlngqsvcpvcgtTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDL-KKRKEYLESE 512
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3672 KEAEREmlnkqKEMQELEKKRLEQEKVLAEENkKLRDQLQQLEEAQKEKNT 3722
Cdd:PRK01156 513 EINKSI-----NEYNKIESARADLEDIKIKIN-ELKDKHDKYEEIKNRYKS 557
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2802-2992 |
5.10e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2802 ESALKQKEMAEKELERQRKVADsTAQQKLTA---EQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDEL 2878
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2879 AKMRSEMEILIQ---LKSRAEKETMSNTEKSKML--LDAEASKMRDVAEEAGKLRA-IAEEAkyQRQIAEEEAARQRAEA 2952
Cdd:COG3206 250 GSGPDALPELLQspvIQQLRAQLAELEAELAELSarYTPNHPDVIALRAQIAALRAqLQQEA--QRILASLEAELEALQA 327
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1838104091 2953 -ERILKEKLAAISEATRlkteaeiALKEKEAENERLRRAAE 2992
Cdd:COG3206 328 rEASLQAQLAQLEARLA-------ELPELEAELRRLEREVE 361
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3409-3720 |
5.10e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.61 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3409 AEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLledkelmqKRLDEETEEYQKSLE--AERKR 3486
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKV--------KKLEATVETYKKKLEdlGDLRR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3487 QLEIVAEAEKLKLQVSqlsvaqAKAEEEAKR----------FKKQADNIAARLLETEIATKDKSTVMQQLEV-------E 3549
Cdd:pfam05622 153 QVKLLEERNAEYMQRT------LQLEEELKKanalrgqletYKRQVQELHGKLSEESKKADKLEFEYKKLEEklealqkE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3550 RRNNSKEADDLRNAI----------ANLETEKARLKKDAEELQNKSKEMADAQMK----QIEHEKTMLQ-QTFLTEKEML 3614
Cdd:pfam05622 227 KERLIIERDTLRETNeelrcaqlqqAELSQADALLSPSSDPGDNLAAEIMPAEIRekliRLQHENKMLRlGQEGSYRERL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3615 LKKERLIEDEKKRLEsQYEEEAKKAKALTDE-----QERQRKLMEEEKKklhaTMDEALSKQK-EAEREMLNKQKEmqEL 3688
Cdd:pfam05622 307 TELQQLLEDANRRKN-ELETQNRLANQRILElqqqvEELQKALQEQGSK----AEDSSLLKQKlEEHLEKLHEAQS--EL 379
|
330 340 350
....*....|....*....|....*....|..
gi 1838104091 3689 EKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:pfam05622 380 QKKKEQIEELEPKQDSNLAQKIDELQEALRKK 411
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2601-2833 |
5.11e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.14 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2601 EKAAEAERlRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEK 2680
Cdd:NF012221 1564 KERAEADR-QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAGES 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2681 EKQ------------IQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQeaaHLKKQQEDALKAREEA 2748
Cdd:NF012221 1643 GDQwrnpfagglldrVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQ---NQANAEQDIDDAKADA 1719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2749 EKeldkwRQKanEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAK-KRAKAEESALKQKEMAEKELERQRKVADSTAQ 2827
Cdd:NF012221 1720 EK-----RKD--DALAKQNEAQQAESDANAAANDAQSRGEQDASAAEnKANQAQADAKGAKQDESDKPNRQGAAGSGLSG 1792
|
....*.
gi 1838104091 2828 QKLTAE 2833
Cdd:NF012221 1793 KAYSVE 1798
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2445-2677 |
5.16e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.75 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2445 SELMTLTSQYIKFITE---TQRRLEDEEKAakilKAEEQKkmadlqAELDKQKKLAeahakAIAKAEKEADELKHQMKQE 2521
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERA----EADRQR------LEQEKQQQLA-----AISGSQSQLESTDQNALET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2522 VSKREVAALDAENQKKNIELE--LHELKKLSEQQIND-------KSQLVDDALQS-RTKIEEEIHIIRIQLEttlNQKST 2591
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTtlAQGLDALDSQATYAgesgdqwRNPFAGGLLDRvQEQLDDAKKISGKQLA---DAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2592 AETELKQLREKAAEAErlrkLAQEEAEKLHKQVIEETQKKRTAEEelKRKSEA---EKEAAKQKQKALEDLENLKMQAEE 2668
Cdd:NF012221 1680 HVDNQQKVKDAVAKSE----AGVAQGEQNQANAEQDIDDAKADAE--KRKDDAlakQNEAQQAESDANAAANDAQSRGEQ 1753
|
250
....*....|...
gi 1838104091 2669 ----AERKVKQAQ 2677
Cdd:NF012221 1754 dasaAENKANQAQ 1766
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2639-3050 |
5.17e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2639 KRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVK-QAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESL 2717
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2718 KQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALR-----LRLQAEEE---AHKKSLAQEEAEKQKEE 2789
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkaeeeAKRKAEEErkaAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2790 AEREAKKRAKAEESALKQKEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQ 2869
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2870 QRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQR 2949
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2950 AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQR 3029
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420
....*....|....*....|.
gi 1838104091 3030 QKAMVDDTLKQRRVVEEEIRI 3050
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELR 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3406-3716 |
5.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3406 RQIAEedLVQQRALAEKMLKEkmqAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQkrLDEETEEyqksLEAER- 3484
Cdd:COG4913 610 AKLAA--LEAELAELEEELAE---AEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAE----LEAELe 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3485 ------------KRQLE-IVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLletEIATKDKSTVMQQLEVERR 3551
Cdd:COG4913 679 rldassddlaalEEQLEeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3552 NNSKEADDLRNAIANLETEKARLKkdaEELQNKSKEMADAqMKQIEHEKTMLQQTFLTEKE-------ML--LKKERLIE 3622
Cdd:COG4913 756 AAALGDAVERELRENLEERIDALR---ARLNRAEEELERA-MRAFNREWPAETADLDADLEslpeylaLLdrLEEDGLPE 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3623 dekkrlesqYEEEAKkakaltdeqERQRKLMEEEKKKLHATMDEALskqKEAEREM--LN---KQKEMQELEKKRLEQEK 3697
Cdd:COG4913 832 ---------YEERFK---------ELLNENSIEFVADLLSKLRRAI---REIKERIdpLNdslKRIPFGPGRYLRLEARP 890
|
330
....*....|....*....
gi 1838104091 3698 VLAEENKKLRDQLQQLEEA 3716
Cdd:COG4913 891 RPDPEVREFRQELRAVTSG 909
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3555-3741 |
5.56e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3555 KEADD-LRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYE 3633
Cdd:PRK12704 38 EEAKRiLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3634 EEAKKAKALTDEQERQRKLMEEEKKKLHA----TMDEAlskqkeaeREMLNKQKEmQELEKKRLEQEKVLAEENKklrdq 3709
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERisglTAEEA--------KEILLEKVE-EEARHEAAVLIKEIEEEAK----- 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1838104091 3710 lqqlEEAQKEKNTQVISA-------ATVETTKNVYNGQN 3741
Cdd:PRK12704 184 ----EEADKKAKEILAQAiqrcaadHVAETTVSVVNLPN 218
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3840-3873 |
5.57e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 5.57e-04
10 20 30
....*....|....*....|....*....|....
gi 1838104091 3840 LLEAQAATGYMLDPIKNKKLSVNEAVKEGLIGPE 3873
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2605-2962 |
6.00e-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: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2605 EAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQI 2684
Cdd:pfam15709 164 TPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2685 QIAhvaAEKSATAELQSTQ------------RSFVEKTSKLEESLKQEHGTVLQLQ----QEAAHLKKQQEDALKAREEA 2748
Cdd:pfam15709 244 EVA---AELSGPDVINSKEtedasergafssDSVVEDPWLSSKYDAEESQVSIDGRssptQTFVVTGNMESEEERSEEDP 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2749 EKELDKWRQKANEAlRLRLQAEEeAHKKSLAQEEAEKQkeeaeREAKKRAKAEESALKQKEMAEKELERQRKVadstaqq 2828
Cdd:pfam15709 321 SKALLEKREQEKAS-RDRLRAER-AEMRRLEVERKRRE-----QEEQRRLQQEQLERAEKMREELELEQQRRF------- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2829 kltaeqELIRLRAEFDNAEQQRSLLEDELYRLKNEviAAQQQRKQLEDELAKMrsemeiLIQLKSRAEKETMSNTEKSKM 2908
Cdd:pfam15709 387 ------EEIRLRKQRLEEERQRQEEEERKQRLQLQ--AAQERARQQQEEFRRK------LQELQRKKQQEEAERAEAEKQ 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 2909 LLDAEASKMrdvAEEAGKLRAIAEEAK--YQRQIAE-EEAARQRAEaERILKEKLAA 2962
Cdd:pfam15709 453 RQKELEMQL---AEEQKRLMEMAEEERleYQRQKQEaEEKARLEAE-ERRQKEEEAA 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2728-2949 |
6.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2728 QQEAAHLKKQQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQ 2807
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2808 KEMAEKELERQRKVADSTAQQK-----------LTAEQELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLED 2876
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 2877 ELAKMRSEMEILIQLKSRAEKeTMSNTEKSKMLLDAEASKMRDVAEEAGKL--RAIAEEAKYQRQIAEEEAARQR 2949
Cdd:COG4942 179 LLAELEEERAALEALKAERQK-LLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2694-2953 |
6.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2694 SATAELQSTQRSFVEKTSKLEESLKQehgtVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEAlrlrlQAEEEA 2773
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----EAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2774 HKKSLaqeeaekqkeeaereaKKRAKAE-------------------ESALKQKEMAEKELERQRKVADSTAQQKLTAEQ 2834
Cdd:COG3883 84 RREEL----------------GERARALyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2835 ELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEA 2914
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 1838104091 2915 SKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAE 2953
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2478-2674 |
6.50e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2478 EEQKKMADLQAELDKQKKLAeahaKAIAKAEKEADELKHQMKQEVSKREVAALDAENQK------KNIELELHELKKLSE 2551
Cdd:COG1340 82 ELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKelvekiKELEKELEKAKKALE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2552 Q--QINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQ 2629
Cdd:COG1340 158 KneKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838104091 2630 KKRTAEEELKRKSEAEKEAAKQKQKaledlENLKMQAEEAERKVK 2674
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKREKEK-----EELEEKAEEIFEKLK 277
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3381-3524 |
6.77e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.02 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3381 EAENMKRLAKEAAILSVESQEASRLRQI----AEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQK-------- 3448
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIaiaqANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAEtaraeaea 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3449 --DLAQEQAQRLLEdKELMQKRLDEETEEYQKSLEAERKRQLEIV---AEAEKLKLQV-----SQLSVAQAKAEEEAKRF 3518
Cdd:COG2268 267 ayEIAEANAEREVQ-RQLEIAEREREIELQEKEAEREEAELEADVrkpAEAEKQAAEAeaeaeAEAIRAKGLAEAEGKRA 345
|
....*.
gi 1838104091 3519 KKQADN 3524
Cdd:COG2268 346 LAEAWN 351
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2907-3039 |
7.12e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2907 KMLLDAEAS------KMRD-VAEEAGK---LRAIAEEAkyqrqiAEEEAARQRAEAErilkeklaAISEATRLKTEAEIA 2976
Cdd:PTZ00491 672 AELLEQEARgrlerqKMHDkAKAEEQRtklLELQAESA------AVESSGQSRAEAL--------AEAEARLIEAEAEVE 737
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 2977 LKEKEAENERLRRAAEDEAyQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVD----DTLK 3039
Cdd:PTZ00491 738 QAELRAKALRIEAEAELEK-LRKRQELELEYEQAQNELEIAKAKELADIEATKFERIVEalgrETLI 803
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2866-3013 |
7.42e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2866 AAQQQRKQLEDElAKMRSEMEILiqlKSRAEKEtmsntEKSKMLLDAEASKMrdVAEEAGKLRAIAEEAKYQRQI---AE 2942
Cdd:PTZ00491 667 AARHQAELLEQE-ARGRLERQKM---HDKAKAE-----EQRTKLLELQAESA--AVESSGQSRAEALAEAEARLIeaeAE 735
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 2943 EEAARQRAEAERILkeklaaiseatrlkTEAEIALKEKEAENE---RLRRAAEDEAYQRKALEDEANQHKKEIE 3013
Cdd:PTZ00491 736 VEQAELRAKALRIE--------------AEAELEKLRKRQELEleyEQAQNELEIAKAKELADIEATKFERIVE 795
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
3334-3582 |
7.52e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3334 QRGQVEEELFKVKV--QMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEA-SRLRQIAE 3410
Cdd:PHA02562 151 ARRKLVEDLLDISVlsEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKyDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3411 EDLVQQRALAEKMLKEKMQAI----------QEASRLKAEAELLQRQKDLAQEQ------AQRLLEDKELMQKrLDEETE 3474
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIEdpsaalnklnTAAAKIKSKIEQFQKVIKMYEKGgvcptcTQQISEGPDRITK-IKDKLK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3475 EYQKSLEAERKRQleivaeaEKLKLQVSQLSVAQAKAEEeakrFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNS 3554
Cdd:PHA02562 310 ELQHSLEKLDTAI-------DELEEIMDEFNEQSKKLLE----LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA 378
|
250 260
....*....|....*....|....*...
gi 1838104091 3555 KEADDLRNAIANLETEKARLKKDAEELQ 3582
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2344-2559 |
7.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2344 ITDAKERQEKIQAvsitdskTLKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQLVAYNAKADPHASPLKK 2423
Cdd:COG3883 25 LSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2424 NKMDSASDNII---QEYVTLRTRYSelmtltsqYIKFITETQRRLEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAH 2500
Cdd:COG3883 98 SGGSVSYLDVLlgsESFSDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 2501 AKAIAKAEKEADELKHQMKQEVSKREVAALDAENQKKNIELELHELKKLSEQQINDKSQ 2559
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
3219-3592 |
7.80e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3219 LRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFE-AAKRAQAENaaLEQKKKADAEMAKHKKLAEQTLKQKFQVe 3297
Cdd:pfam19220 74 LTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIElRDKTAQAEA--LERQLAAETEQNRALEEENKALREEAQA- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3298 qeltkvklklddtdkqkdlLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLkvklkieKENQLLIKKDKDKAQQL 3377
Cdd:pfam19220 151 -------------------AEKALQRAEGELATARERLALLEQENRRLQALSEEQA-------AELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3378 LAEEAenmkRLAKEAAILSVESQEASRLRQIAEEDLVQQRAlAEKMLKEKMQAIQE----ASRLKAEAELLQRQKDLAQE 3453
Cdd:pfam19220 205 DATRA----RLRALEGQLAAEQAERERAEAQLEEAVEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3454 QAQRLLEDKELMQKRLDEETEEyqksLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARlLETE 3533
Cdd:pfam19220 280 AAERRLKEASIERDTLERRLAG----LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIAS-LSDR 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3534 IAtkdksTVMQQLEVERrnnskeaddlrnaiANLETEKARLKkdaEELQNKSKEMADAQ 3592
Cdd:pfam19220 355 IA-----ELTKRFEVER--------------AALEQANRRLK---EELQRERAERALAQ 391
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2910-3040 |
8.02e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 43.24 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2910 LDAEASKMRDVAEEAGKLRAIAEEAK--YQRQIAE--EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENE 2985
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALaeYEEKLAEarAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQE 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 2986 RlRRAAEDeayqrkaLEDEANQHKKEIEEKIVQlkksSQAEMQRQKAMVDDTLKQ 3040
Cdd:COG0711 109 R-AKALAE-------LRAEVADLAVAIAEKILG----KELDAAAQAALVDRFIAE 151
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3590-3724 |
8.11e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3590 DAQMKQIEHEKTMLQQtfltEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMD---- 3665
Cdd:COG1579 16 DSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkey 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3666 EALSKQKE-AEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQV 3724
Cdd:COG1579 92 EALQKEIEsLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
3621-3727 |
8.15e-04 |
|
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: 42.60 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3621 IEDEKKRLES---QYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREM--LNKQKEMQELEKKRLEQ 3695
Cdd:pfam20492 4 AEREKQELEErlkQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKerLEESAEMEAEEKEQLEA 83
|
90 100 110
....*....|....*....|....*....|...
gi 1838104091 3696 EKV-LAEENKKLRDQLQQLEEAQKEKNTQVISA 3727
Cdd:pfam20492 84 ELAeAQEEIARLEEEVERKEEEARRLQEELEEA 116
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
3291-3482 |
8.38e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.88 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3291 KQKFQveQELT-KVKLKLDDTDKQ-----KDLLDDELQRLKDEVDDAVKQ---------------RGQVEEELFKVK--- 3346
Cdd:cd16269 88 DQKFQ--KKLMeQLEEKKEEFCKQneeasSKRCQALLQELSAPLEEKISQgsysvpggyqlyledREKLVEKYRQVPrkg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3347 VQMEELLKVKLK--------IEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEaailsvesQEASRLRQIAEEdlvQQRA 3418
Cdd:cd16269 166 VKAEEVLQEFLQskeaeaeaILQADQALTEKEKEIEAERAKAEAAEQERKLLE--------EQQRELEQKLED---QERS 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3419 LAE--KMLKEKMqaiqeasrlkaEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEA 3482
Cdd:cd16269 235 YEEhlRQLKEKM-----------EEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2867-2994 |
8.63e-04 |
|
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: 42.21 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2867 AQQQRKQLEDELAKMRSEMEiliqlksRAEKETMSNTEKSKMLldaeASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAA 2946
Cdd:pfam20492 4 AEREKQELEERLKQYEEETK-------KAQEELEESEETAEEL----EEERRQAEEEAERLEQKRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1838104091 2947 RQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDE 2994
Cdd:pfam20492 73 MEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
2910-3020 |
8.89e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 43.19 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2910 LDAEASKMRDVAEEAGKLRAIAEE--AKYQRQI--AEEEAARQRAEAERilkEKLAAISEAtRLKTE---------AE-- 2974
Cdd:PRK09173 31 LDARADRIKNELAEARRLREEAQQllAEYQRKRkeAEKEAADIVAAAER---EAEALTAEA-KRKTEeyvarrnklAEqk 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2975 IALKEKEAENErLRRAAEDEAYQ--RKALEDEANQHKKE--IEEKIVQLK 3020
Cdd:PRK09173 107 IAQAETDAINA-VRSSAVDLAIAaaEKLLAEKVDAKAASelFKDALAQVK 155
|
|
| 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 ... |
2942-3041 |
9.10e-04 |
|
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: 42.68 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2942 EEEAARQRAEAERILKEKLAAISEAtrlkteaEIALKEKEAENERLRRAAEDEAYQrkaledEANQHKKEIEEKIVQLKK 3021
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEA-------EQQLKEARAEAQEIIENAKKRAEK------LKEEIVAAAEAEAERIIE 98
|
90 100
....*....|....*....|
gi 1838104091 3022 SSQAEMQRQKAMVDDTLKQR 3041
Cdd:pfam00430 99 QAAAEIEQEKDRALAELRQQ 118
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
3571-3707 |
9.55e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.11 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3571 KARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQyEEEAKKAKALTDEQERQR 3650
Cdd:pfam05672 22 QAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE-EEAEEREQREQEEQERLQ 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 3651 KLMEEEKKKLhatmdealskQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLR 3707
Cdd:pfam05672 101 KQKEEAEAKA----------REEAERQRQEREKIMQQEEQERLERKKRIEEIMKRTR 147
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2817-3043 |
9.84e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2817 RQRKVA-DSTAQQKLTAEQEliRLRAEFDNAEQQRSLLEDELyRLKNeviAAQQQRKQLEDELAkmrsemEILIQLKSRA 2895
Cdd:PRK05035 432 RQAKAEiRAIEQEKKKAEEA--KARFEARQARLEREKAAREA-RHKK---AAEARAAKDKDAVA------AALARVKAKK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2896 EKETMSNTEKSKMLLD----AEASKMRDVAEEAGKLRAIAEEAKYQRQiAEEEAARQRAEAERILKEKLAAISEATRLKT 2971
Cdd:PRK05035 500 AAATQPIVIKAGARPDnsavIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 2972 EAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDtlKQRRV 3043
Cdd:PRK05035 579 KAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP--RKAAV 648
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2846-3034 |
1.02e-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: 44.15 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2846 AEQQRSLLEdeLYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKEtmsntekskmlLDAEASKMRDVAEEAG 2925
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-----------LEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2926 KLRAiaEEAKYQRQIAEEEAARqraEAERILKEklaaISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEA 3005
Cdd:COG1579 70 EVEA--RIKKYEEQLGNVRNNK---EYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180
....*....|....*....|....*....
gi 1838104091 3006 NQHKKEIEEKIVQLKKSSQAEMQRQKAMV 3034
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELA 169
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
3604-3719 |
1.02e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.31 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3604 QQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKaKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAE-REMLNK- 3681
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQR-KARQQTKKREESHKQKAAESASKSLAKPERKVSQEEaKEVLQEw 147
|
90 100 110
....*....|....*....|....*....|....*....
gi 1838104091 3682 -QKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKE 3719
Cdd:pfam13904 148 eRKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3422-3535 |
1.03e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 43.41 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3422 KMLKEK----MQAIQEA-SRLK-AEAELLQRQKDL--AQEQAQRLLEDKELMQKRLDEETEEyQKSLEAERKRQ---LEI 3490
Cdd:PRK07352 46 KILEERreaiLQALKEAeERLRqAAQALAEAQQKLaqAQQEAERIRADAKARAEAIRAEIEK-QAIEDMARLKQtaaADL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1838104091 3491 VAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIA 3535
Cdd:PRK07352 125 SAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3417-3650 |
1.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3417 RALAEKMLKEKMQAIqEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRldEETEEYQKSLEAERKRQLEIVAEAEK 3496
Cdd:COG4717 44 RAMLLERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ--EELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3497 LKLQVSQLSVAQ--AKAEEEAKRFKKQADNIAARLLETEiatkdkstvmqqleverrnnskeadDLRNAIANLETEKARL 3574
Cdd:COG4717 121 LEKLLQLLPLYQelEALEAELAELPERLEELEERLEELR-------------------------ELEEELEELEAELAEL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3575 KKDAEELQNKSKEMADAQMKQIEHEKTMLQQtfltEKEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQR 3650
Cdd:COG4717 176 QEELEELLEQLSLATEEELQDLAEELEELQQ----RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3144-3330 |
1.08e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3144 KQKDKADSEAEKQIVAASQAA--LKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAKEA-EAAKEKAEKEAVLL- 3219
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEelQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQaEEAAAKAAAAAKAKa 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3220 ---RKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAE---NAALEQKKKADAEmAKHKKLAEqtlkQK 3293
Cdd:PRK09510 150 eaeAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEakkKAEAEAKKKAAAE-AKKKAAAE----AK 224
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838104091 3294 FQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDD 3330
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2269-2666 |
1.11e-03 |
|
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: 45.83 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2269 SLEEELQKATTVSEKMSRVHSERDIELDHFRQNVSGLQDRWKAVFTQMEIRHRELEQLGRQLgyyhesydwlihwitdAK 2348
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE----------------EK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2349 ERQEkiqavsitdsktLKEQLSQEKKLLEEIENNKENVDECQKYAKAYINSIKDYELQLVAYNAKADPHASPLKKNKMDS 2428
Cdd:TIGR02169 735 LKER------------LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2429 asdniIQEYVT---LRTRYSELMTLTSQYIKFITETQRR-LEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAI 2504
Cdd:TIGR02169 803 -----LEEEVSrieARLREIEQKLNRLTLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2505 -------AKAEKEADELKHQMKQEVSKREVAALDAENQKKNIELELHELKKLSEQQindksqlvdDALQSRTKIEEEIHI 2577
Cdd:TIGR02169 878 rdlesrlGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL---------SEIEDPKGEDEEIPE 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2578 IRIQLETtlnqkstaeteLKQLREKAaeAERLRKLaqEEAEKLHKQVIEETQKKRtaeEELKRKSEAEKEAAKQKQKALE 2657
Cdd:TIGR02169 949 EELSLED-----------VQAELQRV--EEEIRAL--EPVNMLAIQEYEEVLKRL---DELKEKRAKLEEERKAILERIE 1010
|
....*....
gi 1838104091 2658 DLENLKMQA 2666
Cdd:TIGR02169 1011 EYEKKKREV 1019
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3368-3517 |
1.16e-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: 45.38 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3368 KKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEAsrlrQIAEEDLVQQRALAEKMLKEKMQAIQeasrlKAEAELLQRQ 3447
Cdd:pfam05262 219 KEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK----QQEAKNLPKPADTSSPKEDKQVAENQ-----KREIEKAQIE 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3448 KDLAQEQAQRLLEDK--ELMQKRLDEETEEYQKSLEAERKRqLEIVAEAEKLKLQVSqlsvAQAKAEEEAKR 3517
Cdd:pfam05262 290 IKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQVE----AQPTSLNEDAI 356
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2595-2687 |
1.17e-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: 44.59 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAAEAERLRklAQEEAEKLhKQVIEETQKKRTAEEE-LKRKSEAEKEAAKQKQKALEDLE--NLKMQAEEAER 2671
Cdd:cd03406 183 QHQKVVEKEAETERKR--AVIEAEKD-AEVAKIQMQQKIMEKEaEKKISEIEDEMHLAREKARADAEyyRALREAEANKL 259
|
90
....*....|....*.
gi 1838104091 2672 KVKQAQIEKEKQIQIA 2687
Cdd:cd03406 260 KLTPEYLELKKYQAIA 275
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3367-3531 |
1.18e-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: 44.15 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3367 IKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKmLKEKMQAIQEASRLKAeaelLQR 3446
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNKEYEA----LQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3447 QKDlAQEQAQRLLEDKEL-MQKRLDEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLsvaQAKAEEEAKRFKKQADNI 3525
Cdd:COG1579 97 EIE-SLKRRISDLEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL---EAELEELEAEREELAAKI 172
|
....*.
gi 1838104091 3526 AARLLE 3531
Cdd:COG1579 173 PPELLA 178
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3392-3595 |
1.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3392 AAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDE 3471
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3472 ETEEYQKSLEAERKRQ-----LEIVAEAEKLK------LQVSQLSVAQAKAEEEAKRFKKQADNIAARLletEIATKDKS 3540
Cdd:COG3883 84 RREELGERARALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADLLEELKADKAELEAKKAEL---EAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 3541 TVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQ 3595
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2597-2697 |
1.22e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.85 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2597 KQLREKAAEAERLRKLAqEEAEKLHKQVIEETQKKRTAeeelkRKSEAEKEAAKQKQKALEDLEnlkmqaEEAERKVKQA 2676
Cdd:COG0711 34 EKIADGLAEAERAKEEA-EAALAEYEEKLAEARAEAAE-----IIAEARKEAEAIAEEAKAEAE------AEAERIIAQA 101
|
90 100
....*....|....*....|...
gi 1838104091 2677 Q--IEKEKQIQIAHVAAEKSATA 2697
Cdd:COG0711 102 EaeIEQERAKALAELRAEVADLA 124
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3396-3517 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3396 SVESQEASRLRQIAEEDLVQQRALAEKMLKEKM-QAIQEASRLKAEAE--LLQRQKDLaQEQAQRLLEDKELMQKRLD-- 3470
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALlEAKEEIHKLRNEFEkeLRERRNEL-QKLEKRLLQKEENLDRKLEll 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 3471 -----------EETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKA------EEEAKR 3517
Cdd:PRK12704 106 ekreeelekkeKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEillekvEEEARH 169
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3399-3720 |
1.31e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3399 SQEASRLRQIAEEDLVQQRALAEKmlKEKMQAIQEA-SRLKAEAELLQRQKDLAQEQAQRLLEDKELMQK--RLDEETEE 3475
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTS--RRQLAAEQYRlVEMARELAELNEAESDLEQDYQAASDHLNLVQTalRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3476 YQKSLEAERKR---QLEIVAEAEKlklQVSQLSVAQAKAEEEAKRFKKQ-ADniaarlleteiatkdkstVMQQLEVERr 3551
Cdd:PRK04863 353 YQADLEELEERleeQNEVVEEADE---QQEENEARAEAAEEEVDELKSQlAD------------------YQQALDVQQ- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3552 nnsKEADDLRNAIANLETEKARLKKDAEELQNKSK--EMADAQMKQIEHEKTMLQQtfltekemllkKERLIEDEKkrle 3629
Cdd:PRK04863 411 ---TRAIQYQQAVQALERAKQLCGLPDLTADNAEDwlEEFQAKEQEATEELLSLEQ-----------KLSVAQAAH---- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3630 SQYEEEAKKAKALTDEQERqrklmEEEKKKLHATMDEALSKQKEAERE--MLNKQKEMQELEKKRLEQEKVLAEENKKLR 3707
Cdd:PRK04863 473 SQFEQAYQLVRKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547
|
330
....*....|....*....
gi 1838104091 3708 ------DQLQQLEEAQKEK 3720
Cdd:PRK04863 548 knlddeDELEQLQEELEAR 566
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2463-2562 |
1.32e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2463 RRLEDEEKAAKILKAEEQKKMADLQAELDKQK-KLAEAHAKAIAKAEKEADELKHQMK--QEVSKREVAALDAENQKKNI 2539
Cdd:PRK00409 537 EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLeEAEKEAQQAIKEAKKEADEIIKELRqlQKGGYASVKAHELIEARKRL 616
|
90 100
....*....|....*....|....*
gi 1838104091 2540 E--LELHELKKLSEQQINDKSQLVD 2562
Cdd:PRK00409 617 NkaNEKKEKKKKKQKEKQEELKVGD 641
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3879-3909 |
1.34e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|.
gi 1838104091 3879 LSAERAVVGYKDPYTGGKISVFEAMKKGLLE 3909
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2509-3031 |
1.35e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2509 KEADELKHQMKQEVSKREVAALDAENQKKNIELELHELKKLSEQqindksqlVDDALQSRTKIEEEIHIIRIQLETTLNQ 2588
Cdd:pfam05622 3 SEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQ--------LESGDDSGTPGGKKYLLLQKQLEQLQEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2589 KSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKK------RTAEEELKrKSEAEKEAAKQKqkaLEDLENL 2662
Cdd:pfam05622 75 NFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKdemdilRESSDKVK-KLEATVETYKKK---LEDLGDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2663 KMQA---EEAERKVKQAQIEKEKQIQIAHvaaekSATAELQSTQRSFVEKTSKL-EESLKQEhgtvlQLQQEAAHLKKQQ 2738
Cdd:pfam05622 151 RRQVkllEERNAEYMQRTLQLEEELKKAN-----ALRGQLETYKRQVQELHGKLsEESKKAD-----KLEFEYKKLEEKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2739 EDALKAREEAEKELDKWRQkANEALR-LRLQAEEEAHKKSLAQEEAEKQKEeaereakkrAKAEESALKQKEMAEKeLER 2817
Cdd:pfam05622 221 EALQKEKERLIIERDTLRE-TNEELRcAQLQQAELSQADALLSPSSDPGDN---------LAAEIMPAEIREKLIR-LQH 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2818 QRKVAdsTAQQKLTAEQELIRLRAEFDNAEQQRSLLEDELyRLKNEVIAA-QQQRKQLEDELAKMRSEMEILIQLKSRAE 2896
Cdd:pfam05622 290 ENKML--RLGQEGSYRERLTELQQLLEDANRRKNELETQN-RLANQRILElQQQVEELQKALQEQGSKAEDSSLLKQKLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2897 K------ETMSNTEKSKMLLD-----AEASKMRDVAEEAGKLRA-----IAEEAKYQRQIaeeEAARqraEAERILKEKL 2960
Cdd:pfam05622 367 EhleklhEAQSELQKKKEQIEelepkQDSNLAQKIDELQEALRKkdedmKAMEERYKKYV---EKAK---SVIKTLDPKQ 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2961 --AAISEATRLKT-----EAEIALKEKEAENERLRRAAEDE----AYQRKALedeaNQHKKEIEEKIVQLKKSSQAEMQR 3029
Cdd:pfam05622 441 npASPPEIQALKNqllekDKKIEHLERDFEKSKLQREQEEKlivtAWYNMGM----ALHRKAIEERLAGLSSPGQSFLAR 516
|
..
gi 1838104091 3030 QK 3031
Cdd:pfam05622 517 QR 518
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3407-3719 |
1.36e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3407 QIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLqrqKDLAQEQAQRLLEDKELmqKRLDEETEEYQKSLE-AERK 3485
Cdd:PLN03188 915 QTREDKIIRLESLMDGVLSKEDFLEEELASLMHEHKLL---KEKYENHPEVLRTKIEL--KRVQDELEHYRNFYDmGERE 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3486 RQLEivaEAEKLKLQVS---QLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVmQQLEVER-RNNSKE----- 3556
Cdd:PLN03188 990 VLLE---EIQDLRSQLQyyiDSSLPSARKRNSLLKLTYSCEPSQAPPLNTIPESTDESPE-KKLEQERlRWTEAEskwis 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3557 -ADDLRnaiANLETEKARLKKDAEELQNKSK---EMADA-QMKQIEHEKTMLQQTFLTEKEM-LLKKERLIE----DEKK 3626
Cdd:PLN03188 1066 lAEELR---TELDASRALAEKQKHELDTEKRcaeELKEAmQMAMEGHARMLEQYADLEEKHIqLLARHRRIQegidDVKK 1142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3627 RL--------ESQY-EEEAKKAKALTDEQERQRKLMEEEKKKLHATM----------DEALSKQKEAEREMLNKQKEMQE 3687
Cdd:PLN03188 1143 AAaragvrgaESKFiNALAAEISALKVEREKERRYLRDENKSLQAQLrdtaeavqaaGELLVRLKEAEEALTVAQKRAMD 1222
|
330 340 350
....*....|....*....|....*....|..
gi 1838104091 3688 LEKKRLEQEKVLAEENKKLRDQLQQLEEAQKE 3719
Cdd:PLN03188 1223 AEQEAAEAYKQIDKLKRKHENEISTLNQLVAE 1254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3115-3341 |
1.52e-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: 44.75 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3115 TAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQE 3194
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3195 YEKAKKL-AKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAAKRAQAENAALEQKK 3273
Cdd:COG4942 99 LEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3274 KADAEMAKHKKLAEQTLKQkfqvEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEE 3341
Cdd:COG4942 179 LLAELEEERAALEALKAER----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF1663 |
pfam07909 |
Protein of unknown function (DUF1663); The members of this family are hypothetical proteins ... |
2666-3026 |
1.54e-03 |
|
Protein of unknown function (DUF1663); The members of this family are hypothetical proteins expressed by Trypanosoma cruzi, a eukaryotic parasite that causes Chagas' disease in humans. This region is found as multiple copies per protein.
Pssm-ID: 116521 [Multi-domain] Cd Length: 514 Bit Score: 44.80 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2666 AEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQehgtVLQLQqEAAHLKKQQEDALKAR 2745
Cdd:pfam07909 105 AEEDAARGQLVGEESSRVFHVVHDRIGREDAAGHHWVPEDALDAEERRETASRK----CLELE-EAAAFDEIGEMMFQDR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2746 EEAEKELDKWRQKANEALrlrlQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEKELERQ--RKVAD 2823
Cdd:pfam07909 180 LIQAELRSARHEKAEEAL----AAEEDAAMCILAEEEREDTYGLHRDAIDSEEHADRRRIEAGEAAAEDFEEEkgEETAD 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2824 STAQQKLTAEQELIRLRAEFDNAEQQRSLLEDE-LYRLKNEVIAAQQQ--RKQLED-ELAKM-----------RSEMEIL 2888
Cdd:pfam07909 256 AKDWFFSAFELALEALAAEEDAARGKLVLEEREgNYGKHRDAIDSEEQatMNCLEKgEAAAVdagstlaanfsKSEQELG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2889 IQLKSRAEK---ETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILKEKLaaiSE 2965
Cdd:pfam07909 336 EEYEEATDEiadEAIAAEEDIIIHRNKAAARGELVGEEREDMCGLHKDAIDSETTTGEHAVRKLAHPPRLSVQKL---SS 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 2966 ATRLKTEAEIALKEKEAENERLRRAAEDEayqrkALEDEANQHKKEIEEKIVQLKKSSQAE 3026
Cdd:pfam07909 413 QTPLTTTNYNVLIETTTCIERDEAAARDE-----LLDEEILQLIKIIEETRLILTNKTNND 468
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5493-5530 |
1.58e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.58e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1838104091 5493 QRFLEVQYLTGGLIEPDVEGRVSLDESLKKGSIDARTA 5530
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
3445-3731 |
1.58e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3445 QRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLE--AERKRQLEIVAE-AEKLKLQVSQLSVAQAKAEEEAKRFKKQ 3521
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtvMELPQKSTSSDDdHNRASMQRDEAIAAIDNEQQTNSKDGEQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3522 ADNIAARLLETEIATKDKSTVM------QQLE-VERRnnSKEADDLRNAIANLETE----KARLKKDAEElqNKSKEMAD 3590
Cdd:PLN02939 125 LSDFQLEDLVGMIQNAEKNILLlnqarlQALEdLEKI--LTEKEALQGKINILEMRlsetDARIKLAAQE--KIHVEILE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3591 AQMKQIEHEKTM-------------LQQTFLTEKEMLLKKErlIEDEKKRLESQYEEEAKKAKAltdeqERQRKLMEEEK 3657
Cdd:PLN02939 201 EQLEKLRNELLIrgateglcvhslsKELDVLKEENMLLKDD--IQFLKAELIEVAETEERVFKL-----EKERSLLDASL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3658 KKLHATM---DEALSK----QKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATV 3730
Cdd:PLN02939 274 RELESKFivaQEDVSKlsplQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKV 353
|
.
gi 1838104091 3731 E 3731
Cdd:PLN02939 354 E 354
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2593-2719 |
1.64e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREKAAEAERLRKLA-QEEAEKLHKQvIEETQKKRtaeEELKRKSEAEKEAAKQKQKALEDLENLKMQAEEAER 2671
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEAsFERLAELRDE-LAELEEEL---EALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 2672 KVKQAQiEKEKQIQ-----------IAHVAAEKSA--TAELQSTQRsfvEKTSKLEESLKQ 2719
Cdd:COG0542 493 ELAELE-EELAELApllreevteedIAEVVSRWTGipVGKLLEGER---EKLLNLEEELHE 549
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3561-3727 |
1.67e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3561 RNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQYEEEAKKAK 3640
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3641 ALTDEQERQRKLmeEEKKKLHATMDEALSKQKEAERemlnKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:pfam13868 111 QEEDQAEAEEKL--EKQRQLREEIDEFNEEQAEWKE----LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKER 184
|
....*..
gi 1838104091 3721 NTQVISA 3727
Cdd:pfam13868 185 EIARLRA 191
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
877-1043 |
1.76e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 877 SMPKAtVKASRVTTSELTELNVSPKMAPERMCSEETRRTAAVlceAPADKEEVEPAPL------FAEKVKREVPKPKTSS 950
Cdd:PRK07003 375 RVAGA-VPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAA---AAAAATRAEAPPAapappaTADRGDDAADGDAPVP 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 951 TAREAPAAGELA----SAAPVVTAQAAVAPTQTSP--LHKQEEPPIVSQHSASKAAERCTEKQLSAS-------QALKQE 1017
Cdd:PRK07003 451 AKANARASADSRcderDAQPPADSGSASAPASDAPpdAAFEPAPRAAAPSAATPAAVPDARAPAAASredapaaAAPPAP 530
|
170 180
....*....|....*....|....*.
gi 1838104091 1018 EEKKSDSKKDTPSAIATTASAQTDQL 1043
Cdd:PRK07003 531 EARPPTPAAAAPAARAGGAAAALDVL 556
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3480-3671 |
1.79e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3480 LEAERKRQL-EIVAEAEKlklqvsqlsvAQAKAEEEAKRFKKQADNIAArllETEIAtkdkstvmQQLEVERRNNSKEAD 3558
Cdd:COG2268 186 LDALGRRKIaEIIRDARI----------AEAEAERETEIAIAQANREAE---EAELE--------QEREIETARIAEAEA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3559 DLR--NAIANLETEKARLKKDA--EELQNKSKEMADAQMKQIEHEKtmlqQTFLTEKEMLLKKERLIEDEKKRLESQY-- 3632
Cdd:COG2268 245 ELAkkKAEERREAETARAEAEAayEIAEANAEREVQRQLEIAERER----EIELQEKEAEREEAELEADVRKPAEAEKqa 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838104091 3633 -------EEEAKKAKALTdEQERQRKLMEEEKKKLHATMDEALSKQ 3671
Cdd:COG2268 321 aeaeaeaEAEAIRAKGLA-EAEGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
3242-3384 |
1.84e-03 |
|
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.
Pssm-ID: 396537 [Multi-domain] Cd Length: 199 Bit Score: 43.14 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKEAEFEAAKraQAENAALEQKKKADAEMAKHKKLAEQTlkQKFQVEQELTKVKLKLddTDKQKDLLDDEL 3321
Cdd:pfam01991 5 EAEEKAEEIRAKAEEEFAI--EKAELVQEAEEKIDEIYEKKEKQAEMQ--KKIIISNAKNEARLKV--LEAREEILDEVF 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3322 QRLKDEVDDAVKQRGQVEEELFKVKVQ-MEELL--KVKLKIEKENQLLIKKDKDKAQQLLAEEAEN 3384
Cdd:pfam01991 79 NEAEKKLAELEEDTDEYKDLLRKLIVQaLVKLGepEVIVRCRKRDEELVESALDKAAEEYKAKTKK 144
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3290-3720 |
1.85e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3290 LKQKFQVEQ-ELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEllkvklkIEKENQLLIK 3368
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM-------KNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3369 KDKDKAQQLlaEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQK 3448
Cdd:PRK01156 261 AESDLSMEL--EKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3449 DLAQEQAQRLLE-DKELMQKRLDE--------ETEEYQKSLEAERKRQL------------------EIVAEAEKLKLQV 3501
Cdd:PRK01156 339 NDYIKKKSRYDDlNNQILELEGYEmdynsylkSIESLKKKIEEYSKNIErmsafiseilkiqeidpdAIKKELNEINVKL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3502 SQLS--VAQAKAEEEAKRFKKQADNIAARLLE---------TEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETE 3570
Cdd:PRK01156 419 QDISskVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3571 KARLKKDAEELQNKS---KEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEK----KRLESQYeEEAKKAKALT 3643
Cdd:PRK01156 499 IVDLKKRKEYLESEEinkSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKslklEDLDSKR-TSWLNALAVI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3644 D--EQERQRKLMEEEKKKLH---ATMDEALSKQKEAEREMLNKQKEMQElEKKRLEQEKVLAEENKKLRDQLQQLEEAQK 3718
Cdd:PRK01156 578 SliDIETNRSRSNEIKKQLNdleSRLQEIEIGFPDDKSYIDKSIREIEN-EANNLNNKYNEIQENKILIEKLRGKIDNYK 656
|
..
gi 1838104091 3719 EK 3720
Cdd:PRK01156 657 KQ 658
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2862-2983 |
1.88e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2862 NEVIAA-QQQRKQLEDELAkmrsEMEILIQlksRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIA--EEAKYQR 2938
Cdd:PRK00409 519 NELIASlEELERELEQKAE----EAEALLK---EAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAkkEADEIIK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1838104091 2939 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAE 2983
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3459-3719 |
1.93e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3459 LEDKELMQKRLD---EETEEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETE-- 3533
Cdd:pfam05701 34 VERRKLVELELEkvqEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEqg 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3534 IATKDKSTVMQQLEVERRNNSKEADDLRNAIANLET---EKARLKKDAEELQNKSKEmADAQMKQIehEKTMLQQTFlte 3610
Cdd:pfam05701 114 IADEASVAAKAQLEVAKARHAAAVAELKSVKEELESlrkEYASLVSERDIAIKRAEE-AVSASKEI--EKTVEELTI--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3611 kEMLLKKERLIEDEKKRLESqyeEEAKKAKALTDEQ-----ERQRKLMEEEKKKLHATMDEAL---SKQKEAEREMLNKQ 3682
Cdd:pfam05701 188 -ELIATKESLESAHAAHLEA---EEHRIGAALAREQdklnwEKELKQAEEELQRLNQQLLSAKdlkSKLETASALLLDLK 263
|
250 260 270
....*....|....*....|....*....|....*...
gi 1838104091 3683 KEMQELEKKRLEQEKVLAEENKKL-RDQLQQLEEAQKE 3719
Cdd:pfam05701 264 AELAAYMESKLKEEADGEGNEKKTsTSIQAALASAKKE 301
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2598-2870 |
1.98e-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: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2598 QLREKAAEAERLRKLAQEEAEKLHKQViEETQKKRtaeEELKRKS-----EAEKEAAKQKQKALED-LENLKMQAEEAER 2671
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKEL-EEAEAAL---EEFRQKNglvdlSEEAKLLLQQLSELESqLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2672 KVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEaahlkkqqedalkaREEAEKE 2751
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ--------------IAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2752 LDKWRQKANEALRLRLQAeeeahkkslaqeeaekqkeeaereakkrAKAEESALKQkemaekELERQRKVADSTAQQklt 2831
Cdd:COG3206 307 LQQEAQRILASLEAELEA----------------------------LQAREASLQA------QLAQLEARLAELPEL--- 349
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1838104091 2832 aEQELIRLRAEFDNAEQQ-RSLLEdelyRLKNEVIAAQQQ 2870
Cdd:COG3206 350 -EAELRRLEREVEVARELyESLLQ----RLEEARLAEALT 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2648-2823 |
1.99e-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: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2648 AAKQKQKALEDLENLKMQAEEAERKVKQAQIEkekqiqiahVAAEKSATAELQSTQRSFVEKTSKLEESLKQEHGTVLQL 2727
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAE---------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2728 QQEAAHLKKQQEDALKARE----EAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKAEES 2803
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|
gi 1838104091 2804 ALKQKEMAEKELERQRKVAD 2823
Cdd:COG1579 152 AELEAELEELEAEREELAAK 171
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
1151-1255 |
2.01e-03 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 41.25 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1151 VQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRF----HKLQNVQIALDFLRHRQV 1226
Cdd:cd21306 16 VVKKSLITFVNKHLNK---LNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGL 92
|
90 100
....*....|....*....|....*....
gi 1838104091 1227 KLVNIRNDDIADGNPKLTLGLIWTIILHF 1255
Cdd:cd21306 93 PKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1292-1369 |
2.04e-03 |
|
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: 40.75 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1292 DNFTTSWRDGKLFNAVIHKhhprlidMGRVYQQSNQ-------ENLEQAFNVAERdLGVTRLLDPEDVDVPHPDEKSIIT 1364
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNA-------LGGSVPGWPNldpeeseNNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMA 91
|
....*
gi 1838104091 1365 YVSSL 1369
Cdd:cd21185 92 YAAQL 96
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
1153-1221 |
2.16e-03 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 40.72 E-value: 2.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 1153 KKTFTKWVNKHLIKraesQH-HVTDLYEDLRDGHNLISLLEVLSGDTLPREK----GRMRFHKLQNVQIALDFL 1221
Cdd:cd21221 3 VRVLTEWINEELAD----DRiVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2620-2904 |
2.21e-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: 44.51 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2620 LHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAE-EAERKVKQAQIEKEKQIQIAHVAAE--KSAT 2696
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELErQKERLEKELASQQEKRAQEKEALRKemKKER 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2697 AELQSTQRSFVEKTSKLEESL----KQEHGTVLQLQQEAAHLKKQQEDALKA--------------REEAEKELDKWRQK 2758
Cdd:pfam15964 399 EELGATMLALSQNVAQLEAQVekvtREKNSLVSQLEEAQKQLASQEMDVTKVcgemryqlnqtkmkKDEAEKEHREYRTK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2759 ANEALRLrlqAEEEAHKKSLAQEEAEKQKEEAEREAkkrAKAEESALKQKEM---AEKELERQRKVADSTAQ-------- 2827
Cdd:pfam15964 479 TGRQLEI---KDQEIEKLGLELSESKQRLEQAQQDA---ARAREECLKLTELlgeSEHQLHLTRLEKESIQQsfsneaka 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2828 QKLTAEQELIRLRAEFDNAEQQRSLLEDELYRL---KNEVIAAQQQR-----KQLEDELAKMRSEMEILIQ----LKSRA 2895
Cdd:pfam15964 553 QALQAQQREQELTQKMQQMEAQHDKTVNEQYSLltsQNTFIAKLKEEcctlaKKLEEITQKSRSEVEQLSQekeyLQDRL 632
|
....*....
gi 1838104091 2896 EKETMSNTE 2904
Cdd:pfam15964 633 EKLQKRNEE 641
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2593-2816 |
2.22e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 43.11 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLREkaAEAERLRKLAQEEAEKlhkqvIEETQKKRTAEEELKRK----SEAEKEAAKQKQKALEDLENLKMQAEE 2668
Cdd:pfam15665 13 EAEIQALKE--AHEEEIQQILAETREK-----ILQYKSKIGEELDLKRRiqtlEESLEQHERMKRQALTEFEQYKRRVEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2669 AERKVKQAqiekekqiqiaHVAAEKSATAELQSTQRSFVEKTSKLEEslkqehgtvLQLQQEAAHLKKQQEDALKAREEA 2748
Cdd:pfam15665 86 RELKAEAE-----------HRQRVVELSREVEEAKRAFEEKLESFEQ---------LQAQFEQEKRKALEELRAKHRQEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 2749 EKELDKWRQKANEALRLRLQAEE------EAHKKSLAQEEAEKQKEEAEREAKKrakaeesaLKQKEMAEKELE 2816
Cdd:pfam15665 146 QELLTTQRAQSASSLAEQEKLEElhkaelESLRKEVEDLRKEKKKLAEEYEQKL--------SKAQAFYERELE 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2792-3718 |
2.23e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2792 REAKKRAKAEESALKqkemAEKELERQRKvadstaqqKLTAEQE-LIRLRAEFDNAEQQRSLLEDELYRLK---NEVIAA 2867
Cdd:PRK04863 276 RHANERRVHLEEALE----LRRELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2868 QQQRKQLE---DELAKmrsemeiliqLKSRAEKETMSNTEKSKMLLDAEASKmrDVAEEAgKLRAIAEEAKYQRQI-AEE 2943
Cdd:PRK04863 344 LRQQEKIEryqADLEE----------LEERLEEQNEVVEEADEQQEENEARA--EAAEEE-VDELKSQLADYQQALdVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2944 EAARQRAEAERILKE-----KLAAISEATRLKTEAEIALKEKEAENERLrraaedEAYQRKALEDEAnqhkKEIEEKIVQ 3018
Cdd:PRK04863 411 TRAIQYQQAVQALERakqlcGLPDLTADNAEDWLEEFQAKEQEATEELL------SLEQKLSVAQAA----HSQFEQAYQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3019 LKKSSQAEMQRQKAmvddtlkqrrvveeeirilklnFEKASSgkldLELELNKLKNIAEETQQSKLR---AEEEAEKQRK 3095
Cdd:PRK04863 481 LVRKIAGEVSRSEA----------------------WDVARE----LLRRLREQRHLAEQLQQLRMRlseLEQRLRQQQR 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3096 LameeekrrreaeetVKKITAAEKEAGRQRKiAQDELDRLKKKAEEARKQKDKADSEAEKQivaasqaalkcRTAEQQVQ 3175
Cdd:PRK04863 535 A--------------ERLLAEFCKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARER-----------RMALRQQL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3176 SVLAQQKEDsmmHKKLQQEYEKAKKLAKEaeaakekaekeavlLRKQAEEAESQKAAAEKEAaiqakaQEDAERLRkEAE 3255
Cdd:PRK04863 589 EQLQARIQR---LAARAPAWLAAQDALAR--------------LREQSGEEFEDSQDVTEYM------QQLLERER-ELT 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3256 FE----AAKRAQAENAALEQKKKADAEMAKHKKLAEQ-------------TLKQK--FQ----------VEQELTKVKLK 3306
Cdd:PRK04863 645 VErdelAARKQALDEEIERLSQPGGSEDPRLNALAERfggvllseiyddvSLEDApyFSalygparhaiVVPDLSDAAEQ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3307 LDdtdKQKDLLDD------ELQRLKDEVDDAvkqrgqveEELFK-VKVQMEEllkVKLKIEK--ENQLLIKKDKDKAQQL 3377
Cdd:PRK04863 725 LA---GLEDCPEDlyliegDPDSFDDSVFSV--------EELEKaVVVKIAD---RQWRYSRfpEVPLFGRAAREKRIEQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3378 LAEEAEnmkRLAKEAAILSVESQEASRLRQIAEEDLVQQRALA-----EKMLKEKMQAIQEASRLKA---EAELLQRQK- 3448
Cdd:PRK04863 791 LRAERE---ELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALAdheSQEQQQRSQl 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3449 DLAQEQAQRL--------LEDKELMQKRLDEETEEYQKSLEAER--KRQLEIVAEAEKL--KLQVSQLSVAQAKAE-EEA 3515
Cdd:PRK04863 868 EQAKEGLSALnrllprlnLLADETLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIvsVLQSDPEQFEQLKQDyQQA 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3516 KRFKKQADNiAARLLeTEIatkdkstvmqqleVERRNN---SKEADDLRNAIANLETEKARLKKdAEELQNKSKEM---A 3589
Cdd:PRK04863 948 QQTQRDAKQ-QAFAL-TEV-------------VQRRAHfsyEDAAEMLAKNSDLNEKLRQRLEQ-AEQERTRAREQlrqA 1011
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3590 DAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIED----------------------------------EKKR--LESQYE 3633
Cdd:PRK04863 1012 QAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpadsgaeerararrdelharlsanrsrrnqlEKQLtfCEAEMD 1091
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3634 EEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEA--EREMLNKQK--EMQELEKKRLEQEKVLAEENKKLRDQ 3709
Cdd:PRK04863 1092 NLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERrlHRRELAYLSadELRSMSDKALGALRLAVADNEHLRDV 1171
|
....*....
gi 1838104091 3710 LQQLEEAQK 3718
Cdd:PRK04863 1172 LRLSEDPKR 1180
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
2847-2999 |
2.26e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 41.96 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2847 EQQRSLLEDELYRLKNEVIaaqqqRKQLEDELAKMRSEMEILIQLKSRAEKETMsntekskmlldaeaskMRDVAEEAGK 2926
Cdd:pfam15346 2 EAESKLLEEETARRVEEAV-----AKRVEEELEKRKDEIEAEVERRVEEARKIM----------------EKQVLEELER 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838104091 2927 LRAIAEEAKYQRqiaEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKE--AENERLRRAAEDEAYQRK 2999
Cdd:pfam15346 61 EREAELEEERRK---EEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQrrMKEERQRREKEEEEREKR 132
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
3427-3682 |
2.45e-03 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 44.12 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3427 KMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKsleAERKRQLEI---------------- 3490
Cdd:pfam05914 46 KRQEAAEKAREEAFAEEMVQNDKIALMLEKREEEDRRRLNKELNEFRQQHQR---PETRREFDLndpdalkkdlparvsd 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3491 -----------------VAEAEKLKLQVSQL---SVAQAKAEEEAKRFKKQADniaaRLLETEIATKDKSTV-MQQLEVE 3549
Cdd:pfam05914 123 ddprcgpssmqkfegedLNREERKKLQQEQMrewLEQQIEEKKQAEEEEKHAE----LLYDQKRLERDRRALeLAKLEEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3550 RRNNSKEADDLRN-AIANLETEKARLKKDAEElqnkskemaDAQMKQIEHektMLQQTFLTE------------------ 3610
Cdd:pfam05914 199 CRRAVNAATKNFNqALAAEQAERRRLEKRQEQ---------EDNLAEIYN---HLTSDLLTEnpevaqsslgphrvipdr 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3611 ----------------KEMLLKKERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATmDEALSKQKEA 3674
Cdd:pfam05914 267 wkgmspeqlkeirkeqEQQREEKERRREEEKQRDAEWDRQRLELARAALLLEREQQRLRRELRRQLDEE-NLQLAQEQKA 345
|
....*...
gi 1838104091 3675 EREMLNKQ 3682
Cdd:pfam05914 346 RQEYLNKE 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3316-3656 |
2.46e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3316 LLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEaaiL 3395
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQL-EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE---L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3396 SVESQEASRLRQIAEEDLVQQRALAEKM--LKEKMQAIQEASRLKaEAELLQRQKDLAQEQAQrLLEDKELMQKRLDEET 3473
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRkqLEAQIAELQSEIAER-EEELKELEEQLESLQEE-LAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3474 EEYQKSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTV--MQQLEVERR 3551
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEllEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3552 NNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKKERLIEDEKKRLESQ 3631
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
330 340
....*....|....*....|....*
gi 1838104091 3632 YEEEAKKAKALTDEQERQRKLMEEE 3656
Cdd:COG4372 342 LLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2839-3157 |
2.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2839 LRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQLKSRAEKEtmsntekskmlLDAEASKMR 2918
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-----------LQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2919 DVAEEAGKLRAiaEEAKYQRQIAEEEAARQRAEAERilKEKLAAISEATRLKTEAEIALKEKEAENERLRRAAEDEAYQR 2998
Cdd:COG4372 98 QAQEELESLQE--EAEELQEELEELQKERQDLEQQR--KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2999 KALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEE 3078
Cdd:COG4372 174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3079 TQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQI 3157
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
3291-3729 |
2.70e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3291 KQKFQVEQELTKVKLK-----LDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKvklkiekenQL 3365
Cdd:PRK04778 86 EQLFEAEELNDKFRFRkakheINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRK---------SL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3366 LIKKDK-DKAQQLLAEEAENMKRLAKEAAILSVESQ--EASRLRQIAEEDLVQqralaekmLKEKMQAIQEASRlKAEAE 3442
Cdd:PRK04778 157 LANRFSfGPALDELEKQLENLEEEFSQFVELTESGDyvEAREILDQLEEELAA--------LEQIMEEIPELLK-ELQTE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3443 LLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEaerkrqlEIVAEAEKLKLqvsqlsvaqAKAEEEAKRFKKQA 3522
Cdd:PRK04778 228 LPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQID-------ENLALLEELDL---------DEAEEKNEEIQERI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3523 DNIAArLLETEIATKDkstvmqqlEVErrnnsKEADDLRNAIANLETEKARLKKDAEELQN----------KSKEMaDAQ 3592
Cdd:PRK04778 292 DQLYD-ILEREVKARK--------YVE-----KNSDTLPDFLEHAKEQNKELKEEIDRVKQsytlneseleSVRQL-EKQ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3593 MKQIEHEKTMLQQTFlTEKEML--LKKERLIEDEK--KRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATM---- 3664
Cdd:PRK04778 357 LESLEKQYDEITERI-AEQEIAysELQEELEEILKqlEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKryle 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3665 --------DEALSKQKEAEREMlnkQKEMQELEKKRLEQEKVlaeeNKKLRDQLQQLEEAqKEKNTQVISAAT 3729
Cdd:PRK04778 436 ksnlpglpEDYLEMFFEVSDEI---EALAEELEEKPINMEAV----NRLLEEATEDVETL-EEETEELVENAT 500
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2961-3270 |
2.88e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2961 AAISEATRLKTEAEIALKEKEAENERLRR-AAEDEAYQRKALEDEANQHKKEIeekivqlkkssQAEMQRQKAmvddtlk 3039
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEReKAAREARHKKAAEARAAKDKDAV-----------AAALARVKA------- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3040 qrrvveeeirilklnfEKASSgkldlelELNKLKNIAEETQQSKLRAEEEAEKQRKLAMEEEKrrreaeetvkkiTAAEK 3119
Cdd:PRK05035 498 ----------------KKAAA-------TQPIVIKAGARPDNSAVIAAREARKAQARARQAEK------------QAAAA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3120 EAGRQRKIAQDeLDRLK-KKAEEARKQKDKADSEAEKQI-VAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEK 3197
Cdd:PRK05035 543 ADPKKAAVAAA-IARAKaKKAAQQAANAEAEEEVDPKKAaVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI 621
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 3198 AKKLAKEAEAAKEKAEKEAVLLRKQAEEAESQKAAAEKEAAIQAKAQEDAERLRKEAEFEAA-KRAQAENAALE 3270
Cdd:PRK05035 622 ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAiARAKAKKAAQQ 695
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
3295-3384 |
2.92e-03 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 42.30 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3295 QVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEVDDAVKQRGQVEEELFKVKvqmeELLKVKLKIEKENQLLIKKDKDKA 3374
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIK----QISANAIELDEENRELREELAELK 145
|
90
....*....|
gi 1838104091 3375 QQLLAEEAEN 3384
Cdd:TIGR04211 146 QENEALEAEN 155
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3531-3718 |
2.95e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3531 ETEIATKDKSTVMQQLEVERRNNSKE----ADDLRNAIANLETEKArlKKDAEELQNKSKEMADAQMKQIEHEKTMLQQT 3606
Cdd:pfam15709 288 ESQVSIDGRSSPTQTFVVTGNMESEEerseEDPSKALLEKREQEKA--SRDRLRAERAEMRRLEVERKRREQEEQRRLQQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3607 FLTEKEMLLKKErlIEDEKKRlesQYEEEAKKAKALTDEQERQrklmEEEKKKLHATMDEAlskQKEAEREMLNKQKEMQ 3686
Cdd:pfam15709 366 EQLERAEKMREE--LELEQQR---RFEEIRLRKQRLEEERQRQ----EEEERKQRLQLQAA---QERARQQQEEFRRKLQ 433
|
170 180 190
....*....|....*....|....*....|...
gi 1838104091 3687 ELEKKRLEQEKVLAEENKKLRDQLQ-QLEEAQK 3718
Cdd:pfam15709 434 ELQRKKQQEEAERAEAEKQRQKELEmQLAEEQK 466
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2640-2834 |
3.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2640 RKSEAEKEAAKQKQKALEDLENLKMQAEEAERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRSFVEKtsklEESLKQ 2719
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2720 EHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEAL-RL-RLQAEEEahKKSLaqeeaekqkeeaEREAKKR 2797
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELeRIsGLTAEEA--KEIL------------LEKVEEE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1838104091 2798 AKAEESALKQKEMAEKELERQRKVAD--STAQQKLTAEQ 2834
Cdd:PRK12704 167 ARHEAAVLIKEIEEEAKEEADKKAKEilAQAIQRCAADH 205
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3615-3729 |
3.06e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3615 LKKERLIEDEKKRLESQYEEeakkAKALTDEQERQRKLMEEEKKKLhatmDEALSKQKEAEREMLNKQKEMQELEKKRLE 3694
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQ----TLALLDKIDRQKEETEQLKQQL----AQAPAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100 110
....*....|....*....|....*....|....*..
gi 1838104091 3695 QEKVLAEENK--KLRDQLQQLEEAQKEKNTQVISAAT 3729
Cdd:PRK11281 120 TLSLRQLESRlaQTLDQLQNAQNDLAEYNSQLVSLQT 156
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2978-3194 |
3.12e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2978 KEKEAENERLRRAAEDEAyqrkaleDEANQHKKEIEEKIVQLKKSSQAEMQRQKAmvddtLKQRRVVEEEIRilklNFEK 3057
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAA-------KKEQERQKKLEQQAEEAEKQRAAEQARQKE-----LEQRAAAEKAAK----QAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3058 AssgkldlelelnKLKNIAEETQQSKLRAEEEAEKQRKlameeekrrREAEETVKKITAAEKEAgrqrkiaqdELDRLKK 3137
Cdd:TIGR02794 110 A------------AKQAEEKQKQAEEAKAKQAAEAKAK---------AEAEAERKAKEEAAKQA---------EEEAKAK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838104091 3138 KAEEARKQKDKADSEAEKQIVAASQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQE 3194
Cdd:TIGR02794 160 AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3076-3322 |
3.23e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3076 AEETQQSKLRAEEEAEKQRKLAMEEEKRRREAEETVKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEK 3155
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3156 QIVAASQAAlkcrtAEQQVQSVLAQQKEDSMMHKKLQQEyekakklakeaeaakekaekeavllRKQAEEAE---SQKAA 3232
Cdd:TIGR02794 145 KEEAAKQAE-----EEAKAKAAAEAKKKAEEAKKKAEAE-------------------------AKAKAEAEakaKAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3233 AEKEAAIQAKAQEDAERlRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDK 3312
Cdd:TIGR02794 195 KAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQ 273
|
250
....*....|
gi 1838104091 3313 QKDLLDDELQ 3322
Cdd:TIGR02794 274 QNLYDDPSFR 283
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4459-4495 |
3.64e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 3.64e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1838104091 4459 KYLQGSDSIAGIYLEPTKETISIYQAMKKKLLRQNTG 4495
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2519-3093 |
3.76e-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: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2519 KQEVS--KREVAALDAENQKKNIELELHELKK-LSEQQINDKSQLVDDALQSRT---KIEEEIHIIRIQLETTLNQKSTA 2592
Cdd:pfam15964 134 KEELSemKQRVQVVVLENEKLQQELKSQTQEEtLREQTLLDSSGNMQNSWCTPEdsrVHQTSKRPASHNLAERLKSATTG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2593 ETELKQLrekaaEAERLRKLAQEEAEKLHKQVieETQKKRTAEeelkrkSEAEKEAAKQKQKALEDLENLKMQAEEAERK 2672
Cdd:pfam15964 214 EDEKWRL-----ELEKLKLLYEAKTEVLESQV--KSLRKDLAE------SQKTCEDLKERLKHKESLVAASTSSRVGGLC 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2673 VKQAQIEKekqiqiahVAAEKSATAELQSTQRsFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKEL 2752
Cdd:pfam15964 281 LKCAQHEA--------VLAQTHTNVHMQTIER-LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEK 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2753 DKWRQKAnEALRLRLQAEEEAHKKSLAQeeaekqkeeaerEAKKRAKAeesalkqKEMAEKELERQRKVADSTAqqkLTA 2832
Cdd:pfam15964 352 TKALIQC-EQLKSELERQKERLEKELAS------------QQEKRAQE-------KEALRKEMKKEREELGATM---LAL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2833 EQELIRLRAEFDNAEQQRSlledelyRLKNEVIAAQQQRKQLEDELAKMRSEMEILIQlksraeKETMSNTEKSKMLLDA 2912
Cdd:pfam15964 409 SQNVAQLEAQVEKVTREKN-------SLVSQLEEAQKQLASQEMDVTKVCGEMRYQLN------QTKMKKDEAEKEHREY 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2913 EASKMRDVA---EEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERIlkeklaaiseaTRLKTEAEIALKEKEAENERLRR 2989
Cdd:pfam15964 476 RTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTRLEKESIQQ 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2990 AAEDEAyqrKALEDEANQHKKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELEL 3069
Cdd:pfam15964 545 SFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQL 621
|
570 580
....*....|....*....|....
gi 1838104091 3070 NKLKNIAEETQQSKLRAEEEAEKQ 3093
Cdd:pfam15964 622 SQEKEYLQDRLEKLQKRNEELEEQ 645
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3581-3720 |
3.81e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3581 LQNKSKEMADAQ---MKQIEHEKTMLQQTFLTEKEML--LKKERLIEDEKKRlesQYEEEAKKAKALTDE-QERQRKLME 3654
Cdd:PRK09510 67 QQQQQKSAKRAEeqrKKKEQQQAEELQQKQAAEQERLkqLEKERLAAQEQKK---QAEEAAKQAALKQKQaEEAAAKAAA 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3655 EEKKKLHATMDEALSKQKEAEREMLNKQKEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEK 3720
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
3354-3674 |
3.85e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.49 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3354 KVKLKIEKENQLLIKKDKdkaQQLLAEEAENMKRLAKEaailsvESQEASRLRQIAEEDLVQQRALA---EKMLKEKMQ- 3429
Cdd:pfam15558 43 KRQETLERERRLLLQQSQ---EQWQAEKEQRKARLGRE------ERRRADRREKQVIEKESRWREQAedqENQRQEKLEr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3430 AIQEASRLKaeaellqrqkdlaQEQAQRLLEDKELMQKRLDEETEEYQKSLE-AERKRQLEIVAE---------AEKLKL 3499
Cdd:pfam15558 114 ARQEAEQRK-------------QCQEQRLKEKEEELQALREQNSLQLQERLEeACHKRQLKEREEqkkvqennlSELLNH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3500 QVSQLSVA-QAKAEEEAKRFkkqadNIAARLLeteiatkdKSTVMQQLEVERRNNSkeaddLRNAIANLETEKARLKKDA 3578
Cdd:pfam15558 181 QARKVLVDcQAKAEELLRRL-----SLEQSLQ--------RSQENYEQLVEERHRE-----LREKAQKEEEQFQRAKWRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3579 EELQNKSKEMADAQMKqiEHEKTMLQQTFLTEKEMLLKKERLIEdekKRLESQYEEEAKKAKALTDEQERQRKLMEEEKK 3658
Cdd:pfam15558 243 EEKEEERQEHKEALAE--LADRKIQQARQVAHKTVQDKAQRARE---LNLEREKNHHILKLKVEKEEKCHREGIKEAIKK 317
|
330
....*....|....*.
gi 1838104091 3659 KLHATmdEALSKQKEA 3674
Cdd:pfam15558 318 KEQRS--EQISREKEA 331
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2460-2884 |
3.90e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2460 ETQRRLEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADElkHQMKQEVSKREVAALDAENQKKNI 2539
Cdd:PLN02939 43 SSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDD--HNRASMQRDEAIAAIDNEQQTNSK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2540 ELElhelkKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEeaEK 2619
Cdd:PLN02939 121 DGE-----QLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQ--EK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2620 LHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKMQAEeaerkvkqAQIEKEKqiqIAHVAAEKSATAEL 2699
Cdd:PLN02939 194 IHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDD--------IQFLKAE---LIEVAETEERVFKL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2700 QStQRSFvektskLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAR-EEAEKELDKWRQKANEALrLRLQAEEEAHKKsl 2778
Cdd:PLN02939 263 EK-ERSL------LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKvENLQDLLDRATNQVEKAA-LVLDQNQDLRDK-- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2779 aqeeaEKQKEEAEREAK-KRAKAEESALKQKEMaeKELERQRKVADSTAQQKLTAEQELIrlrAEFdnaeqqrsllEDEL 2857
Cdd:PLN02939 333 -----VDKLEASLKEANvSKFSSYKVELLQQKL--KLLEERLQASDHEIHSYIQLYQESI---KEF----------QDTL 392
|
410 420
....*....|....*....|....*..
gi 1838104091 2858 YRLKNEviaaqQQRKQLEDELAKMRSE 2884
Cdd:PLN02939 393 SKLKEE-----SKKRSLEHPADDMPSE 414
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2451-2682 |
3.91e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2451 TSQYIKFITETQRRLEDEEKAAKILKAEEQKKMADLQAELDKQKKLAEAHAKAIAKAEKEADElkhQMKQEVSKREVAAL 2530
Cdd:pfam02029 92 TIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE---EGEEEEDKSEEAEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2531 DAENQKKNIELELHELKKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETT------LNQKSTAETELKQLREKAA 2604
Cdd:pfam02029 169 VPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTkrrqggLSQSQEREEEAEVFLEAEQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2605 EAERLR----KLAQEEAEKLHkqvieetQKKRTAE---EELKRKSEaekeaakQKQKALEDlENLKMQAEEAERKVKQaq 2677
Cdd:pfam02029 249 KLEELRrrrqEKESEEFEKLR-------QKQQEAElelEELKKKRE-------ERRKLLEE-EEQRRKQEEAERKLRE-- 311
|
....*
gi 1838104091 2678 iEKEK 2682
Cdd:pfam02029 312 -EEEK 315
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2727-3063 |
3.92e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2727 LQQEAAHLKKQQEDALKAREEAEKELDKWRQK------ANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAEREAKKRAKA 2800
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKfkelylAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2801 EESALKQKEMAEKELERQRKVADSTAQQKLTAE----QELIRLRAEFDNAEQQRSLLEDELYRLKNEVIAAQQQrKQLED 2876
Cdd:pfam03528 86 VSENTKQEAIDEVKSQWQEEVASLQAIMKETVReyevQFHRRLEQERAQWNQYRESAEREIADLRRRLSEGQEE-ENLED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2877 ELAKMRSEMEILIQLKSRAEKETMS----NTEKSKMLLDAEASKMRDVAE--EAGK-----LRAIAEEAKYQRQIAEEEA 2945
Cdd:pfam03528 165 EMKKAQEDAEKLRSVVMPMEKEIAAlkakLTEAEDKIKELEASKMKELNHylEAEKscrtdLEMYVAVLNTQKSVLQEDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2946 ARQRAEAERILKEKLAAISEATRLKTEAEIAlKEKEAENERLrrAAEDEAYQRKALEDEanqHKKEIEEkivqLKKSSQA 3025
Cdd:pfam03528 245 EKLRKELHEVCHLLEQERQQHNQLKHTWQKA-NDQFLESQRL--LMRDMQRMESVLTSE---QLRQVEE----IKKKDQE 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 1838104091 3026 EMQRQ-KAMVDDTLKQRRVVEEEIRILKLNFEKASSGKL 3063
Cdd:pfam03528 315 EHKRArTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2581-2773 |
3.98e-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: 43.40 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2581 QLETTLNQKSTAETELKQLREKAAEAERLRKlaQEEAEKLHKQVIEETQKKRTAEEELKRKseaekeaakqkqkaLEDLE 2660
Cdd:pfam15709 373 KMREELELEQQRRFEEIRLRKQRLEEERQRQ--EEEERKQRLQLQAAQERARQQQEEFRRK--------------LQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2661 NlKMQAEEAERkvkqAQIEKEKQiqiahvaaeksataelqstqrsfvektSKLEESLKQEHGTVLQLQQEA--AHLKKQQ 2738
Cdd:pfam15709 437 R-KKQQEEAER----AEAEKQRQ---------------------------KELEMQLAEEQKRLMEMAEEErlEYQRQKQ 484
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838104091 2739 EDALKAREEAEKEldkwRQKANEALRLRL-----QAEEEA 2773
Cdd:pfam15709 485 EAEEKARLEAEER----RQKEEEAARLALeeamkQAQEQA 520
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3410-3706 |
4.03e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3410 EEDLVQQRALAEKMLKE----KMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKelmqKRLDEETEEYQKSLEAERK 3485
Cdd:COG1340 10 LEELEEKIEELREEIEElkekRDELNEELKELAEKRDELNAQVKELREEAQELREKR----DELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3486 RQLEIVAEAEKLKLQVSQLSvaqaKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEV--ERRNNSKEADDLRNA 3563
Cdd:COG1340 86 KLNELREELDELRKELAELN----KAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKEleKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3564 IANLETEKARLKKDAEELQNKSKEMADaqmKQIEHEKTMLQqtfLTEKEMLLKKERlieDEKKRlesQYEEEAKKAKALT 3643
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAE---EAQELHEEMIE---LYKEADELRKEA---DELHK---EIVEAQEKADELH 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 3644 DEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEmqELEKKRLEQEKVLAEENKKL 3706
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE--EIFEKLKKGEKLTTEELKLL 290
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
3394-3534 |
4.07e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3394 ILSVESQEASRLRQIAEEDLVQQRALAEKmLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQR---LLEDKELMQKRLD 3470
Cdd:COG1566 73 LARLDPTDLQAALAQAEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqaLYKKGAVSQQELD 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838104091 3471 EETEEYQkSLEAERKRQLEIVAEAEKLKLQVSQLSVAQAkaeeEAKRFKKQADNIAARLLETEI 3534
Cdd:COG1566 152 EARAALD-AAQAQLEAAQAQLAQAQAGLREEEELAAAQA----QVAQAEAALAQAELNLARTTI 210
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3311-3523 |
4.11e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3311 DKQKDLLDDELQRLKDEvddavkqRGQVEEELFKVKVQMEELLKVKLKIEKENQllIKKDKDKAQQLLAEE---AENMKR 3387
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE-------QQQAEELQQKQAAEQERLKQLEKERLAAQE--QKKQAEEAAKQAALKqkqAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3388 LAKEAAILSVEsQEASRLRQIAEedlvQQRALAEKMLKEKMQAIQEASRlKAEAELLQRQKDLAQEQAQRLLEDKElmqk 3467
Cdd:PRK09510 140 KAAAAAKAKAE-AEAKRAAAAAK----KAAAEAKKKAEAEAAKKAAAEA-KKKAEAEAAAKAAAEAKKKAEAEAKK---- 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3468 rldEETEEYQKSLEAERKRQLEIVAEAEKLKLQVSqlsvAQAKAEEEAKRFKKQAD 3523
Cdd:PRK09510 210 ---KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKA----AAAKAAEKAAAAKAAAE 258
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3444-3717 |
4.15e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3444 LQRQKDLAQEQAQRLLEDKELMQKRLDEeTEEYQKSLEAERKRQLEivaeaekLKLQVSQLsvaqakaEEEAKRFKKQAD 3523
Cdd:pfam05622 19 LDQQVSLLQEEKNSLQQENKKLQERLDQ-LESGDDSGTPGGKKYLL-------LQKQLEQL-------QEENFRLETARD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3524 N--IAARLLETEIAT-KDKSTVMQQLEVERRNNSKEADDLRNA---IANLETEKARLKKDAEELQNKSKemadaQMKQIE 3597
Cdd:pfam05622 84 DyrIKCEELEKEVLElQHRNEELTSLAEEAQALKDEMDILRESsdkVKKLEATVETYKKKLEDLGDLRR-----QVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3598 HEKTM-LQQTFltekemllkkerliedekkrlesQYEEEAKKAKALTDEQERQRKLMEEekkkLHATMDEALSKQKEAER 3676
Cdd:pfam05622 159 ERNAEyMQRTL-----------------------QLEEELKKANALRGQLETYKRQVQE----LHGKLSEESKKADKLEF 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1838104091 3677 EMLNKQKEMQEL--EKKRLEQEK-VLAEENKKLR-DQLQQLEEAQ 3717
Cdd:pfam05622 212 EYKKLEEKLEALqkEKERLIIERdTLRETNEELRcAQLQQAELSQ 256
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2464-2672 |
4.26e-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: 43.40 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2464 RLEDEEKAAKILKAEEQKKMAD-LQAELDKQKKLaEAHAKaiaKAEKEADELKHQMKQEVSKREVAALDAENQKKNIELE 2542
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDrLRAERAEMRRL-EVERK---RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2543 LHELKKLSEQQIND----KSQLVDDALQSRTKIEEEI-HIIRIQLETTLNQKSTAETELKQLREK------AAEAERLRK 2611
Cdd:pfam15709 391 LRKQRLEEERQRQEeeerKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQRQKelemqlAEEQKRLME 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 2612 LAQEEAeklhkqvIEETQKKRTAEEelKRKSEAEKEAAKQKQKALEDLENLKMQAEEAERK 2672
Cdd:pfam15709 471 MAEEER-------LEYQRQKQEAEE--KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2468-2642 |
4.26e-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: 43.45 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2468 EEKAAKILKAEEQKKMADL-QAELDKQKKLAEAHAKAIAKAEKEADELKHQMKQEVskrevaaldAENQKKNIELELHEL 2546
Cdd:pfam05262 220 EELDKKQIDADKAQQKADFaQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQV---------AENQKREIEKAQIEI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2547 KKLSEQQINDKSQLVDDAlqsrtkieeeihiiriqlettlnqKSTAETELKQLREKAAEAERLRKLAQEEAEKlhkqVIE 2626
Cdd:pfam05262 291 KKNDEEALKAKDHKAFDL------------------------KQESKASEKEAEDKELEAQKKREPVAEDLQK----TKP 342
|
170
....*....|....*.
gi 1838104091 2627 ETQKKRTAEEELKRKS 2642
Cdd:pfam05262 343 QVEAQPTSLNEDAIDS 358
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
1152-1252 |
4.40e-03 |
|
first 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, and are probably involved in the 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 40.20 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 1152 QKKTFTKWVNKHLIKRAESQH------HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHKLQNVQIALDF 1220
Cdd:cd21293 2 EKGSYVDHINRYLGDDPFLKQflpidpSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1838104091 1221 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1252
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
2586-2692 |
5.03e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 41.56 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2586 LNQKSTAETELKQLREKAAEAERLRKlaqEEAEKLHKQVIEETQKKRTAEE--ELKRKSEAEKEAAKQKQKALEDLENLK 2663
Cdd:pfam09756 3 LGAKKRAKLELKEAKRQQREAEEEER---EEREKLEEKREEEYKEREEREEeaEKEKEEEERKQEEEQERKEQEEYEKLK 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1838104091 2664 ------------MQAEEAERKVKQ--AQIEKEKQIQIAHVAAE 2692
Cdd:pfam09756 80 sqfvveeegtdkLSAEDESQLLEDfiNYIKLKKVVLLEELAAE 122
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3541-3744 |
5.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3541 TVMQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEmADAQMKQIEHEktmlqqtfLTEKEMLLKKERl 3620
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-LQAEIDKLQAE--------IAEAEAEIEERR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3621 iEDEKKRLESQYEEEA------------------KKAKALTDEQERQRKLMEEekkkLHATMDEALSKQKEAEREMLNKQ 3682
Cdd:COG3883 86 -EELGERARALYRSGGsvsyldvllgsesfsdflDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838104091 3683 KEMQELEKKRLEQEKVLAEENKKLRDQLQQLEEAQKEKNTQVISAATVETTKNVYNGQNAGD 3744
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2550-2762 |
5.58e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2550 SEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAAEAERLRKLAQEEAEKLHKQVIE--- 2626
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2627 ETQKKRTAE------------EELKRKSEAEKEAAKQKQKALEDLENLKMQAEEaerkvKQAQIEKEKQIQIAHVAAEKS 2694
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-----KKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 2695 ATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQEDALKAREEAEKELDKWRQKANEA 2762
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
3427-3537 |
5.60e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 41.08 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3427 KMQA-IQEASRLKAEAELLqrqkdLAQEQAQRllEDKELMQKRLDEETEEYQKSLEAERKRQLEivaEAEKLKLQVSQLS 3505
Cdd:PRK14475 45 KIQAeLDEAQRLREEAQAL-----LADVKAER--EEAERQAAAMLAAAKADARRMEAEAKEKLE---EQIKRRAEMAERK 114
|
90 100 110
....*....|....*....|....*....|..
gi 1838104091 3506 VAQAKAEEEAKrFKKQADNIAARLLETEIATK 3537
Cdd:PRK14475 115 IAQAEAQAAAD-VKAAAVDLAAQAAETVLAAR 145
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
3220-3542 |
5.84e-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: 43.21 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3220 RKQAEEAESQKAAAEKEAAIQAKAQEDAERL---RKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQV 3296
Cdd:pfam09731 100 EVAEEEKEATKDAAEAKAQLPKSEQEKEKALeevLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3297 EQELTKVKLKLDDTDKQK---DLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKDKDK 3373
Cdd:pfam09731 180 ATDSALQKAEALAEKLKEvinLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3374 AQQL---------------LAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLvqQRALAEKMLKEKMQAIQEASRLK 3438
Cdd:pfam09731 260 QQELvsifpdiipvlkednLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHI--ERALEKQKEELDKLAEELSARLE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3439 AEAELLQRQKDLAQEqaqrlledkelmqKRLDEETEEYQKSLEAERKRQLEIVAEA-------EKLKLQVSQLSVAQAKA 3511
Cdd:pfam09731 338 EVRAADEAQLRLEFE-------------REREEIRESYEEKLRTELERQAEAHEEHlkdvlveQEIELQREFLQDIKEKV 404
|
330 340 350
....*....|....*....|....*....|.
gi 1838104091 3512 EEEAKRFKKQADNIAARLLETEIATKDKSTV 3542
Cdd:pfam09731 405 EEERAGRLLKLNELLANLKGLEKATSSHSEV 435
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
1292-1352 |
6.08e-03 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 38.82 E-value: 6.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 1292 DNFTTSWRDGKLFNAVIHKHHPRLIDMGRV---YQQS---NQENLEQAFNVAERDLGVTRL-LDPEDV 1352
Cdd:pfam11971 14 EDLLRDLSDGCALAALIHFYCPQLIDLEDIclkESMSladSLYNIQLLQEFCQRHLGNRCChLTLEDL 81
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2729-2991 |
6.23e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2729 QEAAHLKKQQEDALKArEEAekeldKWRqkaNEALRLRLQAEEEAhkkslaqeeaekqkeeaeREAKKRAKAEESALKQK 2808
Cdd:PRK05035 433 QAKAEIRAIEQEKKKA-EEA-----KAR---FEARQARLEREKAA------------------REARHKKAAEARAAKDK 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2809 EMAEKELER-QRKVADSTAQQKLTAEQE--------LIRLRAEFDNAEQQRSLLEDELYRLKNEVIAA--QQQRKQLEDE 2877
Cdd:PRK05035 486 DAVAAALARvKAKKAAATQPIVIKAGARpdnsaviaAREARKAQARARQAEKQAAAAADPKKAAVAAAiaRAKAKKAAQQ 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2878 LAKMRSEMEILIQLKSRAEKETMSNTEKSKMLLDAEASKMRDVAEEAGKLRAIAEEAKYQRQIAEEEAARQRAEAERILK 2957
Cdd:PRK05035 566 AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRK 645
|
250 260 270
....*....|....*....|....*....|....
gi 1838104091 2958 EKLAAISEATRLKTEAEIALKEKEAENERLRRAA 2991
Cdd:PRK05035 646 AAVAAAIARAKARKAAQQQANAEPEEAEDPKKAA 679
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
3491-3685 |
6.53e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.93 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3491 VAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETeiATKDKSTVMQQLEVERRnnsKEADDLRNAI-ANLET 3569
Cdd:PRK00106 20 VLISIKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKT--AKRESKALKKELLLEAK---EEARKYREEIeQEFKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3570 EKARLKKDAEELQNKSKEMaDAQMKQIEHEKTMLQQtfltEKEMLLKKERLI---EDEKKRLESQYEEEAKKAKALTDEQ 3646
Cdd:PRK00106 95 ERQELKQIESRLTERATSL-DRKDENLSSKEKTLES----KEQSLTDKSKHIderEEQVEKLEEQKKAELERVAALSQAE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1838104091 3647 ERQRKLMEEEKKKLHatmdEALSKQKEAEREMLNKQKEM 3685
Cdd:PRK00106 170 AREIILAETENKLTH----EIATRIREAEREVKDRSDKM 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3618-3736 |
6.63e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3618 ERL--IEDEkkrLESQYE------EEAKKAKALTDE-QERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEMQEL 3688
Cdd:COG1196 189 ERLedILGE---LERQLEplerqaEKAERYRELKEElKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1838104091 3689 EKKRLEQEKVLAEENkklrdqlQQLEEAQKEKNTQVISAATVETTKNV 3736
Cdd:COG1196 266 EAELEELRLELEELE-------LELEEAQAEEYELLAELARLEQDIAR 306
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
3242-3369 |
6.79e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 41.14 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3242 KAQEDAERLRKEAEFEAAK-RAQAENAALEQKKKADAEmakhkklAEQTLKQkfQVEQELTKVKL--KLDDTDKQKDLLD 3318
Cdd:PRK02292 13 EARARASEIRAEADEEAEEiIAEAEADAEEILEDREAE-------AEREIEQ--LREQELSSAKLeaKRERLNARKEVLE 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1838104091 3319 DELQRLKDEVDDAVKQRgqvEEELFKVKVQMEELLKVKLKIEKENQLLIKK 3369
Cdd:PRK02292 84 DVRNQVEDEIASLDGDK---REELTKSLLDAADADGVRVYSRKDDEDLVKS 131
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3619-3724 |
6.86e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3619 RLIEDEKKRlESQYEEEAKKAKAltdEQERQRKLMEEEKKKLHATMDEAlskQKEAEREmLNKQKEMQELEKKRLEQEK- 3697
Cdd:COG2268 196 EIIRDARIA-EAEAERETEIAIA---QANREAEEAELEQEREIETARIA---EAEAELA-KKKAEERREAETARAEAEAa 267
|
90 100
....*....|....*....|....*..
gi 1838104091 3698 VLAEENKKLRDQLQQLEEAQKEKNTQV 3724
Cdd:COG2268 268 YEIAEANAEREVQRQLEIAEREREIEL 294
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
3251-3691 |
6.92e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3251 RKEAEFEAAKRAQAENAALEQKKKADAEMAK--HKKLAEQtLKQKFQVEQELTKvklKLDDTDKQKDLLDDELQ---RLK 3325
Cdd:PRK10246 252 LDELQQEASRRQQALQQALAAEEKAQPQLAAlsLAQPARQ-LRPHWERIQEQSA---ALAHTRQQIEEVNTRLQstmALR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3326 DEV-DDAVKQRGQVEEELFKVKVQMEELLKVKL---KIEKENQLLIKKDKDKAQQLLAEE---AENMKRLAKEAAILSVE 3398
Cdd:PRK10246 328 ARIrHHAAKQSAELQAQQQSLNTWLAEHDRFRQwnnELAGWRAQFSQQTSDREQLRQWQQqltHAEQKLNALPAITLTLT 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3399 SQEASRlrqiAEEDLVQQRALAEKML--------KEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLD 3470
Cdd:PRK10246 408 ADEVAA----ALAQHAEQRPLRQRLValhgqivpQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTI 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3471 EETEEYQKSLEAERKRqLE--------------IVAEAEKLKLQVSQLSVAQakAEEEAKRFKKQADNIAARLleteiat 3536
Cdd:PRK10246 484 CEQEARIKDLEAQRAQ-LQagqpcplcgstshpAVEAYQALEPGVNQSRLDA--LEKEVKKLGEEGAALRGQL------- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3537 kdkSTVMQQLEverRNNSkEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQqtfLTEKEMLlk 3616
Cdd:PRK10246 554 ---DALTKQLQ---RDES-EAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRL---LSQRHEL-- 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3617 keRLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLM----EEEKKKLHATMDEALSKQKeaeremlnKQKEMQELEKK 3691
Cdd:PRK10246 622 --QGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTlpqeDEEASWLATRQQEAQSWQQ--------RQNELTALQNR 690
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3501-3681 |
7.30e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3501 VSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLETEKarlkKDAEE 3580
Cdd:pfam05262 177 ISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQR----DEVRQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3581 LQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKK-ERLIEDEKKRLESQYEEEAKKAKAltDEQERQRKLMEEEKKK 3659
Cdd:pfam05262 253 KQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEiKKNDEEALKAKDHKAFDLKQESKA--SEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|...
gi 1838104091 3660 LHATMD-EALSKQKEAEREMLNK 3681
Cdd:pfam05262 331 EPVAEDlQKTKPQVEAQPTSLNE 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3007-3317 |
7.41e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3007 QHKKEIEEKIVQLK--KSSQAEMQRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKL 3084
Cdd:pfam17380 279 QHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3085 RAEEEAEKQRKLAMEeekrrreaeetVKKITAAEK-EAGRQRKIaqdelDRLKKKAEEARKQK---DKADSEAEKQIVAA 3160
Cdd:pfam17380 359 KRELERIRQEEIAME-----------ISRMRELERlQMERQQKN-----ERVRQELEAARKVKileEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3161 SQAALKCRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLAkeaeaakekaekeavlLRKQAEEAESQKAAAEKEAAIQ 3240
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER----------------LRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3241 AKAQEDaERLRKEAEFEAAKRAQAE--------NAALEQKKKADAE-----MAKHKKLAEQTLKQKFQVEQELTKV---K 3304
Cdd:pfam17380 487 KRAEEQ-RRKILEKELEERKQAMIEeerkrkllEKEMEERQKAIYEeerrrEAEEERRKQQEMEERRRIQEQMRKAteeR 565
|
330
....*....|...
gi 1838104091 3305 LKLDDTDKQKDLL 3317
Cdd:pfam17380 566 SRLEAMEREREMM 578
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2073-2720 |
7.47e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2073 NSTQHFDSLLRSMEKGVMVVKLKgqQDETLCKNYISEIKDLRVLIEDCETSTLARIRKPVEKDPLKECNQKTTDQKKCQV 2152
Cdd:COG5022 765 LQALKRIKKIQVIQHGFRLRRLV--DYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSL 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2153 KLESLKKDLVKVSVKTEEVLASPQKSVSAPVLR---------SELDLTVQKMDHAHMLS----SVYLEKLKTVEMVIR-N 2218
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQrvelaerqlQELKIDVKSISSLKLVNleleSEIIELKKSLSSDLIeN 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2219 TQGAEGVLKQYEDCLREVHTVPSDAKEVESYRAKLKKMRAEAEGEQPVFDsLEEELQKATtvsEKMSRVHSERDiELDHF 2298
Cdd:COG5022 923 LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE-YEDLLKKST---ILVREGNKANS-ELKNF 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2299 RQNVSGLQDRWKAVftqmEIRHRELEQLGRQLGYYHESYDWLIHwITDAKERQEKIQAVSITDSKTLKEQLSQEKKLLEE 2378
Cdd:COG5022 998 KKELAELSKQYGAL----QESTKQLKELPVEVAELQSASKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2379 IENNKENVDEC--QKYAKAYINSIKDYELQLVAYNA-----KADPHASPLKKNKMDSASDNIIQEYVTL----RTRYSEL 2447
Cdd:COG5022 1073 RENSLLDDKQLyqLESTENLLKTINVKDLEVTNRNLvkpanVLQFIVAQMIKLNLLQEISKFLSQLVNTlepvFQKLSVL 1152
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2448 MtLTSQYIKFITETQRRLEDEEKAAKILKAEEQKKMADLQAEL-DKQKKLAEAHAKAIAKAEKEADELKHQMKQEVSKRE 2526
Cdd:COG5022 1153 Q-LELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLsSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGW 1231
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2527 VAALDAENQKKNIELELHELKK--LSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLNQKSTAETELKQLREKAA 2604
Cdd:COG5022 1232 VPTEYSTSLKGFNNLNKKFDTPasMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWK 1311
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2605 EAERLRKLAQEEAEKLHKQVIEETQkkrtaeEELkrksEAEKEAAKQKQKALEDLENLKmQAEEAERKVKQAQIEK---- 2680
Cdd:COG5022 1312 SATEVNYNSEELDDWCREFEISDVD------EEL----EELIQAVKVLQLLKDDLNKLD-ELLDACYSLNPAEIQNlksr 1380
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2681 ----------EKQIQIAHVAaeKSATAELQSTQRSFVEKTSKLEESLKQE 2720
Cdd:COG5022 1381 ydpadkennlPKEILKKIEA--LLIKQELQLSLEGKDETEVHLSEIFSEE 1428
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3378-3685 |
7.62e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3378 LAEEAENMKRLAKEAAILSVESQEASRLRQIAEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQR 3457
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3458 LLEDKELMQKRLdEETEEYQKSLEAERKRQLEIVAEAEKlklQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIatk 3537
Cdd:COG4372 113 LQEELEELQKER-QDLEQQRKQLEAQIAELQSEIAEREE---ELKELEEQLESLQEELAALEQELQALSEAEAEQAL--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3538 dkstvmQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTEKEMLLKK 3617
Cdd:COG4372 186 ------DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838104091 3618 ERLIEDEKKRLESQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKEAEREMLNKQKEM 3685
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2508-2827 |
7.95e-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: 42.33 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2508 EKEADELKhQMKQEVSKREvaALDAENQKKNIELELHElKKLSEQQINDKSQLVDDALQSRTKIEEEIHIIRIQLETTLN 2587
Cdd:pfam15558 37 LRRRDQKR-QETLERERRL--LLQQSQEQWQAEKEQRK-ARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2588 QKSTAETELKQLRE---KAAEAERLRKLAQEEAEkLHKQVIEETQKKRTAEEELKRKSEAEKEAAKQKQKALEDLENLKM 2664
Cdd:pfam15558 113 RARQEAEQRKQCQEqrlKEKEEELQALREQNSLQ-LQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2665 QAEEA------ERKVKQAQIEKEKQIQIAHVAAEKSATAELQSTQRsfVEKTSKLEESLKQEHGTVLQLQQEAAHLKKQQ 2738
Cdd:pfam15558 192 KAEELlrrlslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQR--AKWRAEEKEEERQEHKEALAELADRKIQQARQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2739 EDALKAREEAE--KELDKWRQKANEALRLRLQAEEEAHKKSLAQEeaekqkeeaereAKKRAKAEESALKQKEMAekeLE 2816
Cdd:pfam15558 270 VAHKTVQDKAQraRELNLEREKNHHILKLKVEKEEKCHREGIKEA------------IKKKEQRSEQISREKEAT---LE 334
|
330
....*....|.
gi 1838104091 2817 RQRKVADSTAQ 2827
Cdd:pfam15558 335 EARKTARASFH 345
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2462-2751 |
8.11e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2462 QRRLEDEEK-------AAKILKAEEQKKMADLQA-ELDKQKKLAEAHAkAIAKAEKEADELKHQMKQEVSKRE---VAAL 2530
Cdd:pfam03528 7 QQRVAELEKenaefyrLKQQLEAEFNQKRAKFKElYLAKEEDLKRQNA-VLQEAQVELDALQNQLALARAEMEnikAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2531 DAENQKKNielELHELKKLSEQQINDKSQLVDDALQsrtKIEEEIHIIRIQLETTLNQ-KSTAETELKQLREKAAEAERL 2609
Cdd:pfam03528 86 VSENTKQE---AIDEVKSQWQEEVASLQAIMKETVR---EYEVQFHRRLEQERAQWNQyRESAEREIADLRRRLSEGQEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2610 RKL------AQEEAEKLHKQV------IEETQKKRTAEEELKRKSEAEK--------EAAK---------------QKQK 2654
Cdd:pfam03528 160 ENLedemkkAQEDAEKLRSVVmpmekeIAALKAKLTEAEDKIKELEASKmkelnhylEAEKscrtdlemyvavlntQKSV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2655 ALEDLENLKMQAEEAERKVKQaqiEKEKQIQIAHVAaeKSATAELQSTQRSFVEKTSKLEESLKQEhgtvlQLQQEAAHL 2734
Cdd:pfam03528 240 LQEDAEKLRKELHEVCHLLEQ---ERQQHNQLKHTW--QKANDQFLESQRLLMRDMQRMESVLTSE-----QLRQVEEIK 309
|
330
....*....|....*..
gi 1838104091 2735 KKQQEDALKAREEAEKE 2751
Cdd:pfam03528 310 KKDQEEHKRARTHKEKE 326
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
2455-2546 |
8.22e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2455 IKFITE----TQRRLE---DEEKAAKILKAEEQKKmaDLQAELDKQKKLAEAHAKAIAKA---EKEADELKHQMKQevSK 2524
Cdd:PRK05431 4 IKLIREnpeaVKEALAkrgFPLDVDELLELDEERR--ELQTELEELQAERNALSKEIGQAkrkGEDAEALIAEVKE--LK 79
|
90 100
....*....|....*....|..
gi 1838104091 2525 REVAALDAENqkKNIELELHEL 2546
Cdd:PRK05431 80 EEIKALEAEL--DELEAELEEL 99
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
3249-3610 |
8.40e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3249 RLRKEAEFEAAKRAQAENAALEQKKKADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKDLLDDELQRLKDEV 3328
Cdd:COG5278 128 ALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3329 DDAVKQRGQVEEELFKVKVQMEELLKVKLKIEKENQLLIKKDKDKAQQLLAEEAENMKRLAKEAAILSVESQEASRLRQI 3408
Cdd:COG5278 208 LLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3409 AEEDLVQQRALAEKMLKEKMQAIQEASRLKAEAELLQRQKDLAQEQAQRLLEDKELMQKRLDEETEEYQKSLEAERKRQL 3488
Cdd:COG5278 288 ALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3489 EIVAEAEKLKLQVSQLSVAQAKAEEEAKRFKKQADNIAARLLETEIATKDKSTVMQQLEVERRNNSKEADDLRNAIANLE 3568
Cdd:COG5278 368 AAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASS 447
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1838104091 3569 TEKARLKKDAEELQNKSKEMADAQMKQIEHEKTMLQQTFLTE 3610
Cdd:COG5278 448 ELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEA 489
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
3453-3716 |
8.43e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3453 EQAQRLLEDK--ELMQKRLDEET---EEYQKSLEAERKRQLEIVAEAEKLKLQVSqlsvaqaKAEEEAKRFKKQadniaa 3527
Cdd:pfam00038 24 EQQNKLLETKisELRQKKGAEPSrlySLYEKEIEDLRRQLDTLTVERARLQLELD-------NLRLAAEDFRQK------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3528 rlLETEIATKdkstvmQQLEVERRNNSKEADDLRNAIANLETEKARLKKDAEEL-QNKSKEMADAQmKQIEHEKTMLQ-- 3604
Cdd:pfam00038 91 --YEDELNLR------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLkKNHEEEVRELQ-AQVSDTQVNVEmd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3605 ---QTFLTE--KEMLLKKERLIEDEKKRLESQYE---EEAKKAKALTDEQERQRKlmeEEKKKLHATMDEalskqKEAER 3676
Cdd:pfam00038 162 aarKLDLTSalAEIRAQYEEIAAKNREEAEEWYQsklEELQQAAARNGDALRSAK---EEITELRRTIQS-----LEIEL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1838104091 3677 EMLNKQKEmqELEKKRLEQEKVLAEENKKLRDQLQQLEEA 3716
Cdd:pfam00038 234 QSLKKQKA--SLERQLAETEERYELQLADYQELISELEAE 271
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2808-3030 |
8.81e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2808 KEMAEKELERQRKVADSTAQQKLTAEQELIRLRAEfdnAEQQRSLLEDELyRLKNEVIAA-QQQRKQLeDELAKMRSEME 2886
Cdd:pfam00038 49 YSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDEL-NLRTSAENDlVGLRKDL-DEATLARVDLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2887 ILIQ--------LKSRAE---KETMSNTEKSKMLLDAEASKMRDVAeeagklRAIAEeakyQRQIAEEEAARQRAEAERI 2955
Cdd:pfam00038 124 AKIEslkeelafLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT------SALAE----IRAQYEEIAAKNREEAEEW 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2956 LKEKLAAISEATRLKTEAEIALKEKEAENERL--RRAAEDEAY--QRKALED-----------EANQHKKEIEEKIVQLK 3020
Cdd:pfam00038 194 YQSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASLERqlaeteeryelQLADYQELISELEAELQ 273
|
250
....*....|
gi 1838104091 3021 KSSQaEMQRQ 3030
Cdd:pfam00038 274 ETRQ-EMARQ 282
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3128-3293 |
8.83e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.14 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3128 AQDELDRLKKKAEEARKQKDKADSEAEKQivaASQAALKcRTAEQQVQSVLAQQKEDSMMHKKLQQEYEKAKKLakeaea 3207
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3208 akekaekeavllRKQAEEAesqKAAAEKEAAIQAKA---QEDAERLRKEAEFEAAKRAQAEN--AALEQKKKADAEmAKH 3282
Cdd:TIGR02794 118 ------------QKQAEEA---KAKQAAEAKAKAEAeaeRKAKEEAAKQAEEEAKAKAAAEAkkKAEEAKKKAEAE-AKA 181
|
170
....*....|.
gi 1838104091 3283 KKLAEQTLKQK 3293
Cdd:TIGR02794 182 KAEAEAKAKAE 192
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
2588-2737 |
9.12e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.72 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2588 QKSTAETELKQLREkaaEAERLRKLAQEEAEKLHKqvIEETQKK--RTAEEELKR-------KSEAEKEAAKQkqkaled 2658
Cdd:pfam10168 569 QKEQQLQELQSLEE---ERKSLSERAEKLAEKYEE--IKDKQEKlmRRCKKVLQRlnsqlpvLSDAEREMKKE------- 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2659 LENLKMQAEEAERKVKQAQIEKEKQI-QIAHVA-AEKSATAELQSTQRsfvektSKLEESLKQEHGTVLQLQQEAAHLKK 2736
Cdd:pfam10168 637 LETINEQLKHLANAIKQAKKKMNYQRyQIAKSQsIRKKSSLSLSEKQR------KTIKEILKQLGSEIDELIKQVKDINK 710
|
.
gi 1838104091 2737 Q 2737
Cdd:pfam10168 711 H 711
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
1922-1966 |
9.35e-03 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 9.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1838104091 1922 IQAVCDFK---QQEITVHKGDECALLNNSQPFKWKVLNHSGNEAVVPS 1966
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2929-3164 |
9.65e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2929 AIAEEakYQRQiAEEEAARQRAEAERILKEKlaaiseatrlkTEAEIALKEKEAENERLRraaEDEAYQRKALEdeanQH 3008
Cdd:PRK09510 59 AVVEQ--YNRQ-QQQQKSAKRAEEQRKKKEQ-----------QQAEELQQKQAAEQERLK---QLEKERLAAQE----QK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3009 KKEIEEKIVQLKKSSQAEMQRQKAMVDDTLKqrrvVEEEIRILKLNFEKASSGKldlelelnklKNIAEETQQSKlraeE 3088
Cdd:PRK09510 118 KQAEEAAKQAALKQKQAEEAAAKAAAAAKAK----AEAEAKRAAAAAKKAAAEA----------KKKAEAEAAKK----A 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838104091 3089 EAEKQRKLAMEEEKRRREAEEtvKKITAAEKEAGRQRKIAQDELDRLKKKAEEARKQKDKADSEAEKQIVAASQAA 3164
Cdd:PRK09510 180 AAEAKKKAEAEAAAKAAAEAK--KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
3609-3746 |
9.72e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 3609 TEKEMLLKKERLIEDEKKRLeSQYEEEAKKAKALTDEQERQRKLMEEEKKKLHATMDEALSKQKE---AEREMLNKQKEM 3685
Cdd:COG2433 396 EAEREKEHEERELTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREI 474
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838104091 3686 QELEKKrLEQEKvlaEENKKLRDQLQQLEEAQKEKNTQ------VISAATVETTKNVYN--GQNAGDVV 3746
Cdd:COG2433 475 ERLERE-LEEER---ERIEELKRKLERLKELWKLEHSGelvpvkVVEKFTKEAIRRLEEeyGLKEGDVV 539
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2595-2809 |
9.80e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2595 ELKQLREKAAEAERLRKLAQEEAEKLHKQVIEETQKKRTAEEELKRKSEAEKEAA------KQKQKALEDLENlKMQAE- 2667
Cdd:COG1340 51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNkaggsiDKLRKEIERLEW-RQQTEv 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838104091 2668 ---EAERKVKQAQIEKEKQIQIAHVAAEK--------SATAELQSTQRSFVEKTSKLEESLKQEHGTVLQLQQEAAHLKK 2736
Cdd:COG1340 130 lspEEEKELVEKIKELEKELEKAKKALEKneklkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRK 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838104091 2737 QQEDALKAREEAEKELDKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAerEAKKRAKAEESALKQKE 2809
Cdd:COG1340 210 EADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE--ELEEKAEEIFEKLKKGE 280
|
|
| |
