|
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 ... |
1113-1229 |
8.62e-73 |
|
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: 238.84 E-value: 8.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1113 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQIALD 1192
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGE------------SLPRERGRMRFHRLQNVQTALD 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1193 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 1229
Cdd:cd21188 69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1110-1244 |
3.35e-68 |
|
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: 226.44 E-value: 3.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsvrlPREKGRMRFHKLQNVQI 1189
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL------------PREKGRMRFHKLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 1190 ALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQSE 1244
Cdd:cd21235 69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ----ISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1110-1242 |
4.85e-65 |
|
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: 217.93 E-value: 4.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsvrlPREKGRMRFHKLQNVQI 1189
Cdd:cd21236 12 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTL------------PREKGRMRFHRLQNVQI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 1190 ALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQ 1242
Cdd:cd21236 80 ALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1246-1351 |
1.37e-64 |
|
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: 215.66 E-value: 1.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1655274895 1326 PEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
1247-1351 |
9.73e-64 |
|
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: 213.02 E-value: 9.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1655274895 1327 EDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1110-1243 |
1.42e-57 |
|
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: 196.02 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGdtllserdvarsVRLPREKGRMRFHKLQNVQI 1189
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 1190 ALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQS 1243
Cdd:cd21237 69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1247-1351 |
1.86e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.21 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1655274895 1327 EDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1245-1351 |
1.23e-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: 172.92 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1245 DMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLL 1324
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1655274895 1325 DPEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
7.97e-49 |
|
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: 170.01 E-value: 7.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 7 MPLRELRAIYEVLFRDGVMVAKKDkRPQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRDYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 1655274895 87 HLPPEIVPASLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1115-1230 |
5.17e-48 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 168.33 E-value: 5.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1115 VQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNRALQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21186 70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1247-1347 |
1.56e-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: 163.74 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1655274895 1327 EDVDVPHPDEKSIITYVSSLY 1347
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 ... |
1110-1226 |
3.22e-45 |
|
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: 160.61 E-value: 3.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPR-EKGRMRFHKLQNVQ 1188
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGE------------RLPKpTKGKMRIHCLENVD 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21246 79 KALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1247-1347 |
6.54e-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: 159.10 E-value: 6.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655274895 1327 EDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1981-2058 |
2.05e-41 |
|
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: 148.13 E-value: 2.05e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 1981 LSWQYLMKDFTLIRSWNITMLKTMKPEEYRLILRNLELHYQDFMRDSQDSQLFGPDDRMQIEGDYTKSTQHFDSLLRS 2058
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
1111-1230 |
2.35e-41 |
|
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: 149.45 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1111 ERDRVQKKTFTKWVNKHLIKSQR--HVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRM--RFHKLQN 1186
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655274895 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21241 69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1108-1226 |
2.40e-40 |
|
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: 146.67 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1108 IEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPR-EKGRMRFHKLQN 1186
Cdd:cd21193 9 LQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGE------------KLGKpNRGRLRVQKIEN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1655274895 1187 VQIALDFLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21193 77 VNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
1243-1347 |
1.90e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 143.99 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1243 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1655274895 1323 LLDPEDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
1246-1351 |
2.18e-39 |
|
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: 143.61 E-value: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1655274895 1326 PEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
1234-1349 |
2.77e-39 |
|
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: 143.66 E-value: 2.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
1111-1230 |
8.09e-39 |
|
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: 142.32 E-value: 8.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1111 ERDRVQKKTFTKWVNKHLIK--SQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRM--RFHKLQN 1186
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHKLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655274895 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21190 69 IRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1109-1347 |
1.06e-38 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 156.64 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1109 EDERDRVQKKTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLsGDTLLSERDVARsvrlprekgRMRFHKLQNV 1187
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEAL-QKDNAGEYNETP---------ETRIHVMENV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1188 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILhfqvSSSISDIQvngQSEDMSAKEKLLLWSQRMTDGYQ-GI 1266
Cdd:COG5069 73 SGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1267 RCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLE--NLEQAFNVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYV 1343
Cdd:COG5069 146 DTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
|
....
gi 1655274895 1344 SSLY 1347
Cdd:COG5069 226 SWYI 229
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1087-1226 |
6.97e-38 |
|
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: 140.19 E-value: 6.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1087 ADKAEWDH--SLGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllser 1164
Cdd:cd21317 1 LADDDWDNdnSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGE------ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 1165 dvarsvRLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21317 75 ------QLPKpTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1108-1226 |
1.26e-37 |
|
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: 139.78 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1108 IEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPR-EKGRMRFHKLQN 1186
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGE------------QLPKpTRGRMRIHSLEN 98
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1655274895 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21318 99 VDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1246-1347 |
1.69e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 138.46 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1655274895 1326 PEDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1243-1355 |
7.87e-37 |
|
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: 136.73 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1243 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|...
gi 1655274895 1323 LLDPEDVDVPHPDEKSIITYVSSLYDAMPRTDA 1355
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2362-3219 |
1.55e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.53 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2362 YIDIIKDYELQLVAYKAQVEPLTSPLKKTKL-DSASDNIIQEYVTLRTRYSELMTLTSQYIKF-ITDTQRRLEDEEKAAE 2439
Cdd:PTZ00121 1017 TIDFNQNFNIEKIEELTEYGNNDDVLKEKDIiDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFdFDAKEDNRADEATEEA 1096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2440 KLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEkeaqelKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQ 2519
Cdd:PTZ00121 1097 FGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE------EARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2520 IKDKSQQVDEALKSrlrieEEIHliriqlettvkqksnaedelkqlrdradAAEKLRKlaqeeAEKLRKqvseeTQKKRL 2599
Cdd:PTZ00121 1171 KAEDAKKAEAARKA-----EEVR----------------------------KAEELRK-----AEDARK-----AEAARK 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2600 AEEElkHKSEAERKAANEKQ-KALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSK 2678
Cdd:PTZ00121 1208 AEEE--RKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK 1285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2679 LEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEaerelekwRQKANEALRlrlqAEEEAHKKSLAQEEAEKQKEEADR 2758
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA--------KKKAEEAKK----KADAAKKKAEEAKKAAEAAKAEAE 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2759 EAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQqrsLLEDELYRLKNEVIAAQQERK 2838
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEK 1430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2839 QLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEE--DAARQRA 2916
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKK 1510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2917 EAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILE-DQANQHKLEIEEKIVLLKKSSDAEMER 2995
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2996 QKAIVDdtlkQRRVVEEEIRILKLNFEKASSGKLDLElELNKLKNIAEETQQSKLRAEEEAEKlrrlvlEEEMRRKEAED 3075
Cdd:PTZ00121 1591 EARIEE----VMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKK------AEELKKAEEEN 1659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3076 KVKKIAAAEEEAARQRKAaqEELdrlqKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQN 3155
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKA--EEA----KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3156 KLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKD 3219
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2391-3191 |
1.91e-36 |
|
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: 153.29 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2391 KLDSASDNIIQEYVTLRTRYSELMTLTSQY---IKFitdtqRRLEDEEKAAEKL-----KAEEQKKMAEMQAELDKQKQL 2462
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAekaERY-----KELKAELRELELAllvlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2463 AEAHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQNIQLELHELKNLseqqIKDKSQQVDEALKSRLRIEEEIH 2542
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYALANE----ISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2543 LIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELkhksEAERKAANEKQKAL 2622
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL----ETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2623 EDLENlrmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRK 2702
Cdd:TIGR02168 396 ASLNN---EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2703 QQEDAENAREEAERELEkwRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADRE----AKKRSKAEESALKQR--DM 2776
Cdd:TIGR02168 473 AEQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSElisvDEGYEAAIEAALGGRlqAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2777 AENELERQRRLAESTAQQKL--AAEQELIRLRADFDNAEQQRSLLEDELYR--LKNEVIAAQQERKQLEDELSKVR---- 2848
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNELgrVTFLPLDSIKGTEIQGNDREILKNIEGFLgvAKDLVKFDPKLRKALSYLLGGVLvvdd 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2849 --SEMDILIQLKSR--------------------AEKETMSNTEKSKQLLEAEAtKLRDLAEEASKLRAIAEEAKHQRQL 2906
Cdd:TIGR02168 631 ldNALELAKKLRPGyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEE 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2907 AEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEdQANQHKLEIEEKIVLLk 2986
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL- 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2987 kssDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEE 3066
Cdd:TIGR02168 788 ---EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3067 EMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQ 3146
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1655274895 3147 QKEDSMMqnklkeEYEKAKALARDAEAAKERAEREAALLRQQAEE 3191
Cdd:TIGR02168 945 LSEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-139 |
2.21e-36 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 135.54 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 5 MLMPLRELRAIYEVLFRDGVMVAKKDkRPQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRD 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKD-PKGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 85 YLHLPPEIVPASLQRVRRPASTLAIARGARvqsvegptsyvPKPGRNNEAESEGA 139
Cdd:PTZ00034 80 YLHLPPDVFPATHKKKSVNFERKTEEEGSR-----------GGRGGRGRGRGYGR 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2856-3659 |
4.07e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 152.99 E-value: 4.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2856 QLKSRAEKETmsnTEKSKQLLEAEATKLRDLAEEASKLRAI---AEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDA 2932
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2933 TRLKTEAEIALKEKEAENERLRRQAED--EAYQRKILEDQAN---QHKLEIEEKIVLLKKSSDA----EMERQKAIVDDT 3003
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKaeaARKAEEERKAEEARKAEDAkkaeAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3004 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKlkniAEETQQS-KLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAA 3082
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3083 AEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvlAQQKEDSMmqNKLKEEYE 3162
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKADAA--KKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3163 KAKALARDAEAAKERAE--REAALLRQQAEEAERQKVAAEQEAANQAKAQD--DAERLRKDAEFEAAKLAQAEAAALKQK 3238
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3239 QQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEEL 3318
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3319 MKL-KVRIEEEnqrlmkkdkdntqkflVEEAENMKKLAEDAARLSIEAQEAarlrqiaeddlnqqRTLAEKMLKEKMQAI 3397
Cdd:PTZ00121 1552 KKAeELKKAEE----------------KKKAEEAKKAEEDKNMALRKAEEA--------------KKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3398 QEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKA 3477
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3478 EEEAKKFKKQADTIAARLHEteiatKEQMTEVKKMEFEKLntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMada 3557
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEE-----AKKAEELKKKEAEEK---KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--- 1749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3558 qqKQIEREMTVLQQTFLTEkemllkkEKLIEDEKKKLESQFEEEIKKakalKDEQDRqrqqMEEEKlKLKATMDAALNKQ 3637
Cdd:PTZ00121 1750 --KKDEEEKKKIAHLKKEE-------EKKAEEIRKEKEAVIEEELDE----EDEKRR----MEVDK-KIKDIFDNFANII 1811
|
810 820
....*....|....*....|....
gi 1655274895 3638 KEAEKD--ILNKQKEMQELERKRL 3659
Cdd:PTZ00121 1812 EGGKEGnlVINDSKEMEDSAIKEV 1835
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1115-1228 |
3.52e-35 |
|
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: 131.75 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1115 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvARSVRLPRekgrMRFHKLQNVQIALDFL 1194
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESL------GRYNKNPK----MRVQKLENVNKALEFI 73
|
90 100 110
....*....|....*....|....*....|....
gi 1655274895 1195 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21215 74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
1111-1230 |
7.60e-35 |
|
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: 130.72 E-value: 7.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1111 ERDRVQKKTFTKWVNKHLIKSQ--RHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQ 1188
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655274895 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21242 69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1237-1355 |
8.96e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 131.33 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1237 IQVNGQSEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEK 1316
Cdd:cd21322 7 IETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQ 86
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274895 1317 DLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDAMPRTDA 1355
Cdd:cd21322 87 HLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKA 125
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
1113-1226 |
1.58e-34 |
|
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: 129.82 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1113 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLLserdvarsvrlPREKGRMRFHKLQNVQIALD 1192
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
|
90 100 110
....*....|....*....|....*....|....
gi 1655274895 1193 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21214 72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1247-1347 |
1.97e-34 |
|
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: 129.45 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655274895 1327 EDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1250-1351 |
3.11e-34 |
|
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: 128.70 E-value: 3.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1250 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 1328
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655274895 1329 VDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2528-3445 |
9.89e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 145.28 E-value: 9.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2528 DEALKSRLRIEEEI---HLIRIQLETTVKQK-----SNAEDELKQLRD-RADAAEKLRKLAQEEAEKLRKQVSEETQKKr 2598
Cdd:PTZ00121 1039 DDVLKEKDIIDEDIdgnHEGKAEAKAHVGQDeglkpSYKDFDFDAKEDnRADEATEEAFGKAEEAKKTETGKAEEARKA- 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2599 laEEELKHKSEAERKAANEKQKALEDLENLRmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELR-SKQMSFAENVS 2677
Cdd:PTZ00121 1118 --EEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARkAEEVRKAEELR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2678 KLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAD 2757
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRS---KAEESAlKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDElyRLKNEVIAAQ 2834
Cdd:PTZ00121 1275 EEARKADelkKAEEKK-KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAE 1351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2835 QERKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQlleaEATKLRDLAEEASKLRAIAEEAKhqrqlaEEDAARQ 2914
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAA---EKKKEEAKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELK------KAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2915 RAEAeriLKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEME 2994
Cdd:PTZ00121 1419 KADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2995 RQKAivdDTLKQRRVVEEEIRILKLNFEKASSgkldlelelNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAE 3074
Cdd:PTZ00121 1496 KKKA---DEAKKAAEAKKKADEAKKAEEAKKA---------DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK 1563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3075 DKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCnmaeQQVQSVLAQQKEDSMMQ 3154
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA----EELKKAEEEKKKVEQLK 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3155 NKLKEEYEKAKALARDAEAAKERAEREAallrQQAEEAERQKVAAEQEAANQAKAqddAERLRKDAEfeaaklaqAEAAA 3234
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEA----KKAEEDKKKAEEAKKAEEDEKKA---AEALKKEAE--------EAKKA 1704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3235 LKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKlqlEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQ 3314
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE---EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3315 MEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAArlrqiaeDDLNQQRTLAEKMLKEKM 3394
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVA-------DSKNMQLEEADAFEKHKF 1854
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3395 QAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKqlMQQRLDEETEEYQRS 3445
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD--EIEKIDKDDIEREIP 1903
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2429-3165 |
1.65e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 144.51 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2429 RRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLE 2508
Cdd:PTZ00121 1176 KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2509 LHELKNLSEQQIKDKSQQVDEALKS-------------RLRIEEEIHLIRiQLETTVKQKSNAEDELKQLRDRADAAEKL 2575
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKAdelkkaeekkkadEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2576 RKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKAledlENLRMQAEE---AERQVKQAEVEKERQIQV 2652
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEkkkADEAKKKAEEDKKKADEL 1410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2653 AHVAAQQSAAAELRSKqmsfAENVSKLEESLK--QEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKwrQKANEAlr 2730
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKK----AEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEA-- 1482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2731 lrlQAEEEAHKKSlaqeeaeKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFD 2810
Cdd:PTZ00121 1483 ---KKADEAKKKA-------EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2811 NAEQQRSlledelyrlKNEVIAAQQERKQLEDELSKVRsEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEA 2890
Cdd:PTZ00121 1553 KAEELKK---------AEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2891 SKLRAIAEEAKHQRQLAEEDAARQRaEAERILKEKLAAISDATRLKTEAEialkEKEAENERLRRQAEDEayqrkilEDQ 2970
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDE-------KKA 1690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2971 ANQHKLEIEEKivllkkssdaemerQKAivddtlKQRRVVEEEirilklnfEKASSGKLDLELELNKLKniaeeTQQSKL 3050
Cdd:PTZ00121 1691 AEALKKEAEEA--------------KKA------EELKKKEAE--------EKKKAEELKKAEEENKIK-----AEEAKK 1737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3051 RAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRL-QKKADEVRKQKEEADKEAEKQIVAAQQA 3129
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEdEKRRMEVDKKIKDIFDNFANIIEGGKEG 1817
|
730 740 750
....*....|....*....|....*....|....*.
gi 1655274895 3130 ALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAK 3165
Cdd:PTZ00121 1818 NLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHK 1853
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2425-3658 |
3.48e-33 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 142.66 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2425 TDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELdkqkqlaeaHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEkqkqn 2504
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2505 iqlelhELKNLSEQQIK---DKSQQVDEALKSRLRIEEEihliRIQLETTVKQKSNAEDElkqlrdRADAAEKLRKlAQE 2581
Cdd:NF041483 156 ------QLRARTESQARrllDESRAEAEQALAAARAEAE----RLAEEARQRLGSEAESA------RAEAEAILRR-ARK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2582 EAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQaeEAERQVKQAEVEKERQIQVA-HVAAQQS 2660
Cdd:NF041483 219 DAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAkEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2661 AAAELRSKQMS---------FAENVSKLEESLKQEHGTVLQ-LQQDAERLRKQqedaenareeaerelekwrqkANEALR 2730
Cdd:NF041483 297 ASAESANEQRTrtakeeiarLVGEATKEAEALKAEAEQALAdARAEAEKLVAE---------------------AAEKAR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2731 lRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSK-AEESALKQRDMAENELERQRRLAESTAQQ-KLAA---------- 2798
Cdd:NF041483 356 -TVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRaAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAkddtkeyrak 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2799 ----EQELIRLRADfdnAEQQRSLLEDELYRLKNE-----VIAAQQERKQLEDELSKVRSEMDiliQLKSRAEKEtmsnT 2869
Cdd:NF041483 435 tvelQEEARRLRGE---AEQLRAEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADAD---ELRSTATAE----S 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2870 EKSKQLLEAEATKLRDLAE--------EASKLRAIAEE-AKHQRQLAEEDAARQRAEAERILKEKLA-AISDATRLKTEA 2939
Cdd:NF041483 505 ERVRTEAIERATTLRRQAEetlertraEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEA 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2940 E-------IALKEKEAENERLRRQAEDEayqrkiledqANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEE 3012
Cdd:NF041483 585 EerltaaeEALADARAEAERIRREAAEE----------TERLRTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3013 EIRIlKLNFEKASsgkldlelELNKLKNIAEETQQsKLRAE----------EEAEKLRRLVLEEEMRRKEAEDkvkKIAA 3082
Cdd:NF041483 655 NVAV-RLRSEAAA--------EAERLKSEAQESAD-RVRAEaaaaaervgtEAAEALAAAQEEAARRRREAEE---TLGS 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3083 AEEEAARQRKAAQEELDRLQKKAdevRKQKEEADKEAEKQIVAAQQAALK-CNMAEQQVQSVlaqqkedsmmqnklkeey 3161
Cdd:NF041483 722 ARAEADQERERAREQSEELLASA---RKRVEEAQAEAQRLVEEADRRATElVSAAEQTAQQV------------------ 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3162 ekakalaRDAEAA-KERAEREAALLRQQAEE-AERQKvaaeqeaanqAKAQDDAERLRKDAefeAAKLAQAEAAALKQKQ 3239
Cdd:NF041483 781 -------RDSVAGlQEQAEEEIAGLRSAAEHaAERTR----------TEAQEEADRVRSDA---YAERERASEDANRLRR 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3240 QADEEMAKHKKLAEQTlkqkfqveqeltkVKLQLEETDKQKSLLDDELQRLKDEVD--------DAMRQKASVEEELFKV 3311
Cdd:NF041483 841 EAQEETEAAKALAERT-------------VSEAIAEAERLRSDASEYAQRVRTEASdtlasaeqDAARTRADAREDANRI 907
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3312 K----IQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMK-KLAEDAARLSIEAQ-EAARLRQIAEDDLNQQRTL 3385
Cdd:NF041483 908 RsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQH 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3386 AEKMLKekmqaiqEASRLKAEAEM-LQRQKDLAQEQAQKLLEDKQlmqqrldeETEEYQRSLEAERKRQLEIIAEAEKLK 3464
Cdd:NF041483 988 AERIRT-------EAERVKAEAAAeAERLRTEAREEADRTLDEAR--------KDANKRRSEAAEQADTLITEAAAEADQ 1052
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3465 LqvsqLSEAQAKAEEEAKKFKKQADTI--AARLHETEI---ATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKE-KA 3538
Cdd:NF041483 1053 L----TAKAQEEALRTTTEAEAQADTMvgAARKEAERIvaeATVEGNSLVEKARTDADELLVGARRDATAIRERAEElRD 1128
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3539 RLKKEAEE-HQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQ 3617
Cdd:NF041483 1129 RITGEIEElHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKA 1208
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|.
gi 1655274895 3618 QMEEEKLKLKATMDAalnkqkEAEKDILNKQKEMQELERKR 3658
Cdd:NF041483 1209 ELVREAEKIKAEAEA------EAKRTVEEGKRELDVLVRRR 1243
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1110-1230 |
6.38e-33 |
|
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: 125.42 E-value: 6.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1110 DERDRVQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQ 1188
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHALNNVN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655274895 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21231 69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
1246-1344 |
8.77e-33 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 124.84 E-value: 8.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1655274895 1326 PEDVDVPHPDEKSIITYVS 1344
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
1246-1344 |
2.43e-31 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 120.71 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1655274895 1326 PEDVDVPHPDEKSIITYVS 1344
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1088-1226 |
3.13e-31 |
|
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: 122.07 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1088 DKAEWDH--SLGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserd 1165
Cdd:cd21316 24 DVDEWDNenSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGE------- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 1166 varsvRLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21316 97 -----RLPKpTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2429-3008 |
6.28e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.06 E-value: 6.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2429 RRLEDEEKAAEK---LKAEEQKKMAEMQA-ELDKQKQLAEAHAKAIAKAEKEAQELklrmQEEVSKRETAAVDAEKQKQN 2504
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKELEAELLLlKLRELEAELEELEAELEELEAELEEL----EAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2505 IQLELHELKnlseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAE 2584
Cdd:COG1196 279 LELELEEAQ----AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2585 KLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE 2664
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2665 LRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSL 2744
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2745 AQEEAEKQKEEADREAKKRSKAE------ESALKQRDMAENElERQRRLAESTAQQKL--AAEQELIRLRADFDNAEQQR 2816
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEaaleaaLAAALQNIVVEDD-EVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2817 SLLEDELYRLKNEVIAAQQERKQLEDELSKVRsemdILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAI 2896
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGR----TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2897 AEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQAnqhkL 2976
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE----E 745
|
570 580 590
....*....|....*....|....*....|..
gi 1655274895 2977 EIEEKIVLLKKSSDAEMERQKAIVDDtLKQRR 3008
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELER-LEREI 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3037-3684 |
7.45e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 135.65 E-value: 7.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3037 KLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQ--------RKAAQEELDRLQKKADEV 3108
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkaeeaRKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3109 RKQKEEADKEAEKQIVAAQQAaLKCNMAEQQVQSVLAQQKEDSmmqnKLKEEYEKAKALARDAEAAKERAEREAALLRQQ 3188
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKA-EEVRKAEELRKAEDARKAEAA----RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3189 AEEAER-QKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELT 3267
Cdd:PTZ00121 1239 AEEAKKaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3268 KVKLQLEETDKQKSLLDD--ELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMK--LKVRIEEENQRLMKKDKDNTQKF 3343
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeAKKKADAAKKKAEEKKKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3344 LVEE----AENMKKlAEDAARLSIEAQEAARLRQIAEDdlnqqrtlaekmLKEKMQAIQEASRLKAEAEmlqrQKDLAQE 3419
Cdd:PTZ00121 1399 KAEEdkkkADELKK-AAAAKKKADEAKKKAEEKKKADE------------AKKKAEEAKKADEAKKKAE----EAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3420 QAQKLLEDKQlmQQRLDEETEEYQRSLEAERKrqleiiaeAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETE 3499
Cdd:PTZ00121 1462 AKKKAEEAKK--ADEAKKKAEEAKKADEAKKK--------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3500 IATKEQmtEVKKM-EFEKLNTSKEADDLRKAiteLEKEKARLKKEAEEHQN----KSKEMADAQQKQIEREMTVLQQTFL 3574
Cdd:PTZ00121 1532 EAKKAD--EAKKAeEKKKADELKKAEELKKA---EEKKKAEEAKKAEEDKNmalrKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3575 TEKEMLLKKE---------KLIEDEKKKLES---QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALN-KQKEAE 3641
Cdd:PTZ00121 1607 MKAEEAKKAEeakikaeelKKAEEEKKKVEQlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEED 1686
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1655274895 3642 KDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQK 3684
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2401-2980 |
1.11e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 134.29 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2401 QEYVTLRTRYSELmtLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEmQAELDKQKQLAEAHAKAIAKAEKEAQEL 2480
Cdd:COG1196 213 ERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2481 KLRMQEEVSKRETAAVDAEKQKQNIQLELHELknlsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAED 2560
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2561 ELKQL-RDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLrmQAEEAERQV 2639
Cdd:COG1196 366 ALLEAeAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--EEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2640 KQAEVEKERQIQVAHVAAQQSaAAELRSKQMSFAENVSKLEESLKQEHgTVLQLQQDAERLRKQQEDAENAREEAERELE 2719
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLEL-LAELLEEAALLEAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2720 KWRQKaneALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAE 2799
Cdd:COG1196 522 LAGAV---AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2800 QELIRLRADFDNAEQQRSLLEDELY---RLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKEtmsnTEKSKQLL 2876
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----RRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2877 EAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQ 2956
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
570 580
....*....|....*....|....
gi 1655274895 2957 AEDEAYQRKILEDQANQHKLEIEE 2980
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1234-1349 |
2.38e-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: 118.01 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1234 ISDIQvngqSEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1314 AEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2946-3715 |
2.76e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 133.73 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2946 KEAENERLRRQAEDEAYQ--RKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVE----EEIRILKL 3019
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3020 NFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIaaaeeeaarqRKAAQEELD 3099
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA----------RKAEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3100 RLQKKADEVRKQKEEAdKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAlardAEAAKERAE 3179
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA----DEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3180 REAALLRQQAEEAERqkvaaeqeaanqakaqddAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQK 3259
Cdd:PTZ00121 1302 KKADEAKKKAEEAKK------------------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3260 FQVEQEltkvKLQLEETDKQKslldDELQRLKDEVDDAMRQKASVEEElfkvKIQMEELMKL---KVRIEEENQRLMKKD 3336
Cdd:PTZ00121 1364 EKAEAA----EKKKEEAKKKA----DAAKKKAEEKKKADEAKKKAEED----KKKADELKKAaaaKKKADEAKKKAEEKK 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3337 KDNTQKFLVEEaenmKKLAEDAARLSIEAQEAARLRQIAEddlnQQRTLAEkmLKEKMQAIQEASRLKAEAEMLQRQKD- 3415
Cdd:PTZ00121 1432 KADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAE----EAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADe 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3416 --LAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAA 3493
Cdd:PTZ00121 1502 akKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3494 RLHETEIATKEQMTEVKKMEFEKlnTSKEADDLRKAitELEKEKARLKKEAEEHQNKSKEMADAQQKQIERemtvlqqtf 3573
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEE--KKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK--------- 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3574 lteKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQE 3653
Cdd:PTZ00121 1649 ---AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 3654 LERK-RLEQERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVEKR 3715
Cdd:PTZ00121 1726 EENKiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1115-1230 |
3.00e-30 |
|
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: 117.39 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1115 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGdtllseRDVARSVRLPRekgrMRFHKLQNVQIALDFL 1194
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQG------RKLGRVIKKPL----NQHQKLENVTLALKAM 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655274895 1195 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21227 74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2536-3128 |
8.36e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.21 E-value: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2536 RIEEEIHLIRIQLETTVKQKSNAE--DELKQLRDRADAAEKLRKL--AQEEAEKLRKQVSEETQKKRLAEEELKHKsEAE 2611
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAEryRELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAEL-EAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2612 RKAANEKQKALEDLENlRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVL 2691
Cdd:COG1196 269 LEELRLELEELELELE-EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2692 QLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESAL 2771
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2772 KQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDElskvrsem 2851
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-------- 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2852 diliqlksRAEKETMSNTEKSKQLLEAEATKLRDLAEEAS--KLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAI 2929
Cdd:COG1196 500 --------EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2930 SDATRLkteAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRV 3009
Cdd:COG1196 572 GRATFL---PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3010 VEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAAR 3089
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
570 580 590
....*....|....*....|....*....|....*....
gi 1655274895 3090 QRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 3128
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1250-1352 |
1.08e-29 |
|
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: 116.18 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1250 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1655274895 1328 DVDVPHPDEKSIITYVSSLYDAMPR 1352
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1111-1230 |
1.66e-29 |
|
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: 115.75 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1111 ERDRVQKKTFTKWVNKHLIKSQR--HVTDLYEDLRDGHNLISLLEVLSGDTLLSERdvarsvrlprEKGRMRFHKLQNVQ 1188
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEY----------KPSSHRIFRLNNIA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655274895 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21191 71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2607-3441 |
3.72e-29 |
|
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: 129.41 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2607 KSEAERK--AANEKQKALED--------LENLRMQAEEAER--QVKQAEVEKERQIQVAHVaaqQSAAAELRSKQMSFAE 2674
Cdd:TIGR02168 174 RKETERKleRTRENLDRLEDilnelerqLKSLERQAEKAERykELKAELRELELALLVLRL---EELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2675 NVSKLEESLKQEHgtvlQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEA-LRLRLQAEEEAHKKSlAQEEAEKQK 2753
Cdd:TIGR02168 251 AEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLER-QLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2754 eeadreakkrskaeESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAA 2833
Cdd:TIGR02168 326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2834 QQERKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQLLEAEatkLRDLAEEASKLRAIAEEAKHQRQLAEEDAAR 2913
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2914 QRAEAERILKEKLAAISDATRLKTEAEIAlkekeaenERLRRQAEDEAYQRKILEDQANQ---------HKLEIEEK--- 2981
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGyea 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2982 ---IVLLKKSSDAEMERQKAIVD--DTLKQ-----------RRVVEEEIRILKLNFEKASSGKLDLELELNKLK------ 3039
Cdd:TIGR02168 538 aieAALGGRLQAVVVENLNAAKKaiAFLKQnelgrvtflplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDpklrka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3040 ------------NIAEETQQSKLRAEEE-------------------AEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAA 3088
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3089 RQRKAAQEELDRLQKKADEVRKQKEeadkEAEKQIVAAQQAALKcnmAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALA 3168
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLAR---LEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3169 RDAEAAKERAEREAALLRQQAEEAERQKvaaEQEAANQAKAQDDAERLRKDAefeaaklaqaeAAALKQKQQADEEMAKH 3248
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEEL---KALREALDELRAELTLLNEEA-----------ANLRERLESLERRIAAT 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3249 KKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEE 3328
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3329 NQRLMKKDKD---NTQKFLVEEAENMKKLAEDAarlSIEAQEAARLRQIAEDDLNQQR---TLAEKMLKE----KMQAIQ 3398
Cdd:TIGR02168 917 LEELREKLAQlelRLEGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARrrlKRLENKIKElgpvNLAAIE 993
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1655274895 3399 EASRLKAEAEMLQRQKDLAQEQAQKLLEdkqlMQQRLDEETEE 3441
Cdd:TIGR02168 994 EYEELKERYDFLTAQKEDLTEAKETLEE----AIEEIDREARE 1032
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1115-1230 |
7.99e-29 |
|
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: 113.57 E-value: 7.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1115 VQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsvrlPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSL------------PKERGSTRVHALNNVNRVLQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21232 70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2605-3195 |
8.52e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.13 E-value: 8.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2605 KHKSEAERKAANEKQKALED--------LENLRMQAEEAER--QVKQAEVEKERQIQVAH-------VAAQQSAAAELRS 2667
Cdd:COG1196 174 KEEAERKLEATEENLERLEDilgelerqLEPLERQAEKAERyrELKEELKELEAELLLLKlreleaeLEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2668 KQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQE 2747
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2748 EAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLK 2827
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2828 NEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLA 2907
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2908 EEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKK 2987
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2988 SSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEE 3067
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3068 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAAlkcnmAEQQVQSVLAQQ 3147
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER-----LEEELEEEALEE 728
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1655274895 3148 KEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAAlLRQQAEEAERQ 3195
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLERE 775
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-105 |
1.04e-28 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 113.10 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 5 MLMPLRELRAIYEVLFRDGVMVAKKDKRpQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRD 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|.
gi 1655274895 85 YLHLPPEIVPASLQRVRRPAS 105
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ 99
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1250-1351 |
1.25e-28 |
|
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: 112.74 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1250 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 1328
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655274895 1329 VDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1114-1231 |
1.26e-28 |
|
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: 113.70 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGR--MRFHKLQNVQIAL 1191
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGK------------KFPKFNKRptFRSQKLENVSVAL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655274895 1192 DFLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21311 82 KFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1252-1347 |
2.75e-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: 111.67 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1252 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED-VD 1330
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1655274895 1331 VPHPDEKSIITYVSSLY 1347
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2428-3354 |
3.95e-28 |
|
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: 126.24 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2428 QRRLEDEEKAAE----KLKAEEQKKMAEMQAELDKQ---KQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEK 2500
Cdd:pfam02463 153 ERRLEIEEEAAGsrlkRKKKEALKKLIEETENLAELiidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2501 QKQNIQLELHELKNLSEQQIKDKSQQVDEAlksrlRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQ 2580
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEK-----EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2581 EEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQS 2660
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2661 AAAELRSKQMSFAENVSKLEESLKQEhgtvLQLQQDAERLRKQQEDAenareeaerelekwrqKANEALRLRLQAEEEAH 2740
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLEL----ARQLEDLLKEEKKEELE----------------ILEEEEESIELKQGKLT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2741 KKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLE 2820
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2821 DELYRLKnEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEA 2900
Cdd:pfam02463 528 HGRLGDL-GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2901 KHQRQLAEEDAARQRAeAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEE 2980
Cdd:pfam02463 607 QLDKATLEADEDDKRA-KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2981 KIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFekassgkldLELELNKLKNIAEETQQSKLRAEEEAEKLR 3060
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR---------VQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3061 RLVLEEEMRRKEAEDKVKKIAAAEEEAARQrKAAQEELDRLQKKADEVRKQKEEADKEAEKQivaaQQAALKCNMAEQQV 3140
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKL-KVEEEKEEKLKAQEEELRALEEELKEEAELL----EEEQLLIEQEEKIK 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3141 QSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDA 3220
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3221 EFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKF-----QVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVD 3295
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEennkeEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3296 DAMRQKASVEEElfKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKL 3354
Cdd:pfam02463 992 KDELEKERLEEE--KKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1114-1228 |
6.20e-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: 111.03 E-value: 6.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsVRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPL---------KRSYNRRPAFQQHYLENVSTALKF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21183 74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3060-3691 |
9.86e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.66 E-value: 9.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3060 RRLVLEE-------EMRRKEAEdkvkkiaaaeeeaaRQRKAAQEELDRLQKKADEVRKQKEEADKEAEK----QIVAAQQ 3128
Cdd:COG1196 157 RRAIIEEaagiskyKERKEEAE--------------RKLEATEENLERLEDILGELERQLEPLERQAEKaeryRELKEEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3129 AALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAK 3208
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3209 AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQ 3288
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3289 RLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmkkdKDNTQKFLVEEAENMKKLAEDAARLSIEAQEA 3368
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL----EEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3369 ARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQ------------------- 3429
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayea 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3430 --------LMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQA-DTIAARLHETEI 3500
Cdd:COG1196 539 aleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAsDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3501 ATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQtfltEKEML 3580
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA----EEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3581 LKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQElERKRLE 3660
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER-ELERLE 773
|
650 660 670
....*....|....*....|....*....|....*....
gi 1655274895 3661 QER-------VLA-DENQKLREKLQQMEEaQKSTLITEK 3691
Cdd:COG1196 774 REIealgpvnLLAiEEYEELEERYDFLSE-QREDLEEAR 811
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2758-3646 |
1.37e-27 |
|
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: 124.31 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQER 2837
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2838 KQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLA-EEASKLRAIAEEAKHQRQLAEEDAARQRA 2916
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLkLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2917 EAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK--------ILEDQANQHKLEIEEKIVLLKKS 2988
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEserlssaaKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2989 SDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKniAEETQQSKLRAEEEAEKLRRLVLEEEM 3068
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE--LELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3069 RRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQK 3148
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3149 EDSMMQNKLKEEYEKAKA-LARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKL 3227
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLpLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3228 AQAEAAA-LKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEvddamrqkasvee 3306
Cdd:pfam02463 652 VSLEEGLaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE------------- 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3307 elfKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLA 3386
Cdd:pfam02463 719 ---AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 EKMLKEKMQAIQEASRLKAEaemLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEaeKLKLQ 3466
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK--EELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3467 VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEK-ARLKKEAE 3545
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLlEEADEKEK 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3546 EHQNKSKEMADAQQKQIERE-------MTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQ 3618
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEelgkvnlMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
890 900
....*....|....*....|....*...
gi 1655274895 3619 MEEEKLKLKATMDAALNKQKEAEKDILN 3646
Cdd:pfam02463 1031 KGWNKVFFYLELGGSAELRLEDPDDPFS 1058
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
1234-1349 |
2.97e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 109.79 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2436-3318 |
7.72e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 121.86 E-value: 7.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2436 KAAEKLKAEEQKKMAEMQAELDkqKQLAEAHAKA-----------IAKAEKEAQELKLRMQEEVSKRETAAVD------- 2497
Cdd:NF041483 323 KEAEALKAEAEQALADARAEAE--KLVAEAAEKArtvaaedtaaqLAKAARTAEEVLTKASEDAKATTRAAAEeaerirr 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2498 -AEKQKQNIQLELHELKNLSEQQIKDKSQQV--------DEALKSR-----LRIEEEIHLIRIQLET---TVKQKSNAED 2560
Cdd:NF041483 401 eAEAEADRLRGEAADQAEQLKGAAKDDTKEYraktvelqEEARRLRgeaeqLRAEAVAEGERIRGEArreAVQQIEEAAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2561 ELKQLRDRADA-AEKLRKLAQEEAEKLRKQVSEE-TQKKRLAEEELKH-KSEAERKAAnekqKALEDLENLRMQAEEAER 2637
Cdd:NF041483 481 TAEELLTKAKAdADELRSTATAESERVRTEAIERaTTLRRQAEETLERtRAEAERLRA----EAEEQAEEVRAAAERAAR 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2638 QVKQaevEKERQIQvahvAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDA----ERLR----------KQ 2703
Cdd:NF041483 557 ELRE---ETERAIA----ARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAaeetERLRteaaerirtlQA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2704 QEDAENAREEAERELEKWRQKA---NEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKR---------SKAEESAL 2771
Cdd:NF041483 630 QAEQEAERLRTEAAADASAARAegeNVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvgteaaealAAAQEEAA 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2772 KQRDMAENELERQRRLAESTAQQKLAAEQELI---RLRADFDNAEQQRsLLEDELYRLKNEVIAAQQERKQLEDELSKVR 2848
Cdd:NF041483 710 RRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLQ 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2849 SEMDILIQ-LKSRAE---KETMSNTEKSKQLLEAEATKLRDLA-EEASKLRAIA-EEAKHQRQLAEEDAARQRAEAERIL 2922
Cdd:NF041483 789 EQAEEEIAgLRSAAEhaaERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLR 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2923 KEklaAISDATRLKTEAEIALKEKEAENERLRRQAEDEAyqRKILEDQANQHKLEIEEkivllkKSSDAEMERQKAIVDD 3002
Cdd:NF041483 869 SD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDA--NRIRSDAAAQADRLIGE------ATSEAERLTAEARAEA 937
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3003 TLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSklrAEEEAEKLRRlvlEEEMRRKEAEdkvkkiaa 3082
Cdd:NF041483 938 ERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGS---AQQHAERIRT---EAERVKAEAA-------- 1003
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3083 aeEEAARQRKAAQEELDRL------------QKKADEVRKQKEEADKEAEKQIVAAQQAALKCNM-AEQQVQS-VLAQQK 3148
Cdd:NF041483 1004 --AEAERLRTEAREEADRTldearkdankrrSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTeAEAQADTmVGAARK 1081
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3149 EDSMMQNKLKEE----YEKAKAlarDAEAAKERAEREAALLRQQAEEAeRQKVAAEQEAANQAKAQDDAERLRKDAEFEA 3224
Cdd:NF041483 1082 EAERIVAEATVEgnslVEKART---DADELLVGARRDATAIRERAEEL-RDRITGEIEELHERARRESAEQMKSAGERCD 1157
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3225 AKLAQAEAAALKQKQQADEEMAKHK-----------KLAEQTLKQKFQVEQELTKvklqleETDKQKSLLDDELQRL--- 3290
Cdd:NF041483 1158 ALVKAAEEQLAEAEAKAKELVSDANseaskvriaavKKAEGLLKEAEQKKAELVR------EAEKIKAEAEAEAKRTvee 1231
|
970 980
....*....|....*....|....*....
gi 1655274895 3291 -KDEVDDAMRQKASVEEELFKVKIQMEEL 3318
Cdd:NF041483 1232 gKRELDVLVRRREDINAEISRVQDVLEAL 1260
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
1233-1349 |
1.25e-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: 107.86 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1233 SISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFN 1312
Cdd:cd21290 3 AIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFE 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 1313 VAEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21290 79 VAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2874-3684 |
1.65e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.93 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2874 QLLEAEATKLRDLAEEA---SKLRAIAEEAkhQRQLAEEDAARQRAEAerILKEKLAAISdatRLKTEAEIALKEKEAEN 2950
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiSKYKERRKET--ERKLERTRENLDRLED--ILNELERQLK---SLERQAEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2951 ERlrrqaedEAYQRKILEDQANQHKLEIEEKivllkKSSDAEMERQKAIVDDTLKqrrVVEEEIRILKLNFEKASSGKLD 3030
Cdd:TIGR02168 221 EL-------RELELALLVLRLEELREELEEL-----QEELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3031 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 3110
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3111 QKEEADKEAEKQIVAAQQAALKCNMAEQQvqsvlaqqkedsmmQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAE 3190
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQ--------------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3191 EAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQE----L 3266
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaL 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3267 TKVKLQLE----------ETDKQKSL-----LDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQR 3331
Cdd:TIGR02168 512 LKNQSGLSgilgvlseliSVDEGYEAaieaaLGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3332 LMKKDKDNTQKFLVEEAENMKKLA----------------EDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQ 3395
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3396 AI---QEASRLKAEAEMLQRQKDLAQEQAQKLLEDkqlmQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSE 3472
Cdd:TIGR02168 672 ILerrREIEELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3473 AQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKsK 3552
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-L 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3553 EMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA 3632
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 3633 ALNKQKEAEKDILNKQKEMQELERkRLEQERVLADENQ-KLREKLQQMEEAQK 3684
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQeRLSEEYSLTLEEAE 957
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2572-3558 |
3.03e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.93 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2572 AEKLRKLAQEEAEKLRKQVSEETQKKRlAEEELKHKSEAERKAanekqkaledlenlRMQAE---EA--ERQVKQAEVEK 2646
Cdd:NF041483 74 AEQLLRNAQIQADQLRADAERELRDAR-AQTQRILQEHAEHQA--------------RLQAElhtEAvqRRQQLDQELAE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2647 ERQIQVAHVAAQQSAAAELRSKQMSFAENVskLEESLKQEHGTVLQLQQDAERLRKQ--QEDAENAREEAERELEKWRQK 2724
Cdd:NF041483 139 RRQTVESHVNENVAWAEQLRARTESQARRL--LDESRAEAEQALAAARAEAERLAEEarQRLGSEAESARAEAEAILRRA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2725 ANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSkAEESALKQRDMAenELERQRRLAESTAQQKLA-AEQELI 2803
Cdd:NF041483 217 RKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQA-AELSRAAEQRMQ--EAEEALREARAEAEKVVAeAKEAAA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2804 RLRADFDNAEQQRS-LLEDELYRLKNEVIA-AQQERKQLEDELSKVRSEMDILI-----QLKSRAEKETMSNTEKSKQLL 2876
Cdd:NF041483 294 KQLASAESANEQRTrTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVaeaaeKARTVAAEDTAAQLAKAARTA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2877 EAEATKLRDLAEEASklRAIAEEAKHQRQLAEEDAARQRAEAERILKE-KLAAISD--------------ATRLKTEAEI 2941
Cdd:NF041483 374 EEVLTKASEDAKATT--RAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDtkeyraktvelqeeARRLRGEAEQ 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2942 ALKEKEAENERLRRQAEDEAYQRkiLEDQANQhkleIEEkiVLLKKSSDAEMERQKAIVDdtlkQRRVVEEEIrilklnf 3021
Cdd:NF041483 452 LRAEAVAEGERIRGEARREAVQQ--IEEAART----AEE--LLTKAKADADELRSTATAE----SERVRTEAI------- 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3022 EKASSgkldlelelnkLKNIAEETQQsklRAEEEAEKLRRLVLEE-EMRRKEAEDKVKKIAAAEEEAARQRKA-AQEELD 3099
Cdd:NF041483 513 ERATT-----------LRRQAEETLE---RTRAEAERLRAEAEEQaEEVRAAAERAARELREETERAIAARQAeAAEELT 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3100 RLQKKADEVRKQKEEADKEAEKQIV-----AAQQAALKCNMAEQQVQSVLAQQKEDSmmqNKLKEEyekakaLARDAEAA 3174
Cdd:NF041483 579 RLHTEAEERLTAAEEALADARAEAErirreAAEETERLRTEAAERIRTLQAQAEQEA---ERLRTE------AAADASAA 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3175 KERAEREAALLRQQA-EEAERQKvaaeqeaanqAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQqadEEMAKHKKLAE 3253
Cdd:NF041483 650 RAEGENVAVRLRSEAaAEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQ---EEAARRRREAE 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3254 QTL-KQKFQVEQELTKVKLQLEE----TDKQKSLLDDELQRLKDEVD-------DAMRQKA-SVEEELFKVKIQM-EELM 3319
Cdd:NF041483 717 ETLgSARAEADQERERAREQSEEllasARKRVEEAQAEAQRLVEEADrratelvSAAEQTAqQVRDSVAGLQEQAeEEIA 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3320 KLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQ-------------------EAARLRQIAEDDLN 3380
Cdd:NF041483 797 GLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQeeteaakalaertvseaiaEAERLRSDASEYAQ 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3381 QQRTLAEKMLKekmQAIQEASRLKAEA-EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAE-----RKRQL 3454
Cdd:NF041483 877 RVRTEASDTLA---SAEQDAARTRADArEDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEaraeaERVRA 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3455 EIIAEAEKLKLQVS----QLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEK-LNTSKEADDLRKA 3529
Cdd:NF041483 954 DAAAQAEQLIAEATgeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRtLDEARKDANKRRS 1033
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1655274895 3530 ---------ITELEKEKARLKKEAEEHQNKSKEMADAQ 3558
Cdd:NF041483 1034 eaaeqadtlITEAAAEADQLTAKAQEEALRTTTEAEAQ 1071
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
1250-1349 |
2.75e-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: 103.13 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1250 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED- 1328
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1655274895 1329 VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1114-1228 |
4.38e-25 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 102.95 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSgdtllsERDVARSVRlprEKGRMRFHKLQNVQIALDF 1193
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLS------QKRMYKKYN---KRPTFRQMKLENVSVALEF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21228 74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
1234-1349 |
5.90e-25 |
|
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: 103.27 E-value: 5.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1246-1352 |
6.95e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 102.36 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1246 MSAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVY--RQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1655274895 1323 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 1352
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2383-3297 |
6.95e-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: 115.45 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2383 LTSPLKKTKLDSASdNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQL 2462
Cdd:pfam02463 149 MMKPERRLEIEEEA-AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2463 AEAHAKAIAKAEKEAQELKLrmqeevSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEeih 2542
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLR------DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2543 liRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKAL 2622
Cdd:pfam02463 299 --KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2623 EDLENLRMQAEEAERQVKQAEVEKERQIQvahvaaQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQdaERLRK 2702
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEK------EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ--GKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2703 QQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLaqeeaekQKEEADREAKKRSKAEESALKQRdmAENELE 2782
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL-------SRQKLEERSQKESKARSGLKVLL--ALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2783 RQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAqqerKQLEDELSKVRSEMDILIQLKSRAE 2862
Cdd:pfam02463 520 VGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRAL----TELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2863 KETMSNTEKSKQLLEAEATKLRDLAEEASKlRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIA 2942
Cdd:pfam02463 596 VLEIDPILNLAQLDKATLEADEDDKRAKVV-EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2943 LKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLkkssdaEMERQKAIVDDTLKQRRVVEEEIRILKLNFE 3022
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL------EAEELLADRVQEAQDKINEELKLLKQKIDEE 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3023 KASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQ 3102
Cdd:pfam02463 749 EEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3103 KKADEVRKQKEEADKEAEKQIVAAQQAALKcNMAEQQVQsVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREA 3182
Cdd:pfam02463 829 KIKEEELEELALELKEEQKLEKLAEEELER-LEEEITKE-ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3183 ALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKK-----LAEQTLK 3257
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKvnlmaIEEFEEK 986
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1655274895 3258 QKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDA 3297
Cdd:pfam02463 987 EERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
1114-1231 |
1.28e-24 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 102.03 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvaRSVRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQK---------KMYRKYHPRPNFRQMKLENVSVALEF 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21310 86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1880-1946 |
1.55e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 99.64 E-value: 1.55e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 1880 QLKPRNptTPIKGNLPVQAVCDFKQVEITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPSVCFLVP 1946
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2873-3462 |
2.10e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2873 KQLLEAEATKLRDLaeeasKLRAIAEEAKHQRQLAEEDAARQraeaerilkeklaaisdatrlktEAEIALKEKEAENER 2952
Cdd:COG1196 222 LKELEAELLLLKLR-----ELEAELEELEAELEELEAELEEL-----------------------EAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2953 LRRQAEDEAYQRKILEDQANQHKLE--IEEKIVLLKKSSDAEMERQKAivddtlkqrrvvEEEIRILKLNFEKASSGKLD 3030
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELArlEQDIARLEERRRELEERLEEL------------EEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3031 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 3110
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3111 QKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAE 3190
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3191 EAErQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKfqveqELTKVK 3270
Cdd:COG1196 502 DYE-GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA-----KAGRAT 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3271 LQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAEN 3350
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3351 MKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQL 3430
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580 590
....*....|....*....|....*....|..
gi 1655274895 3431 MQQRLDEETEEYQRSLEAERKRQLEIIAEAEK 3462
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1247-1347 |
2.49e-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: 100.58 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1655274895 1327 EDV---DVphPDEKSIITYVSSLY 1347
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2762-3546 |
3.89e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.84 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2762 KRSKAEESALkQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLE 2841
Cdd:TIGR02168 216 KELKAELREL-ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2842 DELSKVrsEMDILIQLKSRAEKETmSNTEKSKQLLEAEAtKLRDLAEEASKLRAIAEEAKHQRQLAEED---AARQRAEA 2918
Cdd:TIGR02168 295 NEISRL--EQQKQILRERLANLER-QLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAEleeLEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2919 ERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKivlLKKSSDAEMERQKA 2998
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---ELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2999 IVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEE----------- 3067
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlse 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3068 ------------------------MRRKEA---------EDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKE- 3113
Cdd:TIGR02168 528 lisvdegyeaaieaalggrlqavvVENLNAakkaiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDl 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3114 -EADKEAEK---------------QIVAAQQAALKCNM-------------------AEQQVQSVLAQQKEDSmmqnKLK 3158
Cdd:TIGR02168 608 vKFDPKLRKalsyllggvlvvddlDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIE----ELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3159 EEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQK 3238
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3239 QQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEEL 3318
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3319 MKLKVRIEEENQRLmkkdkdntqkflveeAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQ 3398
Cdd:TIGR02168 844 EEQIEELSEDIESL---------------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3399 EASRLKAEAEMLQRQKDLAQEQAQKLledKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQakae 3478
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI---- 981
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 3479 eeakkfkkqadtiaARLHETEIATKEQMTEVKKmEFEKLNTSKEadDLRKAITELEKEKARLKKEAEE 3546
Cdd:TIGR02168 982 --------------KELGPVNLAAIEEYEELKE-RYDFLTAQKE--DLTEAKETLEEAIEEIDREARE 1032
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1252-1347 |
9.26e-24 |
|
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: 98.76 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1252 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED-VD 1330
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1655274895 1331 VPHPDEKSIITYVSSLY 1347
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1250-1350 |
9.61e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 98.69 E-value: 9.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1250 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPEDV 1329
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1655274895 1330 DVPHPDEKSIITYVSSLYDAM 1350
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
1234-1349 |
1.10e-23 |
|
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: 99.38 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1118-1227 |
1.40e-23 |
|
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: 98.16 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1118 KTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSvrlprekgRMRFHKLQNVQIALDFLRH 1196
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLV-DKKKVAAS--------LSRFKKIENINLALSFAEK 71
|
90 100 110
....*....|....*....|....*....|.
gi 1655274895 1197 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 1227
Cdd:smart00033 72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1096-1230 |
6.11e-23 |
|
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: 97.14 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1096 LGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKSQRHV--TDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLP 1173
Cdd:cd21247 1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGE------------QLP 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 1174 R-EKGRMRFHKLQNVQIALDFLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21247 69 RpSRGKMRVHFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2331-2929 |
7.09e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2331 LKEQLAKEKKLLEEIEKNKDKVDEcqkyakayidiikdYELQLVAYKAQVEPLTspLKKTKLDSASDNIIQEYVTLRTRY 2410
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEE--------------LEAELAELEAELEELR--LELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2411 SELmtltSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK 2490
Cdd:COG1196 298 ARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2491 RETAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETtvkqksnAEDELKQLRDRAD 2570
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAE-------LEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2571 AAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELkhksEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQI 2650
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAAL----AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2651 QVAHVAAQQSAAAELRskqmsfAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAenareeaerelekwRQKANEALR 2730
Cdd:COG1196 522 LAGAVAVLIGVEAAYE------AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG--------------RATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2731 LRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFD 2810
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2811 NAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEA 2890
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580 590
....*....|....*....|....*....|....*....
gi 1655274895 2891 SKLRAIAEEAKHQRQLAEEDAARQRAEAERiLKEKLAAI 2929
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELER-LEREIEAL 779
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1248-1351 |
9.17e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.01 E-value: 9.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1248 AKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21245 4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 1655274895 1328 DVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3005-3631 |
1.07e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3005 KQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEdkvkkiaaae 3084
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE---------- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3085 eeaarqRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEdsmmqnkLKEEYEKA 3164
Cdd:COG1196 290 ------EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-------AEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3165 KALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEE 3244
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3245 MAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAmrqkasveEELFKVKIQMEELMKLKVR 3324
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA--------AARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3325 IEeenqrlmKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKM--QAIQEASR 3402
Cdd:COG1196 509 GV-------KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3403 LKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAK 3482
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3483 KFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQI 3562
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3563 EREMTVLQQTFLTEKEMLLKKEKLiEDEKKKLESQFE----------EEIKKAKALKDEQDRQRQQMEEEKLKLKATMD 3631
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEEL-ERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2424-3470 |
1.34e-22 |
|
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: 107.95 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2424 ITDTQRRLEDEEKAAEKLKAE---------------------------EQKKMAEMQAELDKQKQLAEAHAKAIAKAEKE 2476
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2477 AQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKnlseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKS 2556
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2557 NAEDELKQLRDR-ADAAEKL--RKLAQEEAEKLRKQVSEE----------TQKKRLAEEELKHKSEAErkaANEKQKALE 2623
Cdd:pfam01576 261 NALKKIRELEAQiSELQEDLesERAARNKAEKQRRDLGEElealkteledTLDTTAAQQELRSKREQE---VTELKKALE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2624 DlENLRMQAEEAERQVKQAEVEKERQIQVAHvaAQQSAAAELRSKQMSFAENvskleESLKQEHGTVLQLQQDAERLRKQ 2703
Cdd:pfam01576 338 E-ETRSHEAQLQEMRQKHTQALEELTEQLEQ--AKRNKANLEKAKQALESEN-----AELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2704 QEDAENAREEaerelekwrqKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELER 2783
Cdd:pfam01576 410 LEGQLQELQA----------RLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2784 QRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKnevIAAQQERKQLEDELSKVRSEMDILIQLKSRAEK 2863
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ---AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2864 ETMSNTEKSKQLLEAEATKLRdLAEEaskLRAIAEEAKHQRQLAEEDAARQRaEAERILKEKLAAISDATRLKTEAEIAL 2943
Cdd:pfam01576 557 LTQQLEEKAAAYDKLEKTKNR-LQQE---LDDLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEA 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2944 KEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEkivlLKKSSDA------EMERQKAIVDDTLKQRRVVEEEiriL 3017
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMED----LVSSKDDvgknvhELERSKRALEQQVEEMKTQLEE---L 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3018 KLNFEKASSGKLDLELELNKLKNIAEETQQSKlraEEEAEKLRRLvLEEEMRRKEAEdkvkkiaaaeeeaarqrkaaqEE 3097
Cdd:pfam01576 705 EDELQATEDAKLRLEVNMQALKAQFERDLQAR---DEQGEEKRRQ-LVKQVRELEAE---------------------LE 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3098 LDRLQKKADEVRKQKEEAD-KEAEKQIVAAQQAAlkcNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEaaKE 3176
Cdd:pfam01576 760 DERKQRAQAVAAKKKLELDlKELEAQIDAANKGR---EEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE--KK 834
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3177 RAEREAALLRQQAEEAErqkvaaeqeaanqakaqddAERLRKDAEfeaaklaqaeaaalKQKQQADEEMAKHKKLAEQTL 3256
Cdd:pfam01576 835 LKNLEAELLQLQEDLAA-------------------SERARRQAQ--------------QERDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3257 KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKA---SVEEELFKVKIQMEELMK-LKVRIEEENQRL 3332
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAaerSTSQKSESARQQLERQNKeLKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3333 MKKDKDNTQKFlveEAenmkKLAEDAARLSIEAQEaarlRQIAEDDLNQqrtlAEKMLKEKMqaiqeasrLKAEAEmlQR 3412
Cdd:pfam01576 962 KSKFKSSIAAL---EA----KIAQLEEQLEQESRE----RQAANKLVRR----TEKKLKEVL--------LQVEDE--RR 1016
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3413 QKDLAQEQAQKL-LEDKQLMQQrLDEETEEYQRSLEAERK--RQLEIIAE-AEKLKLQVSQL 3470
Cdd:pfam01576 1017 HADQYKDQAEKGnSRMKQLKRQ-LEEAEEEASRANAARRKlqRELDDATEsNESMNREVSTL 1077
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2208-2941 |
2.02e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.92 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2208 DVKEVETYRTNLKKMRAEaEAEQPVFDSLEEELKKASAVSdkmsRVHSERDAELDQHRQHLSSLQD--RWKAVFTQIDLR 2285
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAE-AARKAEEVRKAEELRKAEDAR----KAEAARKAEEERKAEEARKAEDakKAEAVKKAEEAK 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2286 QRELD-QLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEqlAKEKKLLEEIEKN--KDKVDECQKYAKAy 2362
Cdd:PTZ00121 1237 KDAEEaKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK--AEEKKKADEAKKAeeKKKADEAKKKAEE- 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2363 idiikdyelqlvAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKfiTDTQRRLEDEEKAAEKLK 2442
Cdd:PTZ00121 1314 ------------AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKKKEEAKKK 1379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2443 AEEQKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELKlRMQEEVSKRETAAVDAEKQKQniqlelhelknlsEQQIKD 2522
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAE-------EDKKKADELK-KAAAAKKKADEAKKKAEEKKK-------------ADEAKK 1438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2523 KSQQVDEALKSRLRIEEeihliriqlettvkqKSNAEdELKQLRDRADAAEKLRKLAQEeaeklrKQVSEETQKKrlaEE 2602
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEE---------------AKKAE-EAKKKAEEAKKADEAKKKAEE------AKKADEAKKK---AE 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2603 ELKHKSEAERKAANEKQKAledlENLRmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELR-SKQMSFAENVSKLEE 2681
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKA----DEAK-KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKkAEELKKAEEKKKAEE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2682 SLKQEHGTVLQLQQdAERLRKQQEDAENAREEAERELEKwrQKANEAlrlrlQAEEEAHKKSlaqeeaekqkeeadREAK 2761
Cdd:PTZ00121 1569 AKKAEEDKNMALRK-AEEAKKAEEARIEEVMKLYEEEKK--MKAEEA-----KKAEEAKIKA--------------EELK 1626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2762 KRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDElyRLKNEVIAAQQERKQLE 2841
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAEALKKEAEEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2842 DELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKlrdlAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERI 2921
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
730 740
....*....|....*....|
gi 1655274895 2922 LKEKLAAISDATRLKTEAEI 2941
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKI 1800
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2327-3312 |
2.09e-22 |
|
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: 107.18 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2327 DSKTLKEQLAKEKKLLEEI--------EKNKDKVDECQKYAKAYIDIIKDYELQLVA-----YKAQVEPLTSPLKKTK-- 2391
Cdd:pfam01576 58 EAEEMRARLAARKQELEEIlhelesrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEeeaarQKLQLEKVTTEAKIKKle 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2392 -----LDSASDNIIQEYVTLRTRYSELMT--------------LTSQYIKFITDTQRRLEDEEKA---AEKLKAEEQKKM 2449
Cdd:pfam01576 138 edillLEDQNSKLSKERKLLEERISEFTSnlaeeeekakslskLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2450 AEMQAEL-DKQKQLAEAHAKaIAKAEKEAQELKLRMQEEVSKRETAavdaekQKQNIQLELHelknLSEQQ--IKDKSQQ 2526
Cdd:pfam01576 218 TDLQEQIaELQAQIAELRAQ-LAKKEEELQAALARLEEETAQKNNA------LKKIRELEAQ----ISELQedLESERAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2527 VDEALKSRLRIEEEIHLIRIQLETTVkQKSNAEDELKQLRDRAdaAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKH 2606
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEDTL-DTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQALEELTE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2607 KSEAER--KAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLK 2684
Cdd:pfam01576 364 QLEQAKrnKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2685 QEHGTVLQLQQDAERLRKQ-QEDAENAREEAERELEKWRQKANEALRLRlQAEEEahKKSLAQEEaekqkeeaDREAKKR 2763
Cdd:pfam01576 444 SVSSLLNEAEGKNIKLSKDvSSLESQLQDTQELLQEETRQKLNLSTRLR-QLEDE--RNSLQEQL--------EEEEEAK 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2764 SKAEesalKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLkneviaaQQERKQLEDE 2843
Cdd:pfam01576 513 RNVE----RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------EKTKNRLQQE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2844 LSKVRSEMDILIQLKSRAEKETmsntEKSKQLLEAEATKLRDLAEEASKLRAIAEEaKHQRQL----AEEDAARQRAEAE 2919
Cdd:pfam01576 582 LDDLLVDLDHQRQLVSNLEKKQ----KKFDQMLAEEKAISARYAEERDRAEAEARE-KETRALslarALEEALEAKEELE 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2920 RILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQ---ANQHKLEIEEKIVLLKKSSDAEM--- 2993
Cdd:pfam01576 657 RTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDElqaTEDAKLRLEVNMQALKAQFERDLqar 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2994 -----ERQKAIVddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEET---------QQSKLRAE------ 3053
Cdd:pfam01576 737 deqgeEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgreeavkQLKKLQAQmkdlqr 812
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3054 --EEAEKLRRLVL----EEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKK-ADEVRKQKEEADkeaEKQIVAA 3126
Cdd:pfam01576 813 elEEARASRDEILaqskESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEiASGASGKSALQD---EKRRLEA 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3127 QQAALKCNMAEQQ--VQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAE-----RQKVAA 3199
Cdd:pfam01576 890 RIAQLEEELEEEQsnTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEgtvksKFKSSI 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3200 EQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEmakhKKLAEQTLKQKFQVEQELTKVKLQLEETDKQ 3279
Cdd:pfam01576 970 AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE----RRHADQYKDQAEKGNSRMKQLKRQLEEAEEE 1045
|
1050 1060 1070
....*....|....*....|....*....|...
gi 1655274895 3280 KSLLDDELQRLKDEVDDAMRQKASVEEELFKVK 3312
Cdd:pfam01576 1046 ASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2225-3104 |
2.17e-22 |
|
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: 107.36 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2225 EAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYREsyd 2304
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE--- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2305 wlirwiadaKQRQENIQavpitDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEplt 2384
Cdd:pfam02463 237 ---------ERIDLLQE-----LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK--- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2385 spLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAE 2464
Cdd:pfam02463 300 --SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2465 AHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQNIQLELHELKNLSEQQikdksqqvDEALKSRLRIEEEIHLI 2544
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELEL-----------KSEEEKEAQLLLELARQLEDLL--------KEEKKEELEILEEEEES 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2545 RIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALED 2624
Cdd:pfam02463 439 IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2625 LENLRMQAEEAERQVKQAEVEKER------QIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAE 2698
Cdd:pfam02463 519 GVGGRIISAHGRLGDLGVAVENYKvaistaVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2699 RLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMA- 2777
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEi 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2778 ---------ENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRslLEDELYRLKNEVIAAQQERKQLEDELSKVR 2848
Cdd:pfam02463 679 qelqekaesELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2849 SE-MDILIQLKSRAEKETMSNTEKSKQLLEAEATKLR-DLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKL 2926
Cdd:pfam02463 757 LKkEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEeKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2927 AAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQ 3006
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3007 RRVVEEEIRILKLNFEKASSGKLDL---ELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAA 3083
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLleeADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900
....*....|....*....|.
gi 1655274895 3084 EEEAARQRKAAQEELDRLQKK 3104
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQ 1017
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1115-1229 |
7.14e-22 |
|
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: 93.51 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1115 VQKKTFTKWVNKHLIKSQRH--VTDLYEDLRDGHNLISLLEVLSGDtLLSERDVARSvrlprekgrmRFHKLQNVQIALD 1192
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKS----------EFDKLENINLALD 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 1193 FLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 1229
Cdd:pfam00307 71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2758-3631 |
7.42e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 7.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQRDMAENELERQRRLAEstAQQKLAaeQELIRLRADFDNAEQQRSL-----LEDELYRLKNEVIA 2832
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLE--RQAEKA--ERYKELKAELRELELALLVlrleeLREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2833 AQQERKQLEDELSKVRSEMDILIQLKSRAEKEtmsntekskqlLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAA 2912
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2913 RQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQanqhkleieekivllkkssDAE 2992
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL-------------------EEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2993 MERQKAIVDDTLKQRRVVEEEIRILKlnfekasSGKLDLELELNKLKNIAEETQQSKLRAE-----EEAEKLRRLVLEEE 3067
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLE-------ARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3068 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEkqivaaqqaALKCNMAEQQVQSVLAQQ 3147
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE---------GVKALLKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3148 KEDSMmqnKLKEEYEKA--KALARDAEAA----KERAEREAALLRQqaEEAERQKVAAEQEAANQAKAQDDAERLRKDAE 3221
Cdd:TIGR02168 525 LSELI---SVDEGYEAAieAALGGRLQAVvvenLNAAKKAIAFLKQ--NELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3222 FEAAKLAQAEAAALKQK------------QQADEEMAKHKKL-----------------------AEQTLKQKFQVEQEL 3266
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKalsyllggvlvvDDLDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3267 TKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmKKDKDNTQKFLVE 3346
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3347 EAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAemlqRQKDLAQEQAQKLLE 3426
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3427 DKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEiatkeqm 3506
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE------- 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3507 TEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQtfltekemllkKEKL 3586
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR-----------RLKR 976
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3587 IEDEKKK-----LESqfEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMD 3631
Cdd:TIGR02168 977 LENKIKElgpvnLAA--IEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1247-1347 |
2.24e-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: 92.02 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1655274895 1327 EDVDV--PHPDEKSIITYVSSLY 1347
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2881-3691 |
2.64e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 103.90 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2881 TKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDE 2960
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2961 AYQRKILEDQANQHKLEIEEKIVLLKKSSDaEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKN 3040
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3041 IAEETQQSKLRAEEEAEKLrrlvlEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAE 3120
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKE-----KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3121 KQIVAAQQAALKCNMAEQQVQSVLAQQKEDsmmqnklkeeyekakalARDAEAAKERAEREAALLRQQAEEAERQKVAAE 3200
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLED-----------------LLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3201 QEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQ-TLKQKFQVEQELTKVKLQLEETDKQ 3279
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARsGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3280 KSLLDDELQRLKDEV-DDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEdA 3358
Cdd:pfam02463 533 DLGVAVENYKVAISTaVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK-A 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3359 ARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEkMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEE 3438
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKE-SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3439 TEEyqrsleaERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKkfkkqadTIAARLHETEIATKEQMTEVKKMEFEKLN 3518
Cdd:pfam02463 691 KEE-------ILRRQLEIKKKEQREKEELKKLKLEAEELLADRV-------QEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3519 tskeaddlRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKL--IEDEKKKLES 3596
Cdd:pfam02463 757 --------LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELleEEQLLIEQEE 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3597 QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAA-LNKQKEAEKDILNKQKEmqELERKRLEQERVLADENQKLREK 3675
Cdd:pfam02463 829 KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKeELLQELLLKEEELEEQK--LKDELESKEEKEKEEKKELEEES 906
|
810
....*....|....*.
gi 1655274895 3676 LQQMEEAQKSTLITEK 3691
Cdd:pfam02463 907 QKLNLLEEKENEIEER 922
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2763-3667 |
3.09e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 103.75 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2763 RSKAEESALKQRDMAENELERQR-RLAESTAQQKLAAEQELIRLRAD----FDNAEQQRSLLEDELYRLKNEVIAAQQER 2837
Cdd:NF041483 173 RAEAEQALAAARAEAERLAEEARqRLGSEAESARAEAEAILRRARKDaerlLNAASTQAQEATDHAEQLRSSTAAESDQA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2838 KQLEDELSkvrsemdiliqlksRAEKETMSNTEKSKQLLEAEATKLRDLAEE-ASKLRAIAEEAKHQR-QLAEEDAARQR 2915
Cdd:NF041483 253 RRQAAELS--------------RAAEQRMQEAEEALREARAEAEKVVAEAKEaAAKQLASAESANEQRtRTAKEEIARLV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2916 AEAERilkeklaaisDATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKILEDQANQhkleieekivLLKKSSDAEMER 2995
Cdd:NF041483 319 GEATK----------EAEALKAEAEQALADARAEAEKLVAEAAEKA-RTVAAEDTAAQ----------LAKAARTAEEVL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2996 QKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA-EETQQSKLRAEEEAEKLRRLVLEEEMRRKEAE 3074
Cdd:NF041483 378 TKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkDDTKEYRAKTVELQEEARRLRGEAEQLRAEAV 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3075 DKVKKIAAAEEEAARQR-----KAAQEELDRLQKKADEVRKQkeeADKEAEKQIVAAQQAAlkcnmaeqqvqSVLAQQKE 3149
Cdd:NF041483 458 AEGERIRGEARREAVQQieeaaRTAEELLTKAKADADELRST---ATAESERVRTEAIERA-----------TTLRRQAE 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3150 DSMMQNKLKEEYEKAKALARdAEAAKERAEREAALLRQQAEEAERQKvaaeqeaanQAKAQDDAERLRKDAEfeaaklAQ 3229
Cdd:NF041483 524 ETLERTRAEAERLRAEAEEQ-AEEVRAAAERAARELREETERAIAAR---------QAEAAEELTRLHTEAE------ER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3230 AEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEEtdkqksllddELQRLKDE-VDDAMRQKAsvEEEL 3308
Cdd:NF041483 588 LTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQ----------EAERLRTEaAADASAARA--EGEN 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3309 FKVKIQME---ELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEA-ARLRQIAEDDLNQQRT 3384
Cdd:NF041483 656 VAVRLRSEaaaEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETlGSARAEADQERERARE 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3385 LAEKML----KEKMQAIQEASRLKAEAEmlQRQKDL---AQEQAQKLLEDKQLMQQRLDEETEEYQRSLE--AERKRQlE 3455
Cdd:NF041483 736 QSEELLasarKRVEEAQAEAQRLVEEAD--RRATELvsaAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEhaAERTRT-E 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3456 IIAEAEKLK----LQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTskEADDlrkAIT 3531
Cdd:NF041483 813 AQEEADRVRsdayAERERASEDANRLRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRT--EASD---TLA 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3532 ELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVlqqtfltekemllKKEKLIEDEKKKLESQFEEEIKKAkalkdE 3611
Cdd:NF041483 888 SAEQDAARTRADAREDANRIRSDAAAQADRLIGEATS-------------EAERLTAEARAEAERLRDEARAEA-----E 949
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 3612 QDRQRQQMEEEKLKLKATMDAALNKQKEAEkdilNKQKEMQELERKRLEQERVLAD 3667
Cdd:NF041483 950 RVRADAAAQAEQLIAEATGEAERLRAEAAE----TVGSAQQHAERIRTEAERVKAE 1001
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2440-3121 |
4.60e-21 |
|
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: 102.74 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2440 KLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNL--SE 2517
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAlqQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2518 QQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQksnaEDELKQLRDRADAAEKLRKLAQE-----EAEKLRKQVSE 2592
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ----EAVLEETQERINRARKAAPLAAHikavtQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2593 ETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQ----VAHVAAQQSAAAELRSK 2668
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtlTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2669 QMSFAENVSKLEESLKQ---EHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQ--KANEAL------RLRLQAEE 2737
Cdd:TIGR00618 395 LQSLCKELDILQREQATidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceKLEKIHlqesaqSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2738 EAHKKSLAQEEAEKQKEEADReaKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRS 2817
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLAR--LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2818 LLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIA 2897
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2898 EEAKHQRQLAEEDAARQRaEAERILKEK-----LAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQaN 2972
Cdd:TIGR00618 633 HLQQCSQELALKLTALHA-LQLTLTQERvrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL-E 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2973 QHKLEIE---EKIVLLKKSSDAEMERQKAIVDDTLKQ-RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQS 3048
Cdd:TIGR00618 711 THIEEYDrefNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3049 KLRAEEEAEKLRRLVLEEEMRRKEAED-------KVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEK 3121
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDEDilnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2590-3466 |
1.59e-20 |
|
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: 101.20 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2590 VSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAER---QVKQAEVEKERQIQVAHVAAQQSAAAELR 2666
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2667 SKQMSFAE-NVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALR-LRLQAEEEAHKKSL 2744
Cdd:pfam02463 244 ELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2745 AQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQEliRLRADFDNAEQQRSLLEDELY 2824
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--LESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2825 RLKNEVIAAQQERKQLEDELSKVR-SEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQ 2903
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKkEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2904 RQLAEEDAARQRAEAERilkeklaaisdatrlkteaEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIV 2983
Cdd:pfam02463 482 LQEQLELLLSRQKLEER-------------------SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2984 LLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLV 3063
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3064 LEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSV 3143
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3144 LAQQKEDSMMQNKLKEEYEKakaLARDAEAAKERAEREAALLRQQAEEAErqkvaaeqeaanqakaQDDAERLRKDAEFE 3223
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEEL---LADRVQEAQDKINEELKLLKQKIDEEE----------------EEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3224 AAKLAQAEAAALKQKQQADEEmaKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEvddamrqkas 3303
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK---------- 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3304 vEEELFKVKIQMEELMKLKVRIEEENQRLMK-------KDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAE 3376
Cdd:pfam02463 832 -EEELEELALELKEEQKLEKLAEEELERLEEeitkeelLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3377 DDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEET-------EEYQRSLEAE 3449
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGkvnlmaiEEFEEKEERY 990
|
890
....*....|....*...
gi 1655274895 3450 RKRQLEII-AEAEKLKLQ 3466
Cdd:pfam02463 991 NKDELEKErLEEEKKKLI 1008
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
1114-1234 |
2.25e-20 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 90.14 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvaRSVRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQK---------RMYRKYHQRPTFRQMQLENVSVALEF 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVSSSI 1234
Cdd:cd21309 87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPV 127
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
1248-1347 |
2.37e-20 |
|
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: 89.16 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1248 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1655274895 1328 D-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2998-3685 |
3.39e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 100.13 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2998 AIVDDTLKQRRVVEEE---IRILKLNFEKASSgKLDLELE-LNKLKNIAEET--QQSKLRAE-EEAEKLRRLVLEEE--- 3067
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEaagISKYKERRKETER-KLERTREnLDRLEDILNELerQLKSLERQaEKAERYKELKAELRele 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3068 -----MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQs 3142
Cdd:TIGR02168 227 lallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3143 vLAQQKEDSmmqnkLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEF 3222
Cdd:TIGR02168 306 -ILRERLAN-----LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3223 EAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQK-----SLLDDELQRLKDEVDDA 3297
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3298 MRQKASVEEELFKVKiqmEELMKLKVRIEEENQRL-----MKKDKDNTQKFLVEEAENMKKLAEDAARLS---------- 3362
Cdd:TIGR02168 460 EEALEELREELEEAE---QALDAAERELAQLQARLdslerLQENLEGFSEGVKALLKNQSGLSGILGVLSelisvdegye 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3363 --IEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQ--AIQEASRLKAeaemlqRQKDLAQEQAQKLLEDKQLMQQRLDEE 3438
Cdd:TIGR02168 537 aaIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGrvTFLPLDSIKG------TEIQGNDREILKNIEGFLGVAKDLVKF 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3439 TEEYQRSLEAERKRQL------EIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLH-ETEIATKEQmtEVKK 3511
Cdd:TIGR02168 611 DPKLRKALSYLLGGVLvvddldNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILErRREIEELEE--KIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3512 MEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEK 3591
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3592 KKLEsQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK 3671
Cdd:TIGR02168 768 ERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
730
....*....|....
gi 1655274895 3672 LREKLQQMEEAQKS 3685
Cdd:TIGR02168 847 IEELSEDIESLAAE 860
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2835-3681 |
6.56e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.99 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2835 QERKQLEDELSKVrSEMDILIQlKSRAEKETMSNTEKSKQLLEAEATKLRDlaeeasKLRAIAEEAKHQRQLAEEdaaRQ 2914
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKE-KALEELEEVEENIERLDLIIDEKRQQLE------RLRREREKAERYQALLKE---KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2915 RAEAERILKEKLAAisDATRLKTEAEIALKEKEAEN-ERLRRQAEDEAYQRKILEDQANqhkleieEKIvllKKSSDAEM 2993
Cdd:TIGR02169 222 EYEGYELLKEKEAL--ERQKEAIERQLASLEEELEKlTEEISELEKRLEEIEQLLEELN-------KKI---KDLGEEEQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2994 ERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEEtqqskLRAEEEAEKLRRLVLEEEMrrKEA 3073
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-----LEREIEEERKRRDKLTEEY--AEL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3074 EDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKE-DSM 3152
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINElEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3153 M---QNKLKEEYEKAKALARDAEAAKERAEREAALLRqQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQ 3229
Cdd:TIGR02169 443 KedkALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD-RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3230 AEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKV--------------------KLQLEETDKQKSLLDDELQR 3289
Cdd:TIGR02169 522 GVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKeaiellkrrkagratflplnKMRDERRDLSILSEDGVIGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3290 LKDEVdDAMRQKASVEEELFKVKIQMEELmklkvrieEENQRLMKKDKDNT-QKFLVEEAENM-------KKLAEDAARL 3361
Cdd:TIGR02169 602 AVDLV-EFDPKYEPAFKYVFGDTLVVEDI--------EAARRLMGKYRMVTlEGELFEKSGAMtggsrapRGGILFSRSE 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3362 SIEAQE-AARLR--QIAEDDLNQQRTLAEKMLKEKMQAIQEASR----LKAEAEMLQRQkdlaQEQAQKLLEDKQLMQQR 3434
Cdd:TIGR02169 673 PAELQRlRERLEglKRELSSLQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQE----EEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3435 LDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSeaqakaeeeakkfkkqadtiaARLHETEIATKEQmtEVKKMEF 3514
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---------------------ARLSHSRIPEIQA--ELSKLEE 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3515 EKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQIEREMTVLqQTFLTEKEMLLKK----EKLIEDE 3590
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENL-NGKKEELEEELEEleaaLRDLESR 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3591 KKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKaTMDAALNKQKEAEKDILNKQKEMQElERKRLEQERVLADENQ 3670
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS-ELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQ 961
|
890
....*....|.
gi 1655274895 3671 KLREKLQQMEE 3681
Cdd:TIGR02169 962 RVEEEIRALEP 972
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
1114-1231 |
9.23e-20 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 88.60 E-value: 9.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLLserdvarsvRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMH---------RKHNQRPTFRQMQLENVSVALEF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21308 90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
1247-1346 |
1.12e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 87.15 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1655274895 1327 ED-VDVPHPDEKSIITYVSSL 1346
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
1251-1348 |
1.27e-19 |
|
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: 87.40 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1251 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD-PEDV 1329
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1655274895 1330 DVPHPDEKSIITYVSSLYD 1348
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2601-3685 |
2.94e-19 |
|
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: 96.78 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2601 EEELKHKSEaerkaanEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE-----LRSKQMSFAEN 2675
Cdd:pfam01576 4 EEEMQAKEE-------ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEemrarLAARKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2676 VSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREeaerelekwrqkANEALRLRLQAEeeahKKSLaqeeaekqkee 2755
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLD------------EEEAARQKLQLE----KVTT----------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2756 adrEAKKRsKAEESALKQRDmAENELERQRRLAE---STAQQKLAAEQELIRLRADFDNaeQQRSLLEDELYRLKNEVIA 2832
Cdd:pfam01576 130 ---EAKIK-KLEEDILLLED-QNSKLSKERKLLEeriSEFTSNLAEEEEKAKSLSKLKN--KHEAMISDLEERLKKEEKG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2833 AQQERK---QLEDELSKVRSEMdilIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKH----QRQ 2905
Cdd:pfam01576 203 RQELEKakrKLEGESTDLQEQI---AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQiselQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2906 LAEEDAARQRAEAE-RILKEKLAAisdatrLKTEAEIALKEKEAENErLRRQAEDEAYQ-RKILEDQANQHKLEIEEkiv 2983
Cdd:pfam01576 280 LESERAARNKAEKQrRDLGEELEA------LKTELEDTLDTTAAQQE-LRSKREQEVTElKKALEEETRSHEAQLQE--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2984 LLKKSSDAEMERQKAIvddtlkqrrvveEEIRILKLNFEKAssgKLDLELELNKLKNIAEETQQSKLraeeeaeklrrlv 3063
Cdd:pfam01576 350 MRQKHTQALEELTEQL------------EQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQ------------- 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3064 lEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSV 3143
Cdd:pfam01576 402 -DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3144 LAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQkvaAEQEAANQAKAQDDAERLRKDAEfe 3223
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDAGTLEALEEGKKRLQRELE-- 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3224 aaklaqaeaaalKQKQQADEEMAKHKKLAeqtlKQKFQVEQELTKVKLQLeetDKQKSLLD--DELQRLKDEV---DDAM 3298
Cdd:pfam01576 556 ------------ALTQQLEEKAAAYDKLE----KTKNRLQQELDDLLVDL---DHQRQLVSnlEKKQKKFDQMlaeEKAI 616
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3299 RQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARlsiEAQEAARLRQIAEDD 3378
Cdd:pfam01576 617 SARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGK---NVHELERSKRALEQQ 693
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3379 LNQQRTLAEKmLKEKMQAIQEAsRLKAEAEM----LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEeyqrsLEAERKRQL 3454
Cdd:pfam01576 694 VEEMKTQLEE-LEDELQATEDA-KLRLEVNMqalkAQFERDLQARDEQGEEKRRQLVKQVRELEAE-----LEDERKQRA 766
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3455 EIIAEAEKLKLQVSQLSeaqakaeeeakkfkkqadtiaARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITEL- 3533
Cdd:pfam01576 767 QAVAAKKKLELDLKELE---------------------AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIl 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3534 ----EKEKARLKKEAEEHQ-NKSKEMADAQQKQIEREMTVLQQTF---LTEKEMLLKKEKLIEDEKKKLESQFEEEIKKA 3605
Cdd:pfam01576 826 aqskESEKKLKNLEAELLQlQEDLAASERARRQAQQERDELADEIasgASGKSALQDEKRRLEARIAQLEEELEEEQSNT 905
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3606 KALKDEQDRQRQQMEEeklklkatmdaaLNKQKEAEKDILNKQKEM-QELERKrleqervladeNQKLREKLQQMEEAQK 3684
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQ------------LTTELAAERSTSQKSESArQQLERQ-----------NKELKAKLQEMEGTVK 962
|
.
gi 1655274895 3685 S 3685
Cdd:pfam01576 963 S 963
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2406-3343 |
3.01e-19 |
|
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: 97.04 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2406 LRTRYSELMTLTS-----QYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 2480
Cdd:TIGR00606 171 LKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2481 KLRmQEEVSKRETAAVDAEKqkqniqlELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSnaed 2560
Cdd:TIGR00606 251 KNR-LKEIEHNLSKIMKLDN-------EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2561 elkqlRDRADAAEKLRK-------LAQEEAEKLRKQVSEETQKKRLAEEELKHKSEaerKAANEKQKALEDLEnlrmQAE 2633
Cdd:TIGR00606 319 -----RELVDCQRELEKlnkerrlLNQEKTELLVEQGRLQLQADRHQEHIRARDSL---IQSLATRLELDGFE----RGP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2634 EAERQVKQA-EVEKERQIQVAHVAAQQsaAAELRSKQMSFAENVSKLEESLKQEHGTvlqLQQDAERLRKQQEDAENARE 2712
Cdd:TIGR00606 387 FSERQIKNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKKGLGRT---IELKKEILEKKQEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2713 EAERELE------KWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDmaenelERQRR 2786
Cdd:TIGR00606 462 ELQQLEGssdrilELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH------TTTRT 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2787 LAESTAQQKLAAEQ-----------ELIRLRADFDNAEQqrslLEDELYRLKNEViaaqqerKQLEDELSKVRSEMDILI 2855
Cdd:TIGR00606 536 QMEMLTKDKMDKDEqirkiksrhsdELTSLLGYFPNKKQ----LEDWLHSKSKEI-------NQTRDRLAKLNKELASLE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2856 QLKSRAEKETMSNTEKSKQLLEA--EATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDAT 2933
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2934 R-LKTEAEIALKEKEAENERLRRQAEDEAYQRKIledqanqHKLEIEEKIVLLKKSSDA-EMERQKAIVDDTLKQRRVVE 3011
Cdd:TIGR00606 685 RvFQTEAELQEFISDLQSKLRLAPDKLKSTESEL-------KKKEKRRDEMLGLAPGRQsIIDLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3012 EEIRILKLNFEKASS--GKLDLELELNK--------LKNIAEETQQSKLRAEEEAEKLR-----RLVLEEEMRRKEAEDK 3076
Cdd:TIGR00606 758 RDIQRLKNDIEEQETllGTIMPEEESAKvcltdvtiMERFQMELKDVERKIAQQAAKLQgsdldRTVQQVNQEKQEKQHE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3077 VKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNK 3156
Cdd:TIGR00606 838 LDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3157 LKEEYEKAKALARDAEAAKERAEREAALLRqqaeeaERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALK 3236
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNKKAQDKVNDIK------EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEK 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3237 QKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKiqME 3316
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIK--RN 1069
|
970 980
....*....|....*....|....*..
gi 1655274895 3317 ELMKLKVRIEEENQRLMKKDKDNTQKF 3343
Cdd:TIGR00606 1070 HVLALGRQKGYEKEIKHFKKELREPQF 1096
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1247-1345 |
3.92e-19 |
|
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: 85.75 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVY-RQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1655274895 1326 PEDVDVPHPDEKSIITYVSS 1345
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2313-3123 |
4.93e-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: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2313 AKQRQENIQAVPITDSKTLKEQLAKEKklLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAqvepltspLKKTKL 2392
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEE--LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA--------LLKEKR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2393 DSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEK---AAEKLKAEEQKKMAEMQAE--LDKQKQLAEAHA 2467
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleEIEQLLEELNKKIKDLGEEeqLRVKEKIGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2468 KaIAKAEKEAQELKLRMQeevskretaavDAEKQKQNIQLELHELK----NLSEQ--QIKDKSQQVDEALKSRlriEEEI 2541
Cdd:TIGR02169 302 E-IASLERSIAEKERELE-----------DAEERLAKLEAEIDKLLaeieELEREieEERKRRDKLTEEYAEL---KEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2542 HLIRIQLETTVKQKSNAEDELKQLRDRADAA-------EKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKhKSEAERKA 2614
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLkreinelKRELDRLQEELQRLSEELADLNAAIAGIEAKIN-ELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2615 ANEKQKALE-DLENLRMQAEEAERQV-----KQAEVEKER---QIQVAHVAAQQSAAaelRSKQMSFAENVSKLEESLKQ 2685
Cdd:TIGR02169 446 KALEIKKQEwKLEQLAADLSKYEQELydlkeEYDRVEKELsklQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2686 EHGTVLQLQQDAERL----------RKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEE 2755
Cdd:TIGR02169 523 VHGTVAQLGSVGERYataievaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFA 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2756 AD--REAKKRSKAEESALKQRDMAENeLERQRRL--------------------------AESTAQQKLAAEQELIRLRA 2807
Cdd:TIGR02169 603 VDlvEFDPKYEPAFKYVFGDTLVVED-IEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2808 DFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE---KETMSNTEKSKQLLEAEATKLR 2884
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELK 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2885 DLAEEASKLraiaEEAKHQRQLAEEDAARQRAEAE--------RILKEKLAAISDATRlktEAEIALKEKEAENERLRRQ 2956
Cdd:TIGR02169 762 ELEARIEEL----EEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2957 AEDEAYQRKILEDQANQHKLEIEEkIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 3036
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3037 KLKNIAEETQQSKLRAEEEAE----------------------KLRRLVLEEEMRRKE-----AEDKVKKIAAAEEEAAR 3089
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSeiedpkgedeeipeeelsledvQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDELKE 993
|
890 900 910
....*....|....*....|....*....|....
gi 1655274895 3090 QRKAAQEELDRLQKKADEVRKQKEEADKEAEKQI 3123
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1250-1346 |
7.19e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 84.67 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1250 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN----LENLEQAFNVAEKDLGVTRLLD 1325
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1655274895 1326 PEDVDVPHPDEKSIITYVSSL 1346
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2800-3674 |
1.75e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 94.36 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2800 QELIRLRADFDNAEQQRSLL----EDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETmsntEKSKQL 2875
Cdd:TIGR02169 198 QQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL----EEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2876 LEAEATKLRDLAEEasklraiaEEAKHQRQLAEEDAarQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRR 2955
Cdd:TIGR02169 274 LEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2956 QAEDEAYQRKILEDQANQHKLEIEEKIVLLkkssdAEMERQKAIVDDTLKQRRvveEEIrilklnfEKASSGKLDLELEL 3035
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAEL-----EEVDKEFAETRDELKDYR---EKL-------EKLKREINELKREL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3036 NKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK----- 3110
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKelskl 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3111 QKEEADKEAEKQIVAAQQAALKCN--MAEQQVQSVLAQQKEdsmmQNKLKEEYEKAKALARDAEAAKERAEREAalLRQQ 3188
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVeeVLKASIQGVHGTVAQ----LGSVGERYATAIEVAAGNRLNNVVVEDDA--VAKE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3189 AEEAERQKVAAEQEAANQAKAQD---DAERLRKDA---------EFEAAKLAQAEAAALKQKQQADEEMAKHkklaeqtL 3256
Cdd:TIGR02169 563 AIELLKRRKAGRATFLPLNKMRDerrDLSILSEDGvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARR-------L 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3257 KQKFQVeqeltkVKLQLEETDKQKSLLDDELqRLKDEVDDAMRQKASVE---EELFKVKIQMEELMKLKVRIEEENQRLM 3333
Cdd:TIGR02169 636 MGKYRM------VTLEGELFEKSGAMTGGSR-APRGGILFSRSEPAELQrlrERLEGLKRELSSLQSELRRIENRLDELS 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3334 KKDKDNTQKflVEEAENmkklaedaaRLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKmqaiQEASRLkaEAEMLQRQ 3413
Cdd:TIGR02169 709 QELSDASRK--IGEIEK---------EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK----SELKEL--EARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3414 KDLAQEQAQ-KLLEDKqLMQQRLDEETEEYqRSLEAERKRQLEIIAEAE----KLKLQVSQLSEAQAKAEEEAKKFKKQA 3488
Cdd:TIGR02169 772 EDLHKLEEAlNDLEAR-LSHSRIPEIQAEL-SKLEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3489 DTIAARLHETEIATKEQMTEVKKMEfeklntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmadaQQKQIEREMTV 3568
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELE-------AALRDLESRLGDLKKERDELEAQLRELERKIEE----LEAQIEKKRKR 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3569 LQQTfLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKdeqdrQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQ 3648
Cdd:TIGR02169 919 LSEL-KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA-----ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
890 900
....*....|....*....|....*.
gi 1655274895 3649 KEMQELERKRLEQERVLADENQKLRE 3674
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2435-3181 |
1.82e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 94.36 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2435 EKAAEKLKAEEQKkMAEMQAELDKQKQLAEAHAKAIAKAEKeAQELKLRMQE-EVSKRETAAVDAEKQKQNIQLELHELk 2513
Cdd:TIGR02169 173 EKALEELEEVEEN-IERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREyEGYELLKEKEALERQKEAIERQLASL- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2514 nlsEQQIKDKSQQVDEalksrlrIEEEIHLIRIQLEttvkqksnaedelkqlrdraDAAEKLRKLAQEEAEKLRKQVSEE 2593
Cdd:TIGR02169 250 ---EEELEKLTEEISE-------LEKRLEEIEQLLE--------------------ELNKKIKDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2594 TQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQ------------AEVEKERQIQVAHVAAQQSA 2661
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklteeyAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2662 AAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWrQKANEALRLRLQAEEEaHK 2741
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL-EEEKEDKALEIKKQEW-KL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2742 KSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAEneLERQRRLAESTAQQKLAAEQELirlRADFDNAEQQRSLL-- 2819
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--AEAQARASEERVRGGRAVEEVL---KASIQGVHGTVAQLgs 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2820 EDELY----------RLKNEVIA----AQQERKQLEDE---------LSKVRSE------------MDILIQLKSRAEK- 2863
Cdd:TIGR02169 533 VGERYataievaagnRLNNVVVEddavAKEAIELLKRRkagratflpLNKMRDErrdlsilsedgvIGFAVDLVEFDPKy 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2864 ---------ET--MSNTEKSKQLL------------------------EAEATKLRDLAEEASKLRAIAEEAKHQRQLae 2908
Cdd:TIGR02169 613 epafkyvfgDTlvVEDIEAARRLMgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKREL-- 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2909 EDAARQRAEAERILKEKLAAISDATR----LKTEAEIALKEKEAENERLRRQAED-EAYQRKILEDQANQHKLEIEEkiv 2983
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDlSSLEQEIENVKSELKELEARI--- 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2984 llkkssdAEMERQKAIVDDTLK--QRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRR 3061
Cdd:TIGR02169 768 -------EELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3062 LVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQ-------EELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAalKCN 3134
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKK--RKR 918
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1655274895 3135 MAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL-ARDAEAAKERAERE 3181
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPEEELsLEDVQAELQRVEEE 966
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2419-3197 |
2.60e-18 |
|
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: 94.03 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2419 QYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQElklrmqeevskretaavDA 2498
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAD-IRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2499 EKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIE---EEIHLIRIQLETTVKQKSNAEDELKQL--RDRADAAE 2573
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2574 KLRKLAQEEAEKLRKQVSEetqkkrlAEEELKH-KSEAERKaanekqkaLEDLenLRMQAEEAERQVKQAEVEkerqiqv 2652
Cdd:pfam15921 224 KILRELDTEISYLKGRIFP-------VEDQLEAlKSESQNK--------IELL--LQQHQDRIEQLISEHEVE------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2653 ahVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenareeaerelekwrqkaneaLRLR 2732
Cdd:pfam15921 280 --ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQ-------------------------LRSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2733 LqaeeeahkkslaqeeaekqkeeadREAKK--RSKAEESAlKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFD 2810
Cdd:pfam15921 333 L------------------------REAKRmyEDKIEELE-KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2811 NAEQQRSLLEDELYRL----KNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE---KETMSNTEKSKQLLEAEATKL 2883
Cdd:pfam15921 388 KREKELSLEKEQNKRLwdrdTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmERQMAAIQGKNESLEKVSSLT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2884 RDLAEEASKLRAIAEEAKhQRQLAEEDAARQRAEAERILKEKLAAI----SDATRLKTEAEIALKEKE---AENERLRR- 2955
Cdd:pfam15921 468 AQLESTKEMLRKVVEELT-AKKMTLESSERTVSDLTASLQEKERAIeatnAEITKLRSRVDLKLQELQhlkNEGDHLRNv 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2956 QAEDEAYQRKILED----QANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILK----LNFEKASSG 3027
Cdd:pfam15921 547 QTECEALKLQMAEKdkviEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKdkkdAKIRELEAR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3028 KLDLELELNKLKNIAEEtqqsKLRAEEEAEKLRRLVLEE---------------EMRRKEAEDKVKKIAAAEEEAARQRK 3092
Cdd:pfam15921 627 VSDLELEKVKLVNAGSE----RLRAVKDIKQERDQLLNEvktsrnelnslsedyEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3093 AAQEELDRLQKKAdevrKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNK----LKEEYEKAKALA 3168
Cdd:pfam15921 703 SAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKekhfLKEEKNKLSQEL 778
|
810 820
....*....|....*....|....*....
gi 1655274895 3169 RDAEAAKERAEREAALLRQQaEEAERQKV 3197
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQ-ERRLKEKV 806
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
1247-1346 |
2.62e-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: 83.36 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1655274895 1327 ED-VDVPHPDEKSIITYVSSL 1346
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1247-1347 |
1.37e-17 |
|
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: 81.58 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|..
gi 1655274895 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEFY 102
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
1243-1348 |
1.52e-17 |
|
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: 81.53 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1243 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1655274895 1323 LLDPEDV-DVPHPDEKSIITYVSSLYD 1348
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2617-3374 |
1.88e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 90.80 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2617 EKQKALEDLENL---RMQAEEAERQVKQAEVEKE---RQIQVAHVAAQQSAAAELRSKQMSFAEnVSKLEESLKQEHGTV 2690
Cdd:TIGR00618 164 EKKELLMNLFPLdqyTQLALMEFAKKKSLHGKAElltLRSQLLTLCTPCMPDTYHERKQVLEKE-LKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2691 LQLQQDAERL-----RKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEA-HKKSLAQEEAEKQKEEADREAKKRS 2764
Cdd:TIGR00618 243 AYLTQKREAQeeqlkKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAaHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2765 KAEESALKQRDMA-ENELERQRRLaestaQQKLAAEQELIRlradfDNAEQQRSLLE--DELYRLKNEVIAAQQERKQLE 2841
Cdd:TIGR00618 323 RAKLLMKRAAHVKqQSSIEEQRRL-----LQTLHSQEIHIR-----DAHEVATSIREisCQQHTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2842 DELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAkhQRQLAEEDAARQRAEAERI 2921
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--QCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2922 LKEKLAAISDATRLKTE---AEIALKEKEAENERL--RRQAEDEAYQRKILEDQANQHKLE-IEEKIVLLKKssdaEMER 2995
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLET----SEED 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2996 QKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQsKLRAEEEAEKLRRLVLEEEMRRKeaed 3075
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD-LTEKLSEAEDMLACEQHALLRKL---- 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3076 kvkkiaaaeeeaarqrkaaQEELDRLQKKADEVRKQKEEADKEAEKqivaaqqAALKCNMAEQQVQSVLA---QQKEDSM 3152
Cdd:TIGR00618 622 -------------------QPEQDLQDVRLHLQQCSQELALKLTAL-------HALQLTLTQERVREHALsirVLPKELL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3153 MQNKLKEEYEKAKAlaRDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEA 3232
Cdd:TIGR00618 676 ASRQLALQKMQSEK--EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3233 AALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDEL-QRLKDEVDDAMRQKASVEEELFKV 3311
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQF 833
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 3312 KIQMEELMKLKVRIEeenqRLMKKDKDNTQKFlveeaenmKKLAEDAARLSIEAQEAARLRQI 3374
Cdd:TIGR00618 834 LSRLEEKSATLGEIT----HQLLKYEECSKQL--------AQLTQEQAKIIQLSDKLNGINQI 884
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
1247-1348 |
2.72e-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: 80.39 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
|
90 100
....*....|....*....|....
gi 1655274895 1327 EDVDV--PHPDEKSIITYVSSLYD 1348
Cdd:cd21261 81 EDMMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
1247-1352 |
6.34e-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: 79.71 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
|
90 100
....*....|....*....|....*...
gi 1655274895 1327 EDVDV--PHPDEKSIITYVSSLYDAMPR 1352
Cdd:cd21258 81 EDMMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2896-3631 |
1.00e-16 |
|
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: 88.64 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2896 IAEEAKHQRQlaeeDAARQRAEAERIL-KEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQAnqH 2974
Cdd:pfam15921 79 VLEEYSHQVK----DLQRRLNESNELHeKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV--H 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2975 KLEIEEKIVL-LKKSSDAEMERQKAIvddtLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAE 3053
Cdd:pfam15921 153 ELEAAKCLKEdMLEDSNTQIEQLRKM----MLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3054 EEAE----KLRRLVLEEEMR--RKEAEDKVKKIAAAEEEAARQRKAAQE-ELDRLQKKADEVRKQKEEADKEAE--KQIV 3124
Cdd:pfam15921 229 LDTEisylKGRIFPVEDQLEalKSESQNKIELLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEiiQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3125 AAQQAALKCNMA--EQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARD--AEAAKER----------------------- 3177
Cdd:pfam15921 309 RNQNSMYMRQLSdlESTVSQLRSELREAKRMYEDKIEELEKQLVLANSelTEARTERdqfsqesgnlddqlqklladlhk 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3178 AEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDA-------ERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKK 3250
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrlEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3251 LAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAmrqKASVEEELFKVKIQMEELMKLK-------- 3322
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT---NAEITKLRSRVDLKLQELQHLKnegdhlrn 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3323 VRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQ-EAARLrqiaEDDLNQQR-TLAE-KMLKEKMQA--- 3396
Cdd:pfam15921 546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQL----EKEINDRRlELQEfKILKDKKDAkir 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3397 ----------IQEASRLKAEAEMLQRQKDLAQEQAQkLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ 3466
Cdd:pfam15921 622 elearvsdleLEKVKLVNAGSERLRAVKDIKQERDQ-LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3467 vsqlseaqakaeeeakkfkkqadtiaarLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAIT------ELEKEKARL 3540
Cdd:pfam15921 701 ----------------------------LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITakrgqiDALQSKIQF 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3541 KKEAEEHQNKSKEMADAQQKQIEREMTvlqqTFLTEKEMLLKKEKLIEDEKKKLE---SQFEEEIKKAKALKDE-QDR-Q 3615
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELS----TVATEKNKMAGELEVLRSQERRLKekvANMEVALDKASLQFAEcQDIiQ 828
|
810
....*....|....*.
gi 1655274895 3616 RQQMEEEKLKLKATMD 3631
Cdd:pfam15921 829 RQEQESVRLKLQHTLD 844
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
1116-1228 |
1.48e-16 |
|
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: 78.39 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1116 QKKTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTllserdVARSVRLPRekgrMRFHKLQNVQIALDF 1193
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEK------VPGIHSRPK----TRAQKLENIQACLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21212 71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2208-2852 |
1.83e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2208 DVKEVETYRTNLKKMRAEAEAeqpvfdsLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDrwkavftQIDLRQR 2287
Cdd:COG1196 223 KELEAELLLLKLRELEAELEE-------LEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2288 ELDQLGRQlgyyresydwLIRWIADAKQRQENIQAvpitdsktLKEQLAKEKKLLEEIEKNKDKVDEcqkyakayidiik 2367
Cdd:COG1196 289 EEYELLAE----------LARLEQDIARLEERRRE--------LEERLEELEEELAELEEELEELEE------------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2368 dyelQLVAYKAQVEpltsplkktkldsasdniiqeyvtlrtryselmtltsqyikfitdtqrRLEDEEKAAEKLKAEEQK 2447
Cdd:COG1196 338 ----ELEELEEELE------------------------------------------------EAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2448 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQV 2527
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEAL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2528 DEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHK 2607
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2608 SEAErkaANEKQKALEDLENLRMQAEEAERQVKQAEVEKER-QIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQE 2686
Cdd:COG1196 525 AVAV---LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAiEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2687 HGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLR----------LQAEEEAHKKSLAQEEAEKQKEEA 2756
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRevtlegeggsAGGSLTGGSRRELLAALLEAEAEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2757 DREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQE 2836
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
650
....*....|....*.
gi 1655274895 2837 RKQLEDELSKVRSEMD 2852
Cdd:COG1196 762 LEELERELERLEREIE 777
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
1249-1350 |
3.62e-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: 77.82 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1249 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 1328
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1655274895 1329 -VDVPHPDEKSIITYVSSLYDAM 1350
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3046-3691 |
4.23e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.56 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3046 QQSKLRAEEEAEKLRRLVLEEE-----MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQ-----KKADEVRKQKEEA 3115
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEaagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeqaKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3116 DKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERA---------EREAALLR 3186
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeeelkllAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3187 QQAEEAERQKVAAEQEA----ANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKL--AEQTLKQKF 3260
Cdd:pfam02463 300 SELLKLERRKVDDEEKLkeseKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLeqLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3261 QVEQE--------LTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVK-IQMEELMKLKVRIEEENQR 3331
Cdd:pfam02463 380 KLESErlssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIeLKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3332 LMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQ 3411
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3412 RQK----DLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQ 3487
Cdd:pfam02463 540 NYKvaisTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3488 ADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDL---RKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIER 3564
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLaekSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3565 EMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE-SQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKD 3643
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEAqDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3644 ILNKQKEMQE--LERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEK 3691
Cdd:pfam02463 780 REKTEKLKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1117-1226 |
4.38e-16 |
|
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: 76.99 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1117 KKTFTKWVNKHL-IKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarSVRLPREKGRMRFHKLQNVQIALDFLR 1195
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPG----------SIPKINKKPKSPFKKRENINLFLNACK 70
|
90 100 110
....*....|....*....|....*....|...
gi 1655274895 1196 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 1226
Cdd:cd00014 71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
1251-1348 |
1.34e-15 |
|
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: 75.69 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1251 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD-PEDV 1329
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1655274895 1330 DVPHPDEKSIITYVSSLYD 1348
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2201-2969 |
1.43e-15 |
|
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: 84.72 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2201 EVHTVPNDVKEVETYRTNLKKMRAEAEAEqpvFDSLEEELKKASAVSDKMSrvhserdAELDQHRQHLSSLQDRWKAVFT 2280
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEE---LAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2281 QIDLRQRELDQLGRQlgyyresydwlirwIADAKQRQENIqavpitdsKTLKEQLAKEK-KLLEEIEKNKDKVDECQKya 2359
Cdd:TIGR02168 380 QLETLRSKVAQLELQ--------------IASLNNEIERL--------EARLERLEDRReRLQQEIEELLKKLEEAEL-- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2360 kayidiiKDYELQLVAYKAQVEPLTSPL--KKTKLDSASDNIIQEYVTLRTRYSELMTLTSQyIKFITDTQRRLEDEEKA 2437
Cdd:TIGR02168 436 -------KELQAELEELEEELEELQEELerLEEALEELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSEG 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2438 AEKLKAeEQKKMAEMQAELDKQKQLAEAHAKAIAKAekeaqeLKLRMQEEVSKRETAAVDA-EKQKQNiqlELHELKNLS 2516
Cdd:TIGR02168 508 VKALLK-NQSGLSGILGVLSELISVDEGYEAAIEAA------LGGRLQAVVVENLNAAKKAiAFLKQN---ELGRVTFLP 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2517 EQQIKDKSQQVDEAlkSRLRIEEEIHLIRIQLETTVKQKSNA-EDELKQLR---DRADAAEKLRKLAQEEA------EKL 2586
Cdd:TIGR02168 578 LDSIKGTEIQGNDR--EILKNIEGFLGVAKDLVKFDPKLRKAlSYLLGGVLvvdDLDNALELAKKLRPGYRivtldgDLV 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2587 RKQ-----VSEETQKKRLAE----EELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIqvahvAA 2657
Cdd:TIGR02168 656 RPGgvitgGSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-----SA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2658 QQSAAAELRSKqmsfaenVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRlRLQAEE 2737
Cdd:TIGR02168 731 LRKDLARLEAE-------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALR 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2738 EAHKKSlaqeeaekqkeeadREAKKRSKAEESALKQR-DMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQR 2816
Cdd:TIGR02168 803 EALDEL--------------RAELTLLNEEAANLRERlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2817 SLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRA- 2895
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEe 948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2896 ---IAEEAKHQRQLAEEDAARQRAEAERiLKEKLAAISDATRLkteaeiALKEKEAENER---LRRQAEDEAYQRKILED 2969
Cdd:TIGR02168 949 yslTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5107-5145 |
2.66e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.36 E-value: 2.66e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 5107 LLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEMNEIL 5145
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2483-3676 |
5.00e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 82.92 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2483 RMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQqVDEALKSRLRIEEEIHLIRIQLETtvkQKSNAEDEL 2562
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNA-LQEQLQAETELCAEAEEMRARLAA---RKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2563 KQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKkrLAEEE-LKHKSEAERKAANEKQKALEdlENLRMQAEEAERQVKQ 2641
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQ--LDEEEaARQKLQLEKVTTEAKIKKLE--EDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2642 AEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENV-SKLEESLKQEHgtvlQLQQDAERLRKQQEDAENAREEAERELek 2720
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEE----KGRQELEKAKRKLEGESTDLQEQIAEL-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2721 wrQKANEALRLRLQAEEEAHKKSLaqeeaekqkeeadreakkrSKAEESALKQRDMAENELERQRRLAEstAQQKLAAEq 2800
Cdd:pfam01576 228 --QAQIAELRAQLAKKEEELQAAL-------------------ARLEEETAQKNNALKKIRELEAQISE--LQEDLESE- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2801 elirlRADFDNAEQQRSLLEDELYRLKNEV------IAAQQE-RKQLEDELSkvrsemdiliQLKSRAEKETMSNTEKSK 2873
Cdd:pfam01576 284 -----RAARNKAEKQRRDLGEELEALKTELedtldtTAAQQElRSKREQEVT----------ELKKALEEETRSHEAQLQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2874 QLLEAEATKLRDLAEEAsklraiaEEAKHQRQLAEEdaARQRAEAERilKEKLAAISDATRLKTEAEIALKEKEAENERL 2953
Cdd:pfam01576 349 EMRQKHTQALEELTEQL-------EQAKRNKANLEK--AKQALESEN--AELQAELRTLQQAKQDSEHKRKKLEGQLQEL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2954 RRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQK--AIVDDTLKQ-RRVVEEEIRiLKLNFekaSSGKLD 3030
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdvSSLESQLQDtQELLQEETR-QKLNL---STRLRQ 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3031 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 3110
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3111 QKEEADKEAEKQIVAA-QQAALKCNMAEQQVQ--SVLAQQKedsMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQ 3187
Cdd:pfam01576 574 TKNRLQQELDDLLVDLdHQRQLVSNLEKKQKKfdQMLAEEK---AISARYAEERDRAEAEAREKETRALSLARALEEALE 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3188 QAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaalkqkqqadeemakhkklaeqtlKQKFQVEQELT 3267
Cdd:pfam01576 651 AKEELERTNKQLRAEMEDLVSSKDDVGKNVHELE-----------------------------------RSKRALEQQVE 695
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3268 KVKLQLEEtdkqkslLDDELQRLKDevddamrQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEE 3347
Cdd:pfam01576 696 EMKTQLEE-------LEDELQATED-------AKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDE 761
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3348 AENMKKLAEDAARLSIEAQEAARlrQIaeDDLNQQRTLAEKMLKekmqaiqeasrlKAEAEMLQRQKDLAQEQAQKlleD 3427
Cdd:pfam01576 762 RKQRAQAVAAKKKLELDLKELEA--QI--DAANKGREEAVKQLK------------KLQAQMKDLQRELEEARASR---D 822
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3428 KQLMQQRldeETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLhETEIAtkeQMT 3507
Cdd:pfam01576 823 EILAQSK---ESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRL-EARIA---QLE 895
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3508 EvkKMEFEKLNTSKEADDLRKAI-------TELEKEKARLKK-----EAEEHQNKS-----KEMADAQQKQIEREMTVLQ 3570
Cdd:pfam01576 896 E--ELEEEQSNTELLNDRLRKSTlqveqltTELAAERSTSQKsesarQQLERQNKElkaklQEMEGTVKSKFKSSIAALE 973
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3571 QTFLTEKEMLLKKE-------KLIEDEKKKLES---QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKatmdaalNKQKEA 3640
Cdd:pfam01576 974 AKIAQLEEQLEQESrerqaanKLVRRTEKKLKEvllQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-------EAEEEA 1046
|
1210 1220 1230
....*....|....*....|....*....|....*.
gi 1655274895 3641 EKDILNKQKEMQELErKRLEQERVLADENQKLREKL 3676
Cdd:pfam01576 1047 SRANAARRKLQRELD-DATESNESMNREVSTLKSKL 1081
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
1247-1347 |
5.82e-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: 73.93 E-value: 5.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEkDLGVTRLLDP 1326
Cdd:cd21199 8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTI 86
|
90 100
....*....|....*....|..
gi 1655274895 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21199 87 DEmVSMERPDWQSVMSYVTAIY 108
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2778-3662 |
6.01e-15 |
|
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: 82.79 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2778 ENELERQRRLAESTaqqklaaEQELIRLRADFDNAEQQRSlledELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQL 2857
Cdd:TIGR00606 230 EAQLESSREIVKSY-------ENELDPLKNRLKEIEHNLS----KIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2858 KSRAEKETMSNTEKSKQLLEAEatkLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKT 2937
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERE---LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2938 EAEIALKEKEAENER--------LRRQAEDEAyqrkileDQANQHKLEIEEKIVLLKKSSDaEMERQKAIVDDTLKQRRV 3009
Cdd:TIGR00606 376 RLELDGFERGPFSERqiknfhtlVIERQEDEA-------KTAAQLCADLQSKERLKQEQAD-EIRDEKKGLGRTIELKKE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3010 VeeeirilklnfekassgkldLELELNKLKNIAEETQQSklraeeEAEKLRRLVLEEEMRRKEAE-DKVKKIAAAEEEAA 3088
Cdd:TIGR00606 448 I--------------------LEKKQEELKFVIKELQQL------EGSSDRILELDQELRKAERElSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3089 RQRKAAQEELDRLQKKADEVRKQKE-EADKEAEKQIvaaQQAALKCNMAEQQVQSVLAQQKEDSMMQ------------- 3154
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQM---EMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqledw 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3155 -NKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQD---DAERLRKDAEFEAAKLAQA 3230
Cdd:TIGR00606 579 lHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIEKSSKQRAML 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3231 EAAALKQKQQADEEMAKHKKLAEqTLKQKFQVEQELTKVKLQLEET-----DKQKSLlDDELQRLKDEVDDAMRQKASVE 3305
Cdd:TIGR00606 659 AGATAVYSQFITQLTDENQSCCP-VCQRVFQTEAELQEFISDLQSKlrlapDKLKST-ESELKKKEKRRDEMLGLAPGRQ 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3306 EELFKVKIQMEELMKLKVRIEEENQRLmkKDKDNTQKFLVEEAENMKKLAEDA-------ARLSIEAQEAAR--LRQIAE 3376
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRL--KNDIEEQETLLGTIMPEEESAKVCltdvtimERFQMELKDVERkiAQQAAK 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3377 DDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLledkqlmQQRLDE-ETEEYQRSLEAERKRQLE 3455
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL-------KSKTNElKSEKLQIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3456 iiaeaEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEK 3535
Cdd:TIGR00606 888 -----EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3536 E----KARLKKEAEEHQNK---SKEMADAQQKQIEREMTVLQQTFLTEK--EMLLKKE---KLIEDEKKKLE---SQFEE 3600
Cdd:TIGR00606 963 KiqdgKDDYLKQKETELNTvnaQLEECEKHQEKINEDMRLMRQDIDTQKiqERWLQDNltlRKRENELKEVEeelKQHLK 1042
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3601 EIKKAKALkdEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQE 3662
Cdd:TIGR00606 1043 EMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3010-3612 |
8.57e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3010 VEEEIRILKLNFEKASSGKLDLElelNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEdKVKKIAAAEEEAAR 3089
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3090 QRKAAQEELDRLQKKADEVRKQKEEADKEAEKqivaaqqaaLKCNMAEqqvqsvLAQQKEDSMMQNKLKEEYEKAKALAR 3169
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEE---------LEEKVKE------LKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3170 DAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHK 3249
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3250 KLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEE-----LFKVKIQMEELMKLKVR 3324
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3325 IEEENQRLmKKDKDNTQKFLVEEAE--NMKKLAEDaarlsIEAQEAaRLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASR 3402
Cdd:PRK03918 471 IEEKERKL-RKELRELEKVLKKESEliKLKELAEQ-----LKELEE-KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3403 LKAEAEMLQ---RQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLseaqAKAEE 3479
Cdd:PRK03918 544 LKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKEL----EREEK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3480 EAKKFKKQADTIAARLHETEIATKEQMTEVKkmEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmadaqq 3559
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE------ 691
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3560 kqIEREMTVLQQtfltEKEMLLKKEKLIEDEKKKLE--SQFEEEIKKAKALKDEQ 3612
Cdd:PRK03918 692 --IKKTLEKLKE----ELEEREKAKKELEKLEKALErvEELREKVKKYKALLKER 740
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2098-2990 |
1.11e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 81.94 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2098 VEKEPLKECIQKTAEQAKVQVELEGLKKDLDKVSTKTQDILNSPQpsatapvLRSELELTVQKMdhaymlssVYLEKLKT 2177
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ-------LKEKLELEEEYL--------LYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2178 VEMVIRNTQGAEGVLKQYENCLREVhtvpnDVKEVETYRTNLKKMRAEAEAEQ---PVFDSLEEELKKASAVSDKMSRVH 2254
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQE-----IEKEEEKLAQVLKENKEEEKEKKlqeEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2255 SERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQ 2334
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2335 LAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYE----------------LQLVAYKAQVEPLTSPLKKTKLDSASDN 2398
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKkeeleileeeeesielKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2399 IIQEYVTLRTRYSELM-TLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEA 2477
Cdd:pfam02463 470 SEDLLKETQLVKLQEQlELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2478 QELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSN 2557
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2558 AEDELKQLRDRADAAE----KLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAE 2633
Cdd:pfam02463 630 KDTELTKLKESAKAKEsglrKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2634 EAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREE 2713
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2714 AERELEKWRQKANEALRLRLQAEEEAHKKSLaqeEAEKQKEEADREAKKRSKAEESALKQRDMAENElERQRRLAESTAQ 2793
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEE---QLLIEQEEKIKEEELEELALELKEEQKLEKLAE-EELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2794 QKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMdiliqlKSRAEKETMSNTEKSK 2873
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI------KEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2874 QLLEAEATKlRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLkTEAEIALKEKEAENERL 2953
Cdd:pfam02463 940 LLLEEADEK-EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL-EEEKKKLIRAIIEETCQ 1017
|
890 900 910
....*....|....*....|....*....|....*..
gi 1655274895 2954 RRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSD 2990
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPD 1054
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3048-3690 |
1.95e-14 |
|
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: 80.92 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3048 SKLRAEEEAEKLRRLVLEEEMRRKEAedkvkKIAAAEEEAARQRKAAQEeldrLQKKADEVRKQKEEADKEAEKQIVAAQ 3127
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKEN-----KLQENRKIIEAQRKAIQE----LQFENEKVSLKLEEEIQENKDLIKENN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3128 QAALKCNMAEQ-----------------QVQSV-----------------LAQQKEDSM--MQNKLKEEYEKAKALARDA 3171
Cdd:pfam05483 152 ATRHLCNLLKEtcarsaektkkyeyereETRQVymdlnnniekmilafeeLRVQAENARleMHFKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3172 EAAKERAEREAALLRQQAEEAERQkvaAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALK-QKQQADEEMAKHKK 3250
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENK---MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHlTKELEDIKMSLQRS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3251 LAEQ-TLKQKFQVEQ----ELTKVK-LQLEETDKQKS------------------LLDDELQRLKDEVDdamrQKASVEE 3306
Cdd:pfam05483 309 MSTQkALEEDLQIATkticQLTEEKeAQMEELNKAKAahsfvvtefeattcsleeLLRTEQQRLEKNED----QLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3307 ELFKVKIQMEELMKLK----VRIEEENQRLMKKDKdntqkfLVEEAENMKKLAEDaarLSIEAQEAARLRQIAEDDLNQQ 3382
Cdd:pfam05483 385 ELQKKSSELEEMTKFKnnkeVELEELKKILAEDEK------LLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3383 RTLAEKMLKEKMQAIQEASRLKAEAEMLQ-RQKDLAQEQAQKLLEDKQLMQQRLDE--ETEEYQRSLEAERKRQLEIIAE 3459
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQEASDMtlELKKHQEDIINCKKQEERMLKQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3460 AEKLKLQVSQLseaQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKA-------ITE 3532
Cdd:pfam05483 536 IENLEEKEMNL---RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQienknknIEE 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3533 LEKEKARLKKEAEEhQNKSKEMADAQQKQIEREMTVLQQTFlteKEMLLKKEKLIEDeKKKLESQFEEEIKKAKALKDEq 3612
Cdd:pfam05483 613 LHQENKALKKKGSA-ENKQLNAYEIKVNKLELELASAKQKF---EEIIDNYQKEIED-KKISEEKLLEEVEKAKAIADE- 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3613 drqrqqmeeeklklkatmdaALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK---LREKLQQMEEAQKSTLIT 3689
Cdd:pfam05483 687 --------------------AVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSAKAALEI 746
|
.
gi 1655274895 3690 E 3690
Cdd:pfam05483 747 E 747
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2811-3467 |
2.55e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2811 NAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE--KETMSNTEKSKQLLEAeatKLRDLAE 2888
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEelEKELESLEGSKRKLEE---KIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2889 EASKLRAIAEEAKHQRQLAEEdaARQRAEAERILKEklaaisdatrLKTEAEIALKEKEAENERLRRQAEdeayqrkile 2968
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKE--LKEKAEEYIKLSE----------FYEEYLDELREIEKRLSRLEEEIN---------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2969 dqanqhklEIEEKIvllkkssdAEMERQKAIVDDTLKQRRVVEEEIRILKlNFEKASSGKLDLELELNKLKniaeetqqs 3048
Cdd:PRK03918 325 --------GIEERI--------KELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLK--------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3049 KLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 3128
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3129 AALKcnMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAK 3208
Cdd:PRK03918 459 AELK--RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3209 AQDDAERLRKDAEfEAAKLAQAEAAALKQKQQADEEMAK-HKKLAEQTLKQKFQVEQELTKVK------LQLEETDKQKS 3281
Cdd:PRK03918 537 LKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3282 LLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRlmkkdkdntqkflveeaENMKKLAEDAARL 3361
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR-----------------EEYLELSRELAGL 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3362 SIEAQEAARLRQIAEDDLnqqrtlaeKMLKEKMQAIQEAsrlKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 3441
Cdd:PRK03918 679 RAELEELEKRREEIKKTL--------EKLKEELEEREKA---KKELEKLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
650 660 670
....*....|....*....|....*....|
gi 1655274895 3442 YQRSLEAE---RKRQ-LEIIAEAEKLKLQV 3467
Cdd:PRK03918 748 IASEIFEElteGKYSgVRVKAEENKVKLFV 777
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3146-3462 |
3.23e-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: 80.17 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3146 QQKEDSMMQNKLKEEYE-KAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDA----ERLRKDA 3220
Cdd:pfam17380 290 QEKFEKMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERkrelERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3221 EFEAAKLAQAEAAALKQKQQADEEMakhKKLAEQTLKQKFQVEQELTKVKLQLEETDK----QKSLLDDELQRLKDEVDd 3296
Cdd:pfam17380 370 IAMEISRMRELERLQMERQQKNERV---RQELEAARKVKILEEERQRKIQQQKVEMEQiraeQEEARQREVRRLEEERA- 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3297 amRQKASVEEELFKVKIQMEELmklkvRIEEENQRLMKKDKDNTQKflveeaenMKKLAEDAARLSIEAQEAARLRQIAE 3376
Cdd:pfam17380 446 --REMERVRLEEQERQQQVERL-----RQQEEERKRKKLELEKEKR--------DRKRAEEQRRKILEKELEERKQAMIE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3377 DDlnQQRTLAEKMLKEKMQAI-QEASRLKAEAEmlqrqkdlaqEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQ-L 3454
Cdd:pfam17380 511 EE--RKRKLLEKEMEERQKAIyEEERRREAEEE----------RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREmM 578
|
....*...
gi 1655274895 3455 EIIAEAEK 3462
Cdd:pfam17380 579 RQIVESEK 586
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4461-4499 |
5.43e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.89 E-value: 5.43e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 4461 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPELHEKL 4499
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
1116-1228 |
6.60e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 70.79 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1116 QKKTFTKWVNKHLIK--SQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVArsvrlPREKGRMRfhklQNVQIALDF 1193
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKL-PGIDWN-----PTTDAERK----ENVEKVLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274895 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21213 71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
1247-1347 |
7.73e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 71.26 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1655274895 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2660-3467 |
9.00e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.96 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2660 SAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenareeaerelekwRQKANE--ALRLRLQ-AE 2736
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE------------------REKAERyqALLKEKReYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2737 EEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENElERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQR 2816
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2817 SLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAI 2896
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2897 AEEAKHQRQLAEE----------------DAARQRAEAERILKEKLAAI-SDATRLKTEAEIALKEKEAENERLRRQAED 2959
Cdd:TIGR02169 384 RDELKDYREKLEKlkreinelkreldrlqEELQRLSEELADLNAAIAGIeAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2960 -EAYQRKILEDQANQHKLEIEEKivlLKKSSDAEMERQKAIVDDTLKQRRVVEEEIR---------ILKLN--------- 3020
Cdd:TIGR02169 464 lSKYEQELYDLKEEYDRVEKELS---KLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtVAQLGsvgeryata 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3021 FEKASSGKLDLE-------------------------LELNKLKniAEETQQSKLRAE---------------------- 3053
Cdd:TIGR02169 541 IEVAAGNRLNNVvveddavakeaiellkrrkagratfLPLNKMR--DERRDLSILSEDgvigfavdlvefdpkyepafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3054 --------EEAEKLRRLVLEEEM--------------------------RRKEAEDKVKKIAAAEEEAARQRKAAQEELD 3099
Cdd:TIGR02169 619 vfgdtlvvEDIEAARRLMGKYRMvtlegelfeksgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3100 RLQKKADEVRkqkeEADKEAEKQIVAAQQAAlkcNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAE 3179
Cdd:TIGR02169 699 RIENRLDELS----QELSDASRKIGEIEKEI---EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3180 REAALLRQQAEEAErqkvaaeqeaanqakAQDDAERLrkdaefeaaklaqaeaaalkqkQQADEEMAKHKKLAEQTLKQK 3259
Cdd:TIGR02169 772 EDLHKLEEALNDLE---------------ARLSHSRI----------------------PEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3260 FQVEQELTKVKLQLEetdkqksLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM----KLKVRIEEENQRL--M 3333
Cdd:TIGR02169 815 REIEQKLNRLTLEKE-------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeeleELEAALRDLESRLgdL 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3334 KKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQqrtlaekmLKEKMQAIQEASRLKAEAEMLQRQ 3413
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDEEIPEEELSLEDVQAE 959
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3414 KDLAQEQAQKL-------LEDKQLMQQRLDeETEEYQRSLEAERKRQLEIIAEAEKLKLQV 3467
Cdd:TIGR02169 960 LQRVEEEIRALepvnmlaIQEYEEVLKRLD-ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1705-1891 |
1.29e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 73.25 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1705 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 1784
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1785 AALQTQWSWILQLCCCVEAHLKENTAYYQFFTDVKDAQDKMKKMQENMKkkySCDRTTTATRLEDLLQDAVDEKEQLNEF 1864
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180
....*....|....*....|....*..
gi 1655274895 1865 KTQVAGLNKRAKSIIQLKPRNPTTPIK 1891
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIE 185
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4793-4831 |
1.67e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.67e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 4793 LLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEIHDKL 4831
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1109-1227 |
1.99e-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: 69.62 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1109 EDERDrvqKKTFTKWVNKHLIKSQRHvtDLYEDLRDGhnlISLLEVLsgDTLLSERDVARSVRLPREKGRMRfhKLQNVQ 1188
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVL--DKIQPGCVNWKKVNKPKPLNKFK--KVENCN 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274895 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1227
Cdd:cd21219 69 YAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3803-3840 |
2.35e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.97 E-value: 2.35e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1655274895 3803 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPELHNK 3840
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2429-2924 |
2.35e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.12 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2429 RRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQNIQLE 2508
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-----------LEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2509 LHELKNLseQQIKDKSQQVdEALKSRLRIEEEihliriQLETTVKQksnaEDELKQLRDRADAAEKLRKLAQEEAEKLRK 2588
Cdd:COG4717 118 LEKLEKL--LQLLPLYQEL-EALEAELAELPE------RLEELEER----LEELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2589 QVSEETqkkrlaEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQ------SAA 2662
Cdd:COG4717 185 QLSLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2663 AELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERlRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKK 2742
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR-EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2743 SLAQEEAEKqkeeadREAKKRSKAEESALKQRDMAENELERQRRLAESTAQ------QKLAAEQELIRLRADFDNAEQQ- 2815
Cdd:COG4717 338 ELLELLDRI------EELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelrAALEQAEEYQELKEELEELEEQl 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2816 ---------------RSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILiqlksrAEKETMSNTEKSKQLLEAEa 2880
Cdd:COG4717 412 eellgeleellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEELKAE- 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1655274895 2881 tkLRDLAEEASKLRAIAEE-AKHQRQLAEEDAARQRAEAERILKE 2924
Cdd:COG4717 485 --LRELAEEWAALKLALELlEEAREEYREERLPPVLERASEYFSR 527
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1247-1347 |
2.60e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 69.29 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1655274895 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1134-1225 |
3.00e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 69.16 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1134 HVTDLYEDLRDGHNLISLLEVLSGDTLLSERDVARSVRLPRekgrmrfhKLQNVQIALDFLRHRQV----KLVNIRNDDI 1209
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQ--------KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
|
90
....*....|....*.
gi 1655274895 1210 ADGNPKLTLGLIWTII 1225
Cdd:cd21223 97 VDGHREKTLALLWRII 112
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1113-1224 |
3.45e-13 |
|
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: 69.10 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1113 DRVQKKTFTKWVNKHLIKSQ-RHVTDLYEDLRDGHNLISLLEVLSGDTLLSERDVARSVRLPRekgrmrfhkLQNVQIAL 1191
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNLHLAM 72
|
90 100 110
....*....|....*....|....*....|....
gi 1655274895 1192 DFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21225 73 LFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2729-3430 |
4.65e-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: 76.70 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2729 LRLRLQAEEEAHKK-------SLAQEEAEKQKEEADREA-----KKRSKAEESALKQRDMAENELERQRRLAE------S 2790
Cdd:pfam15921 90 LQRRLNESNELHEKqkfylrqSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNTVHELEAAKCLKEdmledsN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2791 TAQQKL--------AAEQELIRLRADFDNAEQQRSLLEDELYRL--KNEVIAAQQERKQLEDELSKVRSEM----DILIQ 2856
Cdd:pfam15921 170 TQIEQLrkmmlsheGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDTEISYLKGRIfpveDQLEA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2857 LKSRAEKET----MSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISda 2932
Cdd:pfam15921 250 LKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVS-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2933 tRLKTEAEIALKEKEAENERLRRQ---AEDEAYQRKILEDQANQHKLEIEEKIVLL-----KKSSDAEMERQK------- 2997
Cdd:pfam15921 328 -QLRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEKEQnkrlwdr 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2998 ----AIVDDTLKQ----RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEE--- 3066
Cdd:pfam15921 407 dtgnSITIDHLRRelddRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEElta 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3067 -EMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKAD----EVRKQKEEADkeaEKQIVAAQQAALKCNMAEQ-QV 3140
Cdd:pfam15921 487 kKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqELQHLKNEGD---HLRNVQTECEALKLQMAEKdKV 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3141 QSVLAQQKEDsMMQNKLKEEYEKAKALARDAEAAKERAEREAAL----LRQQAEEAERQKVAAEQEAANQAKAQ---DDA 3213
Cdd:pfam15921 564 IEILRQQIEN-MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELqefkILKDKKDAKIRELEARVSDLELEKVKlvnAGS 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3214 ERLRKDAEFeaaklaqaeaaalkqKQQADEEMAKHK-------KLAE--QTLKQKF-----QVEQELTKVKLQLEETDKQ 3279
Cdd:pfam15921 643 ERLRAVKDI---------------KQERDQLLNEVKtsrnelnSLSEdyEVLKRNFrnkseEMETTTNKLKMQLKSAQSE 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3280 KSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKlKVRIEEENQRLMKKDKdntqKFLVEEAenmKKLAEDaa 3359
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLEEAMTNANKEK----HFLKEEK---NKLSQE-- 777
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 3360 rLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMqAIQEASRLKAEAE-MLQRQ-KDLAQEQAQKLLEDKQL 3430
Cdd:pfam15921 778 -LSTVATEKNKMAGELEVLRSQERRLKEKVANMEV-ALDKASLQFAECQdIIQRQeQESVRLKLQHTLDVKEL 848
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1247-1344 |
5.58e-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: 68.18 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1655274895 1326 PEDVDVPHPDEKSIITYVS 1344
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2476-3123 |
6.76e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2476 EAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNL--SEQQIKDksqQVDEALKSRLRIEEEIHLIRIQLETTVK 2553
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikRTENIEE---LIKEKEKELEEVLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2554 QKSNAEDELKQLrdradaaEKLRklaqEEAEKLRKQVSEETQKKRLAEEELKHKseaeRKAANEKQKALEDLEnlrmqae 2633
Cdd:PRK03918 222 ELEKLEKEVKEL-------EELK----EEIEELEKELESLEGSKRKLEEKIREL----EERIEELKKEIEELE------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2634 EAERQVKQAEVEKERQIQVAhvaaqqsaaaELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREE 2713
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLS----------EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2714 AERELEKWRQKANEALRLR-LQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEEsalkqrdmAENELERQRRLAESTA 2792
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE--------EISKITARIGELKKEI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2793 QQKLAAEQELIRLRADFD------NAEQQRSLLED---ELYRLKNEVIAAQQERKQLEDELSKVRSEM----------DI 2853
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPvcgrelTEEHRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEKVLkkeseliklkEL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2854 LIQLKSRAEKETMSNTEKskqlLEAEATKLRDLAEEASKLRA----IAEEAKHQRQLAEEDAARQRAEAEriLKEKLAAI 2929
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE----LEKKAEEYEKLKEKLIKLKGeiksLKKELEKLEELKKKLAELEKKLDE--LEEELAEL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2930 sdatrLKTEAEIALKEKEAENERLRrqaEDEAYQRKILEDQANQHKLEIEEKivlLKKSSDAEMERQKAIVDDTLKQRRV 3009
Cdd:PRK03918 576 -----LKELEELGFESVEELEERLK---ELEPFYNEYLELKDAEKELEREEK---ELKKLEEELDKAFEELAETEKRLEE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3010 VEEEIRILKLNF-----EKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRrlvlEEEMRRKEAEDKVKKIaaae 3084
Cdd:PRK03918 645 LRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK----EELEEREKAKKELEKL---- 716
|
650 660 670
....*....|....*....|....*....|....*....
gi 1655274895 3085 eeaarqrKAAQEELDRLQKKadeVRKQKEEADKEAEKQI 3123
Cdd:PRK03918 717 -------EKALERVEELREK---VKKYKALLKERALSKV 745
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1609-1798 |
1.31e-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: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1609 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQL---SPISRGKYREYLGRLD 1685
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1686 LQYAKLLNSSKSRLRNLD---SLHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDI 1762
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655274895 1763 QAMGDRLVKDGHPGK-KTVEAFTAALQTQWSWILQLC 1798
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2768-3222 |
1.44e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2768 ESALKQRDMAENELERQRRLAESTAQqklAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKV 2847
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2848 RSEMDILIQL--------KSRAEKEtMSNTEKSKQLLEAEATKLRDLAEEAsKLRAIAEEAKHQRQLAEedAARQRAEAE 2919
Cdd:COG4913 322 REELDELEAQirgnggdrLEQLERE-IERLERELEERERRRARLEALLAAL-GLPLPASAEEFAALRAE--AAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2920 RILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKILEDQANQHK---------LEIEEK----- 2981
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEaelpfvgelIEVRPEeerwr 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2982 --------------IVllkkssDAEMERQ-KAIVDDTLKQRRVVEEEIRILKLNFEKAS------SGKLD---------L 3031
Cdd:COG4913 478 gaiervlggfaltlLV------PPEHYAAaLRWVNRLHLRGRLVYERVRTGLPDPERPRldpdslAGKLDfkphpfrawL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3032 ELELNKLKNIA--EETQQskLRAEEEA--------------EK------LRRLVLEEEMRRK--EAEDKVKKIAAAEEEA 3087
Cdd:COG4913 552 EAELGRRFDYVcvDSPEE--LRRHPRAitragqvkgngtrhEKddrrriRSRYVLGFDNRAKlaALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3088 ARQRKAAQEELDRLQKKADEVRKQKEEADKEAEkqiVAAQQAALkcnmaeQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL 3167
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWDEID---VASAEREI------AELEAELERLDASSDDLAALEEQLEELEAE 700
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3168 ARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEF 3222
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
1108-1224 |
1.82e-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: 67.26 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1108 IEDERDrvqKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVLSGDTLLSERdvarsVRLPREKGRMRFHKLQNV 1187
Cdd:cd21298 2 IEETRE---EKTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIKPGVVDWSR-----VNKPFKKLGANMKKIENC 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274895 1188 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21298 72 NYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQL 108
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2835-3673 |
1.83e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.86 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2835 QERKQLE-DELSKVRSEMDILiqlksraeketmsNTEKSKQLLEAEatklrDLAEEASKLRAIAEEAKhqRQLAEE---D 2910
Cdd:NF041483 7 QESHRADdDHLSRFEAEMDRL-------------KTEREKAVQHAE-----DLGYQVEVLRAKLHEAR--RSLASRpayD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2911 AARQRAEAERILKEklaAISDATRLKTEAEIALKEKEAENERL---------RRQAE--DEAYQRKILEDQ--------- 2970
Cdd:NF041483 67 GADIGYQAEQLLRN---AQIQADQLRADAERELRDARAQTQRIlqehaehqaRLQAElhTEAVQRRQQLDQelaerrqtv 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2971 ----------ANQHKLEIEEKIVLLKKSSDAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASS--------GKLDLE 3032
Cdd:NF041483 144 eshvnenvawAEQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARAeaeailrrARKDAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3033 LELNKLKNIAE---------------ETQQSKLRAEE----------EAE-KLRRLVLEEEMRRKEAEDKVKKIAAAEEE 3086
Cdd:NF041483 222 RLLNAASTQAQeatdhaeqlrsstaaESDQARRQAAElsraaeqrmqEAEeALREARAEAEKVVAEAKEAAAKQLASAES 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3087 AARQR-KAAQEELDRL----QKKADEVRKQKE----EADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKL 3157
Cdd:NF041483 302 ANEQRtRTAKEEIARLvgeaTKEAEALKAEAEqalaDARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3158 KEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQ-----KVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaea 3232
Cdd:NF041483 382 EDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlkgaaKDDTKEYRAKTVELQEEARRLRGEAE----------- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3233 aalkqkQQADEEMAKHKKLAEQTLKQKFQveqeltkvklQLEETDKQKSLLddeLQRLKDEVDDaMRQKASVEEElfKVK 3312
Cdd:NF041483 451 ------QLRAEAVAEGERIRGEARREAVQ----------QIEEAARTAEEL---LTKAKADADE-LRSTATAESE--RVR 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3313 IQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAAR-LSIEAQEAARLRQI-AEDDLNQQRTLAEKML 3390
Cdd:NF041483 509 TEAIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAAReLREETERAIAARQAeAAEELTRLHTEAEERL 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3391 KEKMQAI----QEASRLKAEA-EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAE------RKRQlEIIAE 3459
Cdd:NF041483 589 TAAEEALadarAEAERIRREAaEETERLRTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEgenvavRLRS-EAAAE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3460 AEKLKlqvsqlSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEqmtevkkmefEKLNTSKEADD-LRKAITELEKEKA 3538
Cdd:NF041483 668 AERLK------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQE----------EAARRRREAEEtLGSARAEADQERE 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3539 RLKKEAEEHQNKSKEMADAQQKQIERemtVLQQTFLTEKEMLLKKE---KLIEDEKKKLESQFEEEIKKAK-ALKDEQDR 3614
Cdd:NF041483 732 RAREQSEELLASARKRVEEAQAEAQR---LVEEADRRATELVSAAEqtaQQVRDSVAGLQEQAEEEIAGLRsAAEHAAER 808
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3615 QRQQMEEEKLKLKAtmDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLAD---ENQKLR 3673
Cdd:NF041483 809 TRTEAQEEADRVRS--DAYAERERASEDANRLRREAQEETEAAKALAERTVSEaiaEAERLR 868
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1249-1348 |
2.43e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 66.21 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1249 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMgKVYRQTN----LENLEQAFNVAEK-DLGVTRL 1323
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK-INKKPKSpfkkRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....*
gi 1655274895 1324 LDPEDVdVPHPDEKSIITYVSSLYD 1348
Cdd:cd00014 80 FEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3344-3655 |
2.62e-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: 73.62 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3344 LVEEAENMKKLAEDAARLSIEAQEAARLRQIAED---DLNQQRTLAEKMlKEKMQAIQEASRLKAEAEML--QRQKDLAQ 3418
Cdd:pfam17380 274 LLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAE-KARQAEMDRQAAIYAEQERMamERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3419 -EQAQKLLEDKQLMQQRLDEETE---EYQRsLEAERKRQLEIIAE----AEKLKLQVSQLSEAQAKAEEEAKKFKKQADT 3490
Cdd:pfam17380 353 iRQEERKRELERIRQEEIAMEISrmrELER-LQMERQQKNERVRQeleaARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3491 iaARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAitelEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQ 3570
Cdd:pfam17380 432 --ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ----EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3571 QTFLTEKemllKKEKLIEDEKKKLESQFEEEIKKAKAlkDEQDRQRQQMEEEKLKLKATMDA--------ALNKQKEAEK 3642
Cdd:pfam17380 506 QAMIEEE----RKRKLLEKEMEERQKAIYEEERRREA--EEERRKQQEMEERRRIQEQMRKAteersrleAMEREREMMR 579
|
330
....*....|...
gi 1655274895 3643 DILNKQKEMQELE 3655
Cdd:pfam17380 580 QIVESEKARAEYE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3096-3691 |
2.73e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3096 EELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAK 3175
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3176 ER---AEREAALLRQQAEEAErqkvaaeqeaanqakaqddaERLRKDaefeaaklaqaeaaalkqkqqadEEMAKHKKLA 3252
Cdd:PRK03918 238 EEieeLEKELESLEGSKRKLE--------------------EKIREL-----------------------EERIEELKKE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3253 EQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRL 3332
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3333 MKKDKD----NTQKFLVEEAENMKKLA-----EDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRL 3403
Cdd:PRK03918 355 EELEERhelyEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3404 KAEAEMLQRQkdLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEA--ERKRQLEIIAEAE----KLKLQVSQLSEAQAKA 3477
Cdd:PRK03918 435 KGKCPVCGRE--LTEEHRKELLEEYTAELKRIEKELKEIEEKERKlrKELRELEKVLKKEseliKLKELAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3478 EEEAKKFKKQADTIAARLHETEIATKEQMTEVKKmEFEKLNT-SKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMAD 3556
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK-ELEKLEElKKKLAELEKKLDELEEELAELLKELEELGFESVEELE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3557 AQQKQIE---REMTVLQQTfLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKAtmdaa 3633
Cdd:PRK03918 592 ERLKELEpfyNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR----- 665
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 3634 lNKQKEAEKDILNKQKEMQELERKRLEQERVLadenQKLREKLQQMEEAQKSTLITEK 3691
Cdd:PRK03918 666 -EEYLELSRELAGLRAELEELEKRREEIKKTL----EKLKEELEEREKAKKELEKLEK 718
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5381-5419 |
2.75e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.75e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 5381 LLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMVDRL 5419
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3096-3683 |
2.78e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.85 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3096 EELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLA-QQKEDSMMQNKLKEEYEKAKALARDAEAA 3174
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3175 KERAEREAALLRQQAEEAERQkvaaeQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAaalkqKQQADEEMAKHKKlAEQ 3254
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELR-----AQEAVLEETQERINRARKAAPLAAHIKAVTQI-----EQQAQRIHTELQS-KMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3255 TLKQKFQVEQELTKVKLQLEETDKqkslLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmk 3334
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3335 kdKDNTQKFLVEEAENMKKLAEDAARlSIEAQEAARLR---QIAEDDLNQQRTLAEKMLKEKMQAIQEASR----LKAEA 3407
Cdd:TIGR00618 396 --QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqsLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3408 EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ-----VSQLSEAQAKAEEEAK 3482
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3483 KFKKQADTIAA---RLHETEIATKEQMTEVKKmefEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQ 3559
Cdd:TIGR00618 553 SERKQRASLKEqmqEIQQSFSILTQCDNRSKE---DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3560 K-----QIEREMTvLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMeeeklKLKATMDAAL 3634
Cdd:TIGR00618 630 VrlhlqQCSQELA-LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT-----YWKEMLAQCQ 703
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3635 NKQKEAEKDILNKQKEMQELE------RKRLEQERVLADENQK-----LREKLQQMEEAQ 3683
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIEnassslGSDLAAREDALNQSLKelmhqARTVLKARTEAH 763
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2430-3061 |
3.67e-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: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2430 RLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK------------------R 2491
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatrhlcnllK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2492 ETAAVDAEK------QKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRL----RIEEEIHLIRIQLETTVKQKSNAEDE 2561
Cdd:pfam05483 162 ETCARSAEKtkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2562 LKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANE-------KQKALEDLENLRMQAEE 2634
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEledikmsLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2635 AERQVKQAEVEKERQIQVAHVA--AQQSAAAELRSKQMSFAE----NVSKLEESLKQEHGTVLQLQQDAERLR------- 2701
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAkaAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITMELQKKSSELEemtkfkn 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2702 -KQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSkaEESALKQRDMAENE 2780
Cdd:pfam05483 402 nKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS--EEHYLKEVEDLKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2781 LERQR-RLAESTAQ--------QKLAAEQ-----ELIRLRADFDNAEQQR-------SLLEDELYRLKNEVIAAQQERKQ 2839
Cdd:pfam05483 480 LEKEKlKNIELTAHcdklllenKELTQEAsdmtlELKKHQEDIINCKKQEermlkqiENLEEKEMNLRDELESVREEFIQ 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2840 LEDElskVRSEMDiLIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKlrAIAEEAKHQRQLAEEDAARQRA-EA 2918
Cdd:pfam05483 560 KGDE---VKCKLD-KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK--NIEELHQENKALKKKGSAENKQlNA 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2919 ERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQA-EDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQK 2997
Cdd:pfam05483 634 YEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHK 713
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 2998 AIVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRR 3061
Cdd:pfam05483 714 HQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2331-2900 |
3.80e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2331 LKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTlrtRY 2410
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE---EY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2411 SELMTLTSQYIKFITDTQRRLEDEEKAAEKLKaEEQKKMAEMQAELDKqkqlaeahakaIAKAEKEAQELKLRMQEEVSK 2490
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIE-ERIKELEEKEERLEE-----------LKKKLKELEKRLEELEERHEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2491 RETAavdaeKQKQNiQLELHElKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLI---RIQLETTVKQKSNAEDELKQLRD 2567
Cdd:PRK03918 364 YEEA-----KAKKE-ELERLK-KRLTGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2568 RADAAEklRKLAQEEAEKLRKQVSEETQKkrlAEEELKHKSEAERKAANEK---QKALEDLENLRMQAEEAErQVKQAEv 2644
Cdd:PRK03918 437 KCPVCG--RELTEEHRKELLEEYTAELKR---IEKELKEIEEKERKLRKELrelEKVLKKESELIKLKELAE-QLKELE- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2645 EKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGtvlqLQQDAERLRKQQEDAENAREEAERELEKWRQK 2724
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2725 ANEALRLRLQAEEEAHKKSLaqeeaekqkeeadrEAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIR 2804
Cdd:PRK03918 586 SVEELEERLKELEPFYNEYL--------------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2805 LRADFDNAEQQRslLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILiqlksRAEKETMSNTEKSKQLLEAEATKLR 2884
Cdd:PRK03918 652 LEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKELEKLEKALERVE 724
|
570
....*....|....*.
gi 1655274895 2885 DLAEEASKLRAIAEEA 2900
Cdd:PRK03918 725 ELREKVKKYKALLKER 740
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2151-2896 |
4.00e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.46 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2151 RSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHT--VPNDVKEVETYRTNLKKMRAEAEA 2228
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHerKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2229 EQPVFDSLEEELKKASAVSDKMSR---------VHSERDAELDQHRQ---------HLSSLQDRWKAVFTQIDLRQRELD 2290
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARieelraqeaVLEETQERINRARKaaplaahikAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2291 QL--GRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEknkdKVDECQKYAKAYIDIIKD 2368
Cdd:TIGR00618 325 KLlmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH----TLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2369 YELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEyvtLRTRYSELMTLTSQyiKFITDTQRRLEDEEKAAEKLKAEEQkK 2448
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE---LQQRYAELCAAAIT--CTAQCEKLEKIHLQESAQSLKEREQ-Q 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2449 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKReTAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQVD 2528
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQTYAQL-ETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2529 EALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRdraDAAEKLRKLAQEEAEkLRKQVSEETQKKrlaEEELKHKS 2608
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ---NITVRLQDLTEKLSE-AEDMLACEQHAL---LRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2609 EAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQmSFAENVSKLEESLKQEHG 2688
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ-SEKEQLTYWKEMLAQCQT 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2689 TVLQLQQDAERLRKQQEDAenareeaerelekwrQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADRE-AKKRSKAE 2767
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEI---------------ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTeAHFNNNEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2768 ESALKQRDMAENELER----QRRLAEsTAQQKLAAEQELIRLRADFDnaEQQRSLledelyrlknEVIAAQQERKQLede 2843
Cdd:TIGR00618 770 VTAALQTGAELSHLAAeiqfFNRLRE-EDTHLLKTLEAEIGQEIPSD--EDILNL----------QCETLVQEEEQF--- 833
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2844 LSKVRSEMDILIQLKSRAEKetMSNTEKSKQLLEAEATKLRDLAEEASKLRAI 2896
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLK--YEECSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3402-3711 |
4.04e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3402 RLKAEAE------MLQRQKDLAQEQAQKL-LEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSeaq 3474
Cdd:COG1196 204 PLERQAEkaeryrELKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE--- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3475 akaeeeakkfkkqaDTIAARLHETEIATKEQMTEVKKMEFEKlntsKEADDLRKAITELEKEKARLKKEAEEHQnksKEM 3554
Cdd:COG1196 281 --------------LELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELEELE---EEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3555 ADAQQKQIEREmtvlqqtflTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAAL 3634
Cdd:COG1196 340 EELEEELEEAE---------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 3635 NKQKEAEKdiLNKQKEMQELERKRLEQERvLADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDG 3711
Cdd:COG1196 411 ALLERLER--LEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2359-2960 |
5.33e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2359 AKAYIDIIKDYELQLVAYKAQVEPLTsPLKKTKldsasdniiQEYVTLRTRYSELMTLtsqyikfitDTQRRLEDEEKAA 2438
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLE-PIRELA---------ERYAAARERLAELEYL---------RAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2439 EKLKAEEQkkmaEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAA----VDAEKQKQNIQLELHELKN 2514
Cdd:COG4913 291 ELLEAELE----ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereiERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2515 L----------SEQQIKDKSQQVDEALKsrlRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAE 2584
Cdd:COG4913 367 LlaalglplpaSAEEFAALRAEAAALLE---ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2585 KLRKQVSEETQkkrLAEEELKHKSEA-ERKAANEK-QKALEDLenLRMQA------EEAERQVKQA--EVEKERQIQVAH 2654
Cdd:COG4913 444 ALRDALAEALG---LDEAELPFVGELiEVRPEEERwRGAIERV--LGGFAltllvpPEHYAAALRWvnRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2655 VAAQQSAAAELRSKQMSFAENV----SKLEESLKQEHG---------TVLQLQQD-----AERLRKQqedaenareeAER 2716
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLdfkpHPFRAWLEAELGrrfdyvcvdSPEELRRHpraitRAGQVKG----------NGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2717 ELEKWRQKA----------NEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELER-QR 2785
Cdd:COG4913 589 RHEKDDRRRirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2786 RLAEstaqqklaAEQELIRLRADFDNAEQqrslLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKET 2865
Cdd:COG4913 669 EIAE--------LEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2866 MSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKE--------------KLAAISD 2931
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPE 816
|
650 660 670
....*....|....*....|....*....|
gi 1655274895 2932 -ATRLKTEAEIALKEKEAENERLRRQAEDE 2960
Cdd:COG4913 817 yLALLDRLEEDGLPEYEERFKELLNENSIE 846
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4131-4168 |
5.71e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 5.71e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1655274895 4131 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPELHEKL 4168
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
1111-1222 |
7.15e-12 |
|
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: 65.52 E-value: 7.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1111 ERDRvQKKTFTKWVNKhlIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserDVARSVRLPREKGRMRFHKLQNVQIA 1190
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSV----NWKKVNKAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1655274895 1191 LDFLRHRQVKLVNIRNDDIADGNPKLTLGLIW 1222
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2439-2658 |
8.05e-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: 72.08 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2439 EKLKAEEQKKMAEMQAELD---KQKQLAEAHAKAIAKAEKEAQELKlRMQEEVSKRETAAVDAEKQKQNIQLELHELKNl 2515
Cdd:pfam17380 381 ERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIR-AEQEEARQREVRRLEEERAREMERVRLEEQER- 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2516 sEQQIKDKSQQVDEALKSRLRIEEEIhliRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEEtQ 2595
Cdd:pfam17380 459 -QQQVERLRQQEEERKRKKLELEKEK---RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-E 533
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2596 KKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQ 2658
Cdd:pfam17380 534 RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1249-1344 |
8.88e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 64.71 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1249 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1655274895 1328 DVDVPHPDEKSIITYVS 1344
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2557-3565 |
9.92e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.30 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2557 NAEDELKQLRDRADAAEKLRKlAQEEAEKLRKQVSEETQKKRLAEEELKHKS-------EAERkAANEKQKALEDLENLR 2629
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAA-EQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqTALR-QQEKIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2630 MQAEEaerqvkQAEVEKERQIQVAHVAAQQSAAAElrsKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQE---D 2706
Cdd:PRK04863 362 ERLEE------QNEVVEEADEQQEENEARAEAAEE---EVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcgL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2707 AENAREEAERELEKWRQKANEALRLRLQAEE---------EAHKKSLAQEEAEKQKEeaDREAKKRS--KAEESALKQRD 2775
Cdd:PRK04863 433 PDLTADNAEDWLEEFQAKEQEATEELLSLEQklsvaqaahSQFEQAYQLVRKIAGEV--SRSEAWDVarELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2776 MAENELERQRRLAEstAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEviaAQQERKQLEDELSKV---RSEM- 2851
Cdd:PRK04863 511 LAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEArerRMALr 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2852 DILIQLKSRAEKetmsNTEKSKQLLEAEA--TKLRDLAEEA--------SKLRAIAEEAKHQRQLAEEDAARQRAEAERI 2921
Cdd:PRK04863 586 QQLEQLQARIQR----LAARAPAWLAAQDalARLREQSGEEfedsqdvtEYMQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2922 LKEKLAAISDATRLKTEAE-------------IALKEK---EAENERLR-----RQAEDEAYQRKILEDQANQHKLeIEE 2980
Cdd:PRK04863 662 ERLSQPGGSEDPRLNALAErfggvllseiyddVSLEDApyfSALYGPARhaivvPDLSDAAEQLAGLEDCPEDLYL-IEG 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2981 KIVLLKKSSDAEMERQKAIVDdtlkqrRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLR 3060
Cdd:PRK04863 741 DPDSFDDSVFSVEELEKAVVV------KIADRQWRYSRFP-EVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQ 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3061 RLVL------------------EEEMR-----RKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEE--A 3115
Cdd:PRK04863 814 RLHQafsrfigshlavafeadpEAELRqlnrrRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADEtlA 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3116 DK--EAEKQIVAAQQAAL---KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAE----AAKERAEREAALLR 3186
Cdd:PRK04863 894 DRveEIREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqqafALTEVVQRRAHFSY 973
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3187 QQAEEaerqkvaaeqeaaNQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKL------AEQTLKqkf 3260
Cdd:PRK04863 974 EDAAE-------------MLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLkssydaKRQMLQ--- 1037
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3261 QVEQELTKVKLQLEETdkqkslLDDELQRLKDEVDDAMRQKASVEEELFKvKIQMEELmklkvRIEEENQRLMKKDKDNT 3340
Cdd:PRK04863 1038 ELKQELQDLGVPADSG------AEERARARRDELHARLSANRSRRNQLEK-QLTFCEA-----EMDNLTKKLRKLERDYH 1105
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3341 QkfLVEEAENMKKLAEDAARLSIEAQEAARL--RQIAEDDLNQQRTLAEKMLKEKMQAIqeasrlkAEAEMLQrqkdlaq 3418
Cdd:PRK04863 1106 E--MREQVVNAKAGWCAVLRLVKDNGVERRLhrRELAYLSADELRSMSDKALGALRLAV-------ADNEHLR------- 1169
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3419 eQAQKLLEDkqlmqqrldeeteeyqrSLEAERKRQLeIIAEAEKLKLQVSQlseaqakaeeeakkfkkqaDTIaarlhet 3498
Cdd:PRK04863 1170 -DVLRLSED-----------------PKRPERKVQF-YIAVYQHLRERIRQ-------------------DII------- 1204
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3499 eiatkeqmtevkkmefeklntskEADDLRKAITELEKEKARLKKEAEEHQNK----SKEMADAQQKQIERE 3565
Cdd:PRK04863 1205 -----------------------RTDDPVEAIEQMEIELSRLTEELTSREQKlaisSESVANIIRKTIQRE 1252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2436-2971 |
1.03e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 72.18 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2436 KAAEKLKAEEQKKMAEMQAELDKQ-----KQLAEAHAK----------AIAKAEKE---AQELKLRMQEEvsKRETAAVD 2497
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLlrtldDQWKEKRDElngelsaadaAVAKDRSEleaLEDQHGAFLDA--DIETAAAD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2498 AEkQKQNIQLEL------HELKNLSEQQIKDKSQQVDEALKSRL-----RIEEEIHLIRiqlETTVKQKSNAEDELKQL- 2565
Cdd:pfam12128 346 QE-QLPSWQSELenleerLKALTGKHQDVTAKYNRRRSKIKEQNnrdiaGIKDKLAKIR---EARDRQLAVAEDDLQALe 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2566 ---RDRADAA-------EKLRKLAQEEAEKLRKQV---SEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQA 2632
Cdd:pfam12128 422 selREQLEAGklefneeEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRR 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2633 EEAERQVKQAEVE-KERQIQVAHVAAQQSAAAE-----LRSKQMSFAENVSKLEESlKQEHGTVLQLQQDAERLRKQQED 2706
Cdd:pfam12128 502 DQASEALRQASRRlEERQSALDELELQLFPQAGtllhfLRKEAPDWEQSIGKVISP-ELLHRTDLDPEVWDGSVGGELNL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2707 AENAREEAERELEKWRQkANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQrdMAENELERQRR 2786
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAA-SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFART--ALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2787 LAESTAQQKLAAEQELIRLRadfDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM---------DILIQL 2857
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERK---DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvvegaldAQLALL 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2858 KSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAK--HQRQlaeEDAARQRAEAER----------ILKEK 2925
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRtlERKI---ERIAVRRQEVLRyfdwyqetwlQRRPR 811
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1655274895 2926 LAA-ISDATRLKTEAEIALKEKEAENERLRRQAEDEayqRKILEDQA 2971
Cdd:pfam12128 812 LATqLSNIERAISELQQQLARLIADTKLRRAKLEME---RKASEKQQ 855
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2832-3572 |
1.07e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.92 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2832 AAQQERKQLEDELSKVrsemDILIQLKSRAEKETMSnTEKSKQLLEAEATKLRDLAEEasklRAIAEEAKHQRQLAEEDA 2911
Cdd:TIGR00618 160 AKSKEKKELLMNLFPL----DQYTQLALMEFAKKKS-LHGKAELLTLRSQLLTLCTPC----MPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2912 ARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVllkkssdA 2991
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV-------T 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2992 EMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLkniaeETQQSKLRAEEEAEKLRRlvlEEEMRRK 3071
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL-----HSQEIHIRDAHEVATSIR---EISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3072 EAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKE------AEKQIVAAQQAALKCNMA-EQQVQSVL 3144
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqlahAKKQQELQQRYAELCAAAiTCTAQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3145 AQQKEDSMMQNKLKEEYEKAKALARDAEAAKE-RAEREAALLRQQAEEAE----------------------------RQ 3195
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRkKAVVLARLLELQEEPCPlcgscihpnparqdidnpgpltrrmqrgEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3196 KVAAEQEAANQAKAQDDAERLRK----------DAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQE 3265
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRaslkeqmqeiQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3266 LTKVKLQLEETDKQKSLlddELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM--KLKVRIEEENQRLMKKDKDNTQKF 3343
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRL---HLQQCSQELALKLTALHALQLTLTQERVREHALSirVLPKELLASRQLALQKMQSEKEQL 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3344 ------LVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKE-------KMQAIQEASRLKAEAEML 3410
Cdd:TIGR00618 693 tywkemLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartVLKARTEAHFNNNEEVTA 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3411 QRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEII-AEAEKLKLQVSQLSEAQAKAEEEAKKFKKQAD 3489
Cdd:TIGR00618 773 ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILnLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3490 TIAARLHETEIATKEQ---MTEVKKME-FEKLNTSKEADDLRKAITELEKEKARLKKEAEE---HQNKSKEMADAQQKQI 3562
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQakiIQLSDKLNgINQIKIQFDGDALIKFLHEITLYANVRLANQSEgrfHGRYADSHVNARKYQG 932
|
810
....*....|
gi 1655274895 3563 EREMTVLQQT 3572
Cdd:TIGR00618 933 LALLVADAYT 942
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3247-3690 |
1.13e-11 |
|
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: 71.59 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3247 KHKKLAEQTLKQKFQV----------EQELTKVKLQLEETDKQKSLLDDELQRLKD-------EVDDAMRQKASVEEELF 3309
Cdd:TIGR04523 212 KNKSLESQISELKKQNnqlkdniekkQQEINEKTTEISNTQTQLNQLKDEQNKIKKqlsekqkELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3310 KVKIQMEELMKLK-------VRIEEENQrlmKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQ 3382
Cdd:TIGR04523 292 QLKSEISDLNNQKeqdwnkeLKSELKNQ---EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3383 RTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIiaeaEK 3462
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI----KD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3463 LKLQVSQLSEAqakaeeeakkfkkqadtiaarLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKK 3542
Cdd:TIGR04523 445 LTNQDSVKELI---------------------IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3543 EAEEHQNKSKEMADAQQKQIEREMTVlqqtfltEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEE 3622
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKL-------ESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3623 KLKLKATMDAA--LNKQKEAEKDILNKQKEMQELERKRLEQERVLAD-ENQKLREKLQQMEEAqKSTLITE 3690
Cdd:TIGR04523 577 QKSLKKKQEEKqeLIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKkENEKLSSIIKNIKSK-KNKLKQE 646
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2856-3165 |
1.28e-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: 71.69 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2856 QLKSRAEKETMS-NTEKSKQLLEAEATKLRDLAEEAS----KLRAIAEEAKHQRQLAEEDAARqraEAERILKEKLAAIS 2930
Cdd:pfam17380 298 QERLRQEKEEKArEVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKR---ELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2931 DATRlktEAEIALKEKEAENERLRRQAEdEAYQRKILEDQaNQHKLEiEEKIVLLKKSSDAEMERQKAIvddtlkqRRVV 3010
Cdd:pfam17380 375 SRMR---ELERLQMERQQKNERVRQELE-AARKVKILEEE-RQRKIQ-QQKVEMEQIRAEQEEARQREV-------RRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3011 EEEIRILklnfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLvleEEMRRKEAEDKVKKIAAAEEEAARQ 3090
Cdd:pfam17380 442 EERAREM----ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA---EEQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 3091 RKAAQEELDRLQKK-ADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAK 3165
Cdd:pfam17380 515 RKLLEKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2807-3553 |
1.45e-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: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2807 ADFDNAE---QQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSemdiLIQLKSRAEKETMSNTEKSKQLLEAEATKL 2883
Cdd:pfam05483 68 SDFENSEglsRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQELQFENEKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2884 RDLAEEASKLRaiaeeakHQRQLAEEDAARQRAEAERILKEKlaaiSDATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 2963
Cdd:pfam05483 144 KDLIKENNATR-------HLCNLLKETCARSAEKTKKYEYER----EETRQVYMDLNNNIEKMILAFEELRVQAENARLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2964 R--KILEDQANQHKLEIEEKivllKKSSDAEMERQKAIVDDTlkqrrvvEEEIRILKLNFEkassgkldLELELNKLKNI 3041
Cdd:pfam05483 213 MhfKLKEDHEKIQHLEEEYK----KEINDKEKQVSLLLIQIT-------EKENKMKDLTFL--------LEESRDKANQL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3042 AEETQQsklraeeEAEKLRRLVLEEEMRRKEAEDkvkkIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEK 3121
Cdd:pfam05483 274 EEKTKL-------QDENLKELIEKKDHLTKELED----IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3122 QIVAAQQAALKCNMAEQQVQSVLAQQkedsmmQNKLKEEYEKAKALARDAEAAKERAEREAALLR-QQAEEAERQKVAAE 3200
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTE------QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnKEVELEELKKILAE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3201 QEAANQAKAQddAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQK 3280
Cdd:pfam05483 417 DEKLLDEKKQ--FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3281 SLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKlKVRIEEENQRLMKKDKDNTQKFLVEEAENMK----KLAE 3356
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLRDELESVREEFIQKGDEVKckldKSEE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3357 DAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLD 3436
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3437 EETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQ---------------LSEAQAKAEEEAKKFKKQADTIAARLHETEIA 3501
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklqkeidkrcqhkIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3502 TKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKE 3553
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
1247-1349 |
1.47e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 64.30 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|...
gi 1655274895 1327 EDVdVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHFHSA 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2411-2895 |
1.60e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2411 SELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKkmaemQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK 2490
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEER-----REELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2491 RETAAVDAEkqkqniqlELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRAD 2570
Cdd:PRK02224 288 LEELEEERD--------DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2571 ----AAEKLRKLAQEEAEKLRKQVSE--------ETQKKRLAE--------EELKHKSEAERKAANEKQKALE-DLENLR 2629
Cdd:PRK02224 360 elreEAAELESELEEAREAVEDRREEieeleeeiEELRERFGDapvdlgnaEDFLEELREERDELREREAELEaTLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2630 MQAEEA--------------------------ERQVKQAEVEKER---QIQVAHVAA---QQSAAAELRSKQMSFAENVS 2677
Cdd:PRK02224 440 ERVEEAealleagkcpecgqpvegsphvetieEDRERVEELEAELedlEEEVEEVEErleRAEDLVEAEDRIERLEERRE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2678 KLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAD 2757
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQRDMAENELERQRRLAE-STAQQKLAAEQELIRL---RADFDNAEQQRSLLEDELYRLKneviaa 2833
Cdd:PRK02224 600 AIADAEDEIERLREKREALAELNDERRERLAEkRERKRELEAEFDEARIeeaREDKERAEEYLEQVEEKLDELR------ 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 2834 qQERKQLEDELSKVRSEMDILIQLKSRAEKetmsntekskqlLEAEATKLRDLAEEASKLRA 2895
Cdd:PRK02224 674 -EERDDLQAEIGAVENELEELEELRERREA------------LENRVEALEALYDEAEELES 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2761-3195 |
1.93e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2761 KKRSKAEESALKQRDmaenELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLK---------NEVI 2831
Cdd:COG4717 60 KPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2832 AAQQERKQLEDELSKVRSEMDILIQLKSRAEKetmsntekskqlLEAEATKLR-DLAEEASKLRAIAEEAKHQRQLAEED 2910
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEE------------LEAELAELQeELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2911 AARQRAEAERILKEKLAAISDAtrlktEAEIALKEKEAENERLRRQAEDEAYQRKIL---------EDQANQHKLEIEEK 2981
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEEL-----EEELEQLENELEAAALEERLKEARLLLLIAaallallglGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2982 IVLL----------KKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDlelELNKLKNIAEETQQSKLR 3051
Cdd:COG4717 279 LFLVlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE---ELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3052 AEEEAEKLRRLVLEEEMRRKEAEDKVKKIaaaeeEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAAL 3131
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDE-----EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 3132 kcnmaEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKE--RAEREAALLRQQAEEAERQ 3195
Cdd:COG4717 431 -----EEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2776-3122 |
2.27e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2776 MAENELERQrrLAESTAQQKLAAEQELirlRADFDNAEQQRslledeLYRLKNEVIAAQQERKQLEDELSKVRSEMDIli 2855
Cdd:pfam17380 265 MTENEFLNQ--LLHIVQHQKAVSERQQ---QEKFEKMEQER------LRQEKEEKAREVERRRKLEEAEKARQAEMDR-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2856 QLKSRAEKETMSnTEKSKQLleaEATKLRDLAEEASKLRA--IAEEAKHQRQLaeedaarQRAEAERILKEKlaaisdat 2933
Cdd:pfam17380 332 QAAIYAEQERMA-MEREREL---ERIRQEERKRELERIRQeeIAMEISRMREL-------ERLQMERQQKNE-------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2934 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEI----EEKIVLLKKSSDAEMERQkaivddtlkqrrv 3009
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVrrleEERAREMERVRLEEQERQ------------- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3010 veEEIRILKLNFEKASSGKLDLELELNKLKNIAEetqQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAAR 3089
Cdd:pfam17380 460 --QQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
|
330 340 350
....*....|....*....|....*....|...
gi 1655274895 3090 QRKAaqEELDRLQKKADEVRKQKEEADKEAEKQ 3122
Cdd:pfam17380 535 RREA--EEERRKQQEMEERRRIQEQMRKATEER 565
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3250-3674 |
2.67e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3250 KLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEeelfkvkiQMEELMKLKVRIEEEN 3329
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3330 QRLmkkdkdntqKFLVEEAENMKKLAEDAARLSIEAQEAarlrqiaeddlnqQRTLAEKMLKEKMQAIQEASRLKAEAEM 3409
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3410 LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAE----------------------AEKLKLQV 3467
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3468 SQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEh 3547
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3548 qnkskemadAQQKQIEREMT-VLQQTFLTEKEMLLKKEKL------IEDEKKKLESQFEEEIKKAKALKDEQDRQrqQME 3620
Cdd:COG4717 363 ---------LQLEELEQEIAaLLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALDEE--ELE 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3621 EEKLKLKATMDAALNKQKEAEKDILNKQKEMQELE------RKRLEQERVLADENQKLRE 3674
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEedgelaELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2759-2961 |
2.69e-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: 69.02 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2759 EAKKRSKAEESALKQR-DMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQER 2837
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2838 KQLEDELSKV---------RSEMDILiqLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQ--- 2905
Cdd:COG4942 100 EAQKEELAELlralyrlgrQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAele 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2906 --LAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAEN-----ERLRRQAEDEA 2961
Cdd:COG4942 178 alLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElealiARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2866-3643 |
6.98e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.60 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2866 MSNTEKSKQLLEAEATKLRDLAEEASKLraIAEEAKHQRqLAEEdaARQRAEAERILKEKLAAISDATRLKTEAeIALKE 2945
Cdd:COG3096 274 MRHANERRELSERALELRRELFGARRQL--AEEQYRLVE-MARE--LEELSARESDLEQDYQAASDHLNLVQTA-LRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2946 K--------EAENERLRRQA---EDEAYQRKILEDQANQHKLEIEEKivllkKSSDAEmeRQKAIvdDTLkQRRVVEEEI 3014
Cdd:COG3096 348 KieryqedlEELTERLEEQEevvEEAAEQLAEAEARLEAAEEEVDSL-----KSQLAD--YQQAL--DVQ-QTRAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3015 RILKLNFEKASSGKLDLELElnklkNIAEETQQskLRAEEEAEKLRRLVLEEEMRRKEAedkvkkiaaaeeeAARQRKAA 3094
Cdd:COG3096 418 AVQALEKARALCGLPDLTPE-----NAEDYLAA--FRAKEQQATEEVLELEQKLSVADA-------------ARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3095 qeeLDRLQKKADEV-RKQKEEADKEA-----EKQIVAAQQAALKCNMAE-----QQVQSVLAQQKEDSMMQNK------- 3156
Cdd:COG3096 478 ---YELVCKIAGEVeRSQAWQTARELlrryrSQQALAQRLQQLRAQLAEleqrlRQQQNAERLLEEFCQRIGQqldaaee 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3157 LKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRK--DAEFEAAklaqaeaaa 3234
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREqsGEALADS--------- 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3235 lkqkQQADEEMakhkklaEQTLKQKFQVEQELTKVKLQLEETDKQKSLL-------DDELQRLKDE-------------- 3293
Cdd:COG3096 626 ----QEVTAAM-------QQLLEREREATVERDELAARKQALESQIERLsqpggaeDPRLLALAERlggvllseiyddvt 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3294 VDDA---------MRQkASVEEELFKVKIQM---------------------------EELMKLKVRIEEENQ------- 3330
Cdd:COG3096 695 LEDApyfsalygpARH-AIVVPDLSAVKEQLagledcpedlyliegdpdsfddsvfdaEELEDAVVVKLSDRQwrysrfp 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3331 ---RLMKKDKDNTQKFLVEEAEnmkKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLA-----EKMLKEKMQAIQEASR 3402
Cdd:COG3096 774 evpLFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3403 LKAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQQRLDEETEEYQRSLEAERK--------RQLEIIAEA- 3460
Cdd:COG3096 851 ELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETL-ADRLEELREELDAAQEAQAFiqqhgkalAQLEPLVAVl 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3461 -------EKLKLQVSQLSeaqAKAEEEAKKFKKQADTIAARLHeteiatkeqmtevkkmefekLNTSKEADDLRKAITEL 3533
Cdd:COG3096 930 qsdpeqfEQLQADYLQAK---EQQRRLKQQIFALSEVVQRRPH--------------------FSYEDAVGLLGENSDLN 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3534 EKEKARLkKEAEEHQNKSKEMADAQQKQIE---REMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEeikKAKALKD 3610
Cdd:COG3096 987 EKLRARL-EQAEEARREAREQLRQAQAQYSqynQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEE---RARIRRD 1062
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1655274895 3611 E------QDRQRQ-QMEEEKLKLKATMDAALNKQKEAEKD 3643
Cdd:COG3096 1063 ElheelsQNRSRRsQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2614-3191 |
7.34e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2614 AANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQmsfaenvskleeSLKQEHGTVLQL 2693
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAL------------RLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2694 QQDAERLRKQQedaenareeaerelekwrqKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADR--EAKKRSKAEESAL 2771
Cdd:COG4913 294 EAELEELRAEL-------------------ARLEAELERLEARLDALREELDELEAQIRGNGGDRleQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2772 KQRdmaENELERQRRLAESTAQQKLAAEQELIRLRADF----DNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSkv 2847
Cdd:COG4913 355 EER---ERRRARLEALLAALGLPLPASAEEFAALRAEAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2848 rsemdiliQLKSRAeketmSNtekskqlLEAEATKLRDLAEEA-----SKLRAIAEEAkhqrQLAEEDAARQRAeAERIL 2922
Cdd:COG4913 430 --------SLERRK-----SN-------IPARLLALRDALAEAlgldeAELPFVGELI----EVRPEEERWRGA-IERVL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2923 ----------KEKLAAIS---DATRLKTEAEIaLKEKEAENERLRRQAEDEAYQRKI--------------LEDQANQHK 2975
Cdd:COG4913 485 ggfaltllvpPEHYAAALrwvNRLHLRGRLVY-ERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawleaeLGRRFDYVC 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2976 LEIEEKI----------VLLKKSSDA-EMERQKAIVD------DTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKL 3038
Cdd:COG4913 564 VDSPEELrrhpraitraGQVKGNGTRhEKDDRRRIRSryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3039 KNIAEETQQSKLRAEEE------AEKLRRlvLEEEMRR-KEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQ 3111
Cdd:COG4913 644 QERREALQRLAEYSWDEidvasaEREIAE--LEAELERlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3112 KEEADKEAEKQIVAAQQAAlkcNMAEQQVQSVLAQQKEDSMMQNKLKeeyEKAKALARDAEAAKERAEREAALLRQQAEE 3191
Cdd:COG4913 722 LEQAEEELDELQDRLEAAE---DLARLELRALLEERFAAALGDAVER---ELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2429-2982 |
8.19e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2429 RRLEDEEKAAEKlkAEEQKKMaemqaeLDKQKQLAEAHAKAIAKAEkEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLE 2508
Cdd:COG4913 235 DDLERAHEALED--AREQIEL------LEPIRELAERYAAARERLA-ELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2509 LHElknlseQQIKDKSQQVDEALKSRLRIEEEIhliriqLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRK 2588
Cdd:COG4913 306 RLE------AELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2589 QVSEEtqkkrlaEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIqvahvaaqqsaaAELRSK 2668
Cdd:COG4913 374 PLPAS-------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI------------ASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2669 QMSFAENVSKLEESLKQEHGT----------VLQLQQDAERlrkqqedaenareeaerelekWRQKANEAL---RLRLQA 2735
Cdd:COG4913 435 KSNIPARLLALRDALAEALGLdeaelpfvgeLIEVRPEEER---------------------WRGAIERVLggfALTLLV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2736 EEEAHKKSLAQEEAEKQKE-------EADREAKKRSKAEESALKQR-DMAENELER--QRRLAESTAQQKLAAEQEL--- 2802
Cdd:COG4913 494 PPEHYAAALRWVNRLHLRGrlvyervRTGLPDPERPRLDPDSLAGKlDFKPHPFRAwlEAELGRRFDYVCVDSPEELrrh 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2803 ----------------------IRLRAD----FDNAEQqRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQ 2856
Cdd:COG4913 574 praitragqvkgngtrhekddrRRIRSRyvlgFDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2857 LKSRAEKE--------TMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAAR---QRAEAERILKEK 2925
Cdd:COG4913 653 LAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDEL 732
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 2926 LAAISDATRLKTEAEIALKEK--EAENERLRRQAEDEAYQRKI--LEDQANQHKLEIEEKI 2982
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEErfAAALGDAVERELRENLEERIdaLRARLNRAEEELERAM 793
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2800-3457 |
1.19e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2800 QELIRLRADFDNAEQQRSLLEdELYRLKNEVIAAQQERKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQLLEAE 2879
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2880 atkLRDLAEEASKLRAIAEEAKHQRQLA----EEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRR 2955
Cdd:COG4913 311 ---LERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2956 QAEDEAYQRKILEDQANQHKLEIEEKIVLLKKssdaemerqkaivddtlkQRRVVEEEIRILKlnfekasSGKLDLELEL 3035
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRR------------------ELRELEAEIASLE-------RRKSNIPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3036 NKLKN-IAEETQQSK-----------LRAEEE-----AEKL-----RRLVLEEEmrrkeAEDKVKKIAAAEEEAARQRka 3093
Cdd:COG4913 443 LALRDaLAEALGLDEaelpfvgelieVRPEEErwrgaIERVlggfaLTLLVPPE-----HYAAALRWVNRLHLRGRLV-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3094 aqeeLDRLQKKADEVRKQKEEADKEAEK-------------QIVAAQQAALKCNMAEQ------------QV-QSVLAQQ 3147
Cdd:COG4913 516 ----YERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleAELGRRFDYVCVDSPEElrrhpraitragQVkGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3148 KEDsmmQNKLKEEYekakALARDAEAAKERAEREAALLRQQAEEAERQkvaaeqeaanQAKAQDDAERLRKdaefeaakl 3227
Cdd:COG4913 592 KDD---RRRIRSRY----VLGFDNRAKLAALEAELAELEEELAEAEER----------LEALEAELDALQE--------- 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3228 aqaeaaalkqkqqadeemakhKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLD---DELQRLKDEVDDAMRQKASV 3304
Cdd:COG4913 646 ---------------------RREALQRLAEYSWDEIDVASAEREIAELEAELERLDassDDLAALEEQLEELEAELEEL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3305 EEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENmkkLAEDAARLSIEAQEAARLRQIAE--DDLNQQ 3382
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDAVERELRENLEEriDALRAR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3383 RTLAEKMLKEKMQAIQ-----EASRLKAEAE-------MLQRQK--DLAqEQAQKLledKQLMQQRLDEETEEYQRSLEA 3448
Cdd:COG4913 782 LNRAEEELERAMRAFNrewpaETADLDADLEslpeylaLLDRLEedGLP-EYEERF---KELLNENSIEFVADLLSKLRR 857
|
730
....*....|..
gi 1655274895 3449 ER---KRQLEII 3457
Cdd:COG4913 858 AIreiKERIDPL 869
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5031-5069 |
1.68e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.68e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 5031 LLEAQAATGYIIDPIKSLKLTVNEAVSMGTVGPEFKDKL 5069
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3879-3916 |
1.78e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.78e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1655274895 3879 VLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEMNKI 3916
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2167-2647 |
2.28e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2167 LSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAV 2246
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2247 SDKMSRVHSERDAELDQHRQ---HLSSLQDRWKAVFTQIDLRQ---RELDQLGRQLGYYRESYDWLIRWIA---DAKQRQ 2317
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREiekRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHElyeEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2318 ENIQAVpitDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLvayKAQVEPLTS-----PLKKTKL 2392
Cdd:PRK03918 372 EELERL---KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL---KKAIEELKKakgkcPVCGREL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2393 DSasdniiQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEE-----QKKMAEMQAELdkQKQLAEAHA 2467
Cdd:PRK03918 446 TE------EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselikLKELAEQLKEL--EEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2468 KAIAKAEKEAQELKLRM------QEEVSKRETAAVDAEKQKQNIQLELHELKN-LSE--QQIKDKSQQVDEALKSRLRIE 2538
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEeLAEllKELEELGFESVEELEERLKEL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2539 EEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEetQKKRLAEEELKHKSEAERKAANEK 2618
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREEYLELSREL 675
|
490 500
....*....|....*....|....*....
gi 1655274895 2619 QKALEDLENLRMQAEEAERQVKQAEVEKE 2647
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2758-3470 |
2.37e-10 |
|
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: 67.56 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAA-EQELIRLRADFDNAEQQRSLLEDELYRLKNEVI---AA 2833
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEALEDQHGAFLDADIetaAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2834 QQER-KQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRD----LAEEASKLRAIAEEA-------- 2900
Cdd:pfam12128 345 DQEQlPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDklakIREARDRQLAVAEDDlqalesel 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2901 --KHQRQLAE-EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERL------RRQAEDEAYQRKILEDQA 2971
Cdd:pfam12128 425 reQLEAGKLEfNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQeaanaeVERLQSELRQARKRRDQA 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2972 NQHkLEIEEKIVLLKKSSDAEMERQKAIVDDTL-----KQRRVVEEEIRILklnFEKASSGKLDLELELNKLKNIAEETQ 3046
Cdd:pfam12128 505 SEA-LRQASRRLEERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKV---ISPELLHRTDLDPEVWDGSVGGELNL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3047 QSKLRAEEEAEKLRRLVLEEEMRRK--EAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIV 3124
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAASEEELRERldKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3125 AAQQAALKCNMAEQQVQsvlaQQKEDSMmqNKLKEEyekAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAA 3204
Cdd:pfam12128 661 EKQSEKDKKNKALAERK----DSANERL--NSLEAQ---LKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3205 NQAKAQDDAERLRKDAEFEA-AKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQksll 3283
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKAlETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQ---- 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3284 ddELQRLKDevddamrQKASVEEELFKVKIQmeeLMKLKVRIEEENQRLMKKDKDNtQKFLVEEAENMKKLAEDAARLsi 3363
Cdd:pfam12128 808 --RRPRLAT-------QLSNIERAISELQQQ---LARLIADTKLRRAKLEMERKAS-EKQQVRLSENLRGLRCEMSKL-- 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3364 eaqeaARLRQIAEDDlnqqrtlaekmlkekmQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLED-----KQLMQQRLDEE 3438
Cdd:pfam12128 873 -----ATLKEDANSE----------------QAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAET 931
|
730 740 750
....*....|....*....|....*....|..
gi 1655274895 3439 TEEYQRSLEAERKRQLEIIAEAEKLKlQVSQL 3470
Cdd:pfam12128 932 WESLREEDHYQNDKGIRLLDYRKLVP-YLEQW 962
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2220-3023 |
2.41e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2220 KKMRAEAEAEQpVFDSLEEELKKASAVSDKMSRVHSERDaELDQHRQHLSSLQD--------RWKAVFTQIDLRQRELDQ 2291
Cdd:TIGR02169 171 KKEKALEELEE-VEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREyegyellkEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2292 LGRQLGYYRESYDWLIRWIADAKQRQENIQAVpiTDSKTLKEQLAKEKKLLE---EIEKNKDKVDECQKYAKAYIDIIKD 2368
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2369 YELQLVAYKAQVEPLTSPLKKTKLDSASdnIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAE---- 2444
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREinel 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2445 --EQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELK---NLSEQQ 2519
Cdd:TIGR02169 405 krELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeeyDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2520 IKDKSQQVDEALKSRLRIEEE-----------------IH-----LIRIQLETTVKQKSNAEDELKQL--RDRADAAEKL 2575
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERvrggraveevlkasiqgVHgtvaqLGSVGERYATAIEVAAGNRLNNVvvEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2576 RKLAQEEAEK-----LRKQVSEETQKKRLAEEELKHKS----EAERKAANEKQKALED---LENLrmqaEEAERQVKQAE 2643
Cdd:TIGR02169 565 ELLKRRKAGRatflpLNKMRDERRDLSILSEDGVIGFAvdlvEFDPKYEPAFKYVFGDtlvVEDI----EAARRLMGKYR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2644 --------VEKERQIQVAHVAAQ--QSAAAELRSKQMSFAENVSKLEESLKQehgtvlqLQQDAERLRKQQEDAENAREE 2713
Cdd:TIGR02169 641 mvtlegelFEKSGAMTGGSRAPRggILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2714 AERELEKWRQKANealrlRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAE--------ESALKQRDMAENELErqR 2785
Cdd:TIGR02169 714 ASRKIGEIEKEIE-----QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElearieelEEDLHKLEEALNDLE--A 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2786 RLAESTAQQKLAAEQELirlradfdnaEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM-DILIQLKSRAEKE 2864
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKL----------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRiDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2865 TMSNTEKSKQLLEAEATK--LRDLAEEASKLRaiAEEAKHQRQLAEEDAARQRAEAERILKEKLAAisdatRLKTEAEiA 2942
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEaaLRDLESRLGDLK--KERDELEAQLRELERKIEELEAQIEKKRKRLS-----ELKAKLE-A 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2943 LKEKEAENERLRRQAEDEAYQRKILEDQAnQHKLEIEEKIVLLKKSSDA---EMERQKAIVDDTLKQRRVVEEEIRILKL 3019
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQ-AELQRVEEEIRALEPVNMLaiqEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....
gi 1655274895 3020 NFEK 3023
Cdd:TIGR02169 1008 RIEE 1011
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2674-3150 |
2.85e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2674 ENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKqk 2753
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2754 eeadREAKKRSKAEESALKQRDMAENELER-QRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIA 2832
Cdd:COG4717 149 ----EELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2833 AQQERKQLEDELS------KVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQL 2906
Cdd:COG4717 225 LEEELEQLENELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2907 AE-EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDeayqrkiLEDQANQHKLEIEEKIVLL 2985
Cdd:COG4717 305 EElQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-------LEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2986 KKSSDAEMERQKAIvdDTLKQRRVVEEEIRILklnfekassgKLDLELELNKLKNIAEETQQSKLRAEEEaeklrrlvlE 3065
Cdd:COG4717 378 EAGVEDEEELRAAL--EQAEEYQELKEELEEL----------EEQLEELLGELEELLEALDEEELEEELE---------E 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3066 EEMRRKEAEDKVKKIaaaeeeaARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKcnMAEQQVQSVLA 3145
Cdd:COG4717 437 LEEELEELEEELEEL-------REELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALK--LALELLEEARE 507
|
....*
gi 1655274895 3146 QQKED 3150
Cdd:COG4717 508 EYREE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3043-3382 |
2.90e-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: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3043 EETQQSKLRAEEEA---EKLRRLVLEEEMRRKEAE-DKVKKIAAAEEEAARQRkaaQEELDRLQKkadEVRKQKEEADKE 3118
Cdd:pfam17380 294 EKMEQERLRQEKEEkarEVERRRKLEEAEKARQAEmDRQAAIYAEQERMAMER---ERELERIRQ---EERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3119 AEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVA 3198
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3199 AEQEAANQAKAQDDAERLRKdaefeaaklaqaeaaalkqkqqaDEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDK 3278
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQ-----------------------QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3279 QKSLLDDELQRLKDEVDDAMRQKASVEEElfkvkiqmeelmklKVRIEEENQRLMKKDKDNTQKflveeAENMKKLAEDA 3358
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIYEEE--------------RRREAEEERRKQQEMEERRRI-----QEQMRKATEER 565
|
330 340
....*....|....*....|....
gi 1655274895 3359 ARLSIEAQEAARLRQIAEDDLNQQ 3382
Cdd:pfam17380 566 SRLEAMEREREMMRQIVESEKARA 589
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4537-4575 |
2.90e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.90e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 4537 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVAKTL 4575
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2541-2918 |
3.65e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.69 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2541 IHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRklaqeEAEKLRKQvsEETQKKRLAEEELKHKSEAER-KAANEKQ 2619
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR-----EVERRRKL--EEAEKARQAEMDRQAAIYAEQeRMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2620 KALEdlenlRMQAEEAERQVKQ-------AEVEKERQIQVAHVAAQQSAAaelRSKQMSFAENVSKLEESLKQEhgTVLQ 2692
Cdd:pfam17380 348 RELE-----RIRQEERKRELERirqeeiaMEISRMRELERLQMERQQKNE---RVRQELEAARKVKILEEERQR--KIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2693 LQQDAERLRKQQEDAENAreeAERELEKwrQKANEALRLRLQAEEEAHKkslaqeeaekQKEEADREAKKRSKAEESALK 2772
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQR---EVRRLEE--ERAREMERVRLEEQERQQQ----------VERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2773 QRDMAENELERQRRLaestaqqklaaEQELIRLRADFDNAEQQRSLLEDELYRLKNeVIAAQQERKQLEDElskvrsemd 2852
Cdd:pfam17380 483 KRDRKRAEEQRRKIL-----------EKELEERKQAMIEEERKRKLLEKEMEERQK-AIYEEERRREAEEE--------- 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 2853 iliqlkSRAEKEtmsnTEKSKQLLEaeatKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEA 2918
Cdd:pfam17380 542 ------RRKQQE----MEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4870-4907 |
3.81e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.81e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1655274895 4870 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKETNEKL 4907
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2758-3685 |
4.43e-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: 66.90 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALkqrdmaenELERQRRlaesTAQQKLAAEQE-LIRLRADFDNAEQQRSLLEDElYRLKNEVIAAQQE 2836
Cdd:COG3096 275 RHANERRELSERAL--------ELRRELF----GARRQLAEEQYrLVEMARELEELSARESDLEQD-YQAASDHLNLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2837 RKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQLLEAEATKLRdlAEEASKlRAIAEEAKHQRQLaeeDAARQRA 2916
Cdd:COG3096 342 ALRQQEKIERYQEDLE---ELTERLEEQEEVVEEAAEQLAEAEARLEA--AEEEVD-SLKSQLADYQQAL---DVQQTRA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2917 EAERilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQ---ANQHKLEIEEKIVLLKKSSDaEM 2993
Cdd:COG3096 413 IQYQ---QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVCKIAG-EV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2994 ERQKAivDDTLKQrrvVEEEIRILKLNFEKASSGKLDL-ELE-----LNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEE 3067
Cdd:COG3096 489 ERSQA--WQTARE---LLRRYRSQQALAQRLQQLRAQLaELEqrlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3068 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRkqkeeadkeaekqivAAQQAALKcnMAEQQVQSVLAQQ 3147
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL---------------AAQDALER--LREQSGEALADSQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3148 KEDSMMQNKLKEEYEkAKALARDAEAAKERAEREAALLRQQ--AEEAERQKVAAEQEAANQAKAQDDAerlrkdaefeaa 3225
Cdd:COG3096 627 EVTAAMQQLLERERE-ATVERDELAARKQALESQIERLSQPggAEDPRLLALAERLGGVLLSEIYDDV------------ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3226 klaqaeaaalkqkqqADEEMAKHKKL---AEQTLkqkfqVEQELTKVKLQLEETDkqkSLLDDEL--QRLKDEVDDAMRq 3300
Cdd:COG3096 694 ---------------TLEDAPYFSALygpARHAI-----VVPDLSAVKEQLAGLE---DCPEDLYliEGDPDSFDDSVF- 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3301 kaSVEEELFKVKIQMEELMKLKVRIEEEnQRLMKKDKDNTQKFLVEEAEnmkKLAEDAARLSIEAQEAARLRQIAEDDLN 3380
Cdd:COG3096 750 --DAEELEDAVVVKLSDRQWRYSRFPEV-PLFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVG 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3381 QQRTLA-----EKMLKEKMQAIQEASRLKAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQQRLDEETEEY 3442
Cdd:COG3096 824 GHLAVAfapdpEAELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETL-ADRLEELREEL 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3443 QRSLEAERK--------RQLEIIAEA--------EKLKLQVSQLSEAQAKAEEEAKKFkkqADTIAARLHeteiatkeqm 3506
Cdd:COG3096 903 DAAQEAQAFiqqhgkalAQLEPLVAVlqsdpeqfEQLQADYLQAKEQQRRLKQQIFAL---SEVVQRRPH---------- 969
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3507 tevkkmefekLNTSKEADDLRKAITELEKEKARLKkEAEEHQNKSKEMADAQQKQIE---REMTVLQQTFLTEKEMLLKK 3583
Cdd:COG3096 970 ----------FSYEDAVGLLGENSDLNEKLRARLE-QAEEARREAREQLRQAQAQYSqynQVLASLKSSRDAKQQTLQEL 1038
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3584 EKLIEDEKKKLESQFEEeikKAKALKDEqdrqrqqmeeeklklkatMDAALNkQKEAEKDILNKQKEMQELERKRLEQEr 3663
Cdd:COG3096 1039 EQELEELGVQADAEAEE---RARIRRDE------------------LHEELS-QNRSRRSQLEKQLTRCEAEMDSLQKR- 1095
|
970 980
....*....|....*....|..
gi 1655274895 3664 vLADENQKLREKLQQMEEAQKS 3685
Cdd:COG3096 1096 -LRKAERDYKQEREQVVQAKAG 1116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2463-2703 |
5.90e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2463 AEAHAKAIAKAEKEAQELKLRMQEEVSKREtaavDAEKQKQNIQLELHELknlsEQQIKDKSQQVDEalksrlrIEEEIH 2542
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2543 LIRIQLETTVKQKSNAEDELKQLRDR-ADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEeLKHKSEAERKAANEKQKA 2621
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2622 LEDLENLRmqaeeaerqvkqAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLR 2701
Cdd:COG4942 159 LAELAALR------------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
..
gi 1655274895 2702 KQ 2703
Cdd:COG4942 227 AL 228
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3387-3685 |
5.97e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.92 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 EKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEdkQLMQQRLDEETEEYQRslEAERKRQLEiiaEAEKLKlq 3466
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEEKAR--EVERRRKLE---EAEKAR-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3467 vsqlseaqakaeeeakkfKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEK--EKARLKKEA 3544
Cdd:pfam17380 326 ------------------QAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRmrELERLQMER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3545 EEHQNKSKEMADAQQKQI----EREMTVLQQTFLTEKeMLLKKEKLIEDEKKKLESQFEEEIKKAKalKDEQDRQ----- 3615
Cdd:pfam17380 388 QQKNERVRQELEAARKVKileeERQRKIQQQKVEMEQ-IRAEQEEARQREVRRLEEERAREMERVR--LEEQERQqqver 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3616 -RQQMEEEKLKlKATMDAALNKQKEAE---KDILnkQKEMQELERKRLEQERvladeNQKLREKlqQMEEAQKS 3685
Cdd:pfam17380 465 lRQQEEERKRK-KLELEKEKRDRKRAEeqrRKIL--EKELEERKQAMIEEER-----KRKLLEK--EMEERQKA 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3091-3574 |
7.16e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3091 RKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL--A 3168
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3169 RDAEAAKERAEREAALLRQQAEEAERQkvaaeqeAANQAKAQDDAERLRKDAEfeaaklaqaeaaalkqkqqadeemAKH 3248
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEER-------LEELRELEEELEELEAELA------------------------ELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3249 KKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQmEELMKLKVRIEEE 3328
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3329 NQRLMKKDKDNTQKFLVEE---------------AENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQR-------TLA 3386
Cdd:COG4717 256 AALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLaalglppDLS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 EKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKlledKQLMQQRLDEETEEYQRSLEAERKRQlEIIAEAEKLKLQ 3466
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3467 VSQLseaqaKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFE------KLNTSKEADDLRKAITELEKEKARL 3540
Cdd:COG4717 411 LEEL-----LGELEELLEALDEEELEEELEELEEELEELEEELEELREElaeleaELEQLEEDGELAELLQELEELKAEL 485
|
490 500 510
....*....|....*....|....*....|....
gi 1655274895 3541 KKEAEEHQNkskemADAQQKQIEREMTVLQQTFL 3574
Cdd:COG4717 486 RELAEEWAA-----LKLALELLEEAREEYREERL 514
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2443-2623 |
1.09e-09 |
|
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: 62.25 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2443 AEEQKKMAEMQA---ELDKQKQLAEAHAKAIAKAEKEAQELklrmQEEVSKRETAAVDAEKQKQNIQLELHELknlsEQQ 2519
Cdd:COG1579 3 PEDLRALLDLQEldsELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEV----EAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2520 IKDKSQQVDEALKSRlrieeEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRL 2599
Cdd:COG1579 75 IKKYEEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|....
gi 1655274895 2600 AEEELkhksEAERKAANEKQKALE 2623
Cdd:COG1579 150 ELAEL----EAELEELEAEREELA 169
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2980-3639 |
1.25e-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: 65.13 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2980 EKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIAEETQQS-------KLRA 3052
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATrhlcnllKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3053 EEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIvaaqqaalk 3132
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEI--------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3133 cNMAEQQVQSVLAQQKEDsmmQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDD 3212
Cdd:pfam05483 236 -NDKEKQVSLLLIQITEK---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3213 AERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKD 3292
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3293 EVDDAMRQKASVE---EELFKVKIQMEELMKLKVRIEEENQRLMKKDKD-----------------------NTQKFLVE 3346
Cdd:pfam05483 392 ELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQElifllqarekeihdleiqltaikTSEEHYLK 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3347 EAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASrlKAEAEMLQRQKDLAQEQAQKLLE 3426
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK--KQEERMLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3427 ----DKQLMQQRLD-----EETEEYQRSLEAERKRQLEIIAEAEK----LKLQVSQLSEAQAKAEEEAKKFKKQADTIAA 3493
Cdd:pfam05483 550 lesvREEFIQKGDEvkcklDKSEENARSIEYEVLKKEKQMKILENkcnnLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3494 RLHETEIATKEQMTEVK--KMEFEKL--NTSKEADDLR----KAITELEKEKA------RLKKEAEEH-QNKSKEMADAQ 3558
Cdd:pfam05483 630 QLNAYEIKVNKLELELAsaKQKFEEIidNYQKEIEDKKiseeKLLEEVEKAKAiadeavKLQKEIDKRcQHKIAEMVALM 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3559 QKQIEREMTVLQQTfltEKEMLLKKEKliEDEKKKLESQFEEEIK--KAKALKDEQDRQRQQMEEEKLKLKATMDAALNK 3636
Cdd:pfam05483 710 EKHKHQYDKIIEER---DSELGLYKNK--EQEQSSAKAALEIELSniKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
...
gi 1655274895 3637 QKE 3639
Cdd:pfam05483 785 DKK 787
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2863-3196 |
1.43e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.76 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2863 KETMSNTEKSKQLLEAEATKLRDLAEEasklraIAEEAKHQRQLAEEDAARQrAEAERilkeKLAAISDATRLKTEAE-- 2940
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEE------KAREVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAMEREre 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2941 ---IALKEKEAENERLRRQaedeayqrkiledqanqhklEIEEKIVLLKKSSDAEMERQKaivddtlKQRRVVEE--EIR 3015
Cdd:pfam17380 350 lerIRQEERKRELERIRQE--------------------EIAMEISRMRELERLQMERQQ-------KNERVRQEleAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3016 ILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLR--AEEEAEKLRRLVLEEE--------MRRKEAEDKVKKIAAAEE 3085
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrlEEERAREMERVRLEEQerqqqverLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3086 EaaRQRKAAQEELDRLQKKADEVRKQK----EEADKEAEKQIVAAQQAalkcnMAEQQvqsvlaQQKEDSMMQNKLKEEY 3161
Cdd:pfam17380 483 K--RDRKRAEEQRRKILEKELEERKQAmieeERKRKLLEKEMEERQKA-----IYEEE------RRREAEEERRKQQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655274895 3162 EKAKALARDAEAAKERA-----EREAALLRQQAEEAERQK 3196
Cdd:pfam17380 550 ERRRIQEQMRKATEERSrleamEREREMMRQIVESEKARA 589
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2405-3059 |
1.70e-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: 64.77 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2405 TLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDkqkqlaeahakAIAKAEKEAQElklrm 2484
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----------ALAVAEKAGQA----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2485 qeEVSKRETAAVDAEKQKQNI----QLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTvkqksnaed 2560
Cdd:pfam07111 116 --EAEGLRAALAGAEMVRKNLeegsQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETK--------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2561 elkqlrdRADAAEKLrKLAQEEAEKLRKQVSEetqkkrlAEEELkhkseaerkaanEKQKALedLENLRMQ-AEEAERQV 2639
Cdd:pfam07111 185 -------RAGEAKQL-AEAQKEAELLRKQLSK-------TQEEL------------EAQVTL--VESLRKYvGEQVPPEV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2640 KQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLeeslkqEHGTVLQLQQDAERLRKQQEDAENAREEAERELE 2719
Cdd:pfam07111 236 HSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSL------THMLALQEEELTRKIQPSDSLEPEFPKKCRSLLN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2720 KWRQKANeALRLRLQAEEEAHKKSLaqeeAEKQKEEADREAKKRSKAEESALKQRDM----AENELER-----------Q 2784
Cdd:pfam07111 310 RWREKVF-ALMVQLKAQDLEHRDSV----KQLRGQVAELQEQVTSQSQEQAILQRALqdkaAEVEVERmsakglqmelsR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2785 RRLAESTAQQKLAAEQELIRLRADFDNAEQQRslLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE-- 2862
Cdd:pfam07111 385 AQEARRRQQQQTASAEEQLKFVVNAMSSTQIW--LETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQlr 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2863 KETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQlAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIA 2942
Cdd:pfam07111 463 QESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2943 LKEKEAENERLRRQ--AEDEAYQRKILEDQANQHKLEIEEKIVLL------------KKSSDAEMERQKAIVDDTLKQRR 3008
Cdd:pfam07111 542 SVGQQLEVARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVetrlreqlsdtkRRLNEARREQAKAVVSLRQIQHR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 3009 VVEE-----EIRILKLNFEKASSGKLDLEL-ELNKLKNIAEET-QQSKLRAEEEAEKL 3059
Cdd:pfam07111 622 ATQEkernqELRRLQDEARKEEGQRLARRVqELERDKNLMLATlQQEGLLSRYKQQRL 679
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2428-2627 |
2.29e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.29 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2428 QRRLEDEEKaaEKLKAEEQKKMAEMQA--ELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKretAAVDAEKQKQni 2505
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKKAE-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2506 qlelhelknlSEQQIKDKSqqvdEALKsrlrieeeihliriQLETTVKQKSNAEDELKQlrdRADAAEKLRKLAQEEAEK 2585
Cdd:PRK09510 173 ----------AEAAKKAAA----EAKK--------------KAEAEAAAKAAAEAKKKA---EAEAKKKAAAEAKKKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1655274895 2586 LRKQVSE--ETQKKRLAEEELKHKSEAERKAANEkQKALEDLEN 2627
Cdd:PRK09510 222 EAKAAAAkaAAEAKAAAEKAAAAKAAEKAAAAKA-AAEVDDLFG 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2053-2700 |
2.47e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2053 DSLLRSMEKGQQDETLCKNYISEVKDLRLRIEDceartvarirKPVEKEPLKECIQKT-AEQAKVQVELEGLKKDLDKVS 2131
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEE----------ERKRRDKLTEEYAELkEELEDLRAELEEVDKEFAETR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2132 TKTQDilnspqpsatapvLRSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDvkE 2211
Cdd:TIGR02169 385 DELKD-------------YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL--E 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2212 VETYRTNLKKMRAEAEAEQPVFDSLEEELKKasaVSDKMSRVHSERDaELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQ 2291
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDR---VEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2292 LGRQLGYYRESYDWLIRWIADAKqrqenIQAVPITDSKTLKE--QLAKEKKL--LEEIEKNKDKVDECQKyAKAYIDIIK 2367
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKMRDERRDL-SILSEDGVI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2368 DYELQLVAYKAQVEP-----LTSPLKKTKLDSASDNIIQ-EYVTLRTRYSE---LMTLTSQYIKFITDTQR-------RL 2431
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPafkyvFGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRsepaelqRL 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2432 EDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELK------------LRMQEEVSKRETAAVDAE 2499
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeklkerleeLEEDLSSLEQEIENVKSE 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2500 KQK-----QNIQLELHELK--------NLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLR 2566
Cdd:TIGR02169 760 LKEleariEELEEDLHKLEealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2567 DRADAAEKLRKLAQEEAEKLRKQVSE---ETQKKRLAEEELkhksEAERKAANEKQKALE-DLENLRMQAEEAERQVKQA 2642
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEEleeELEELEAALRDL----ESRLGDLKKERDELEaQLRELERKIEELEAQIEKK 915
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2643 EVEKERQIQVAHVAAQQSAAAELRSKQMsfaENVSKLEESLKQEHGTVLQLQQDAERL 2700
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGED---EEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5457-5495 |
3.28e-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: 3.28e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 5457 FLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTAQKL 5495
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
3242-3691 |
3.53e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3242 DEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLL-------DDELQRLKDEVDDAMRQKASVEEELFKVKIQ 3314
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLkgrifpvEDQLEALKSESQNKIELLLQQHQDRIEQLIS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3315 MEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAEN-----MKKLAE---DAARLSIEAQEAARLRQIAEDDLNQQRTLA 3386
Cdd:pfam15921 275 EHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNqnsmyMRQLSDlesTVSQLRSELREAKRMYEDKIEELEKQLVLA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 EKMLKE----KMQAIQEASRL-----KAEAEMLQRQKDLAQEQAQ-------------------KLLEDKQLMQQRLDEE 3438
Cdd:pfam15921 355 NSELTEarteRDQFSQESGNLddqlqKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhlrRELDDRNMEVQRLEAL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3439 TEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLN 3518
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3519 TSKEADDLRKAITELEKEKARLKKEAEEHQNKSKE-------MADAQQ------KQIEREMTVLQQTFLTEKEMLLKK-- 3583
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqMAEKDKvieilrQQIENMTQLVGQHGRTAGAMQVEKaq 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3584 -EKLIEDEKKklesqfeeEIKKAKALKDEQDRQRQQMEE-------EKLKL--------------KATMDAALNKQKEAE 3641
Cdd:pfam15921 595 lEKEINDRRL--------ELQEFKILKDKKDAKIRELEArvsdlelEKVKLvnagserlravkdiKQERDQLLNEVKTSR 666
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3642 KDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEK 3691
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2414-2966 |
5.00e-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: 63.32 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2414 MTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQK-KMAEMQAELDKQKQlAEAHAKAIAKAEKEAQELKLRMQEEVSKRE 2492
Cdd:pfam12128 356 LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIKDKLAKIRE-ARDRQLAVAEDDLQALESELREQLEAGKLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2493 taavdAEKQKQNIQLELHELKNLSEQQikdksqQVDEALKSRLRI-EEEIHLIRIQLETTVKQKSNAEDELKQLRDRAD- 2570
Cdd:pfam12128 435 -----FNEEEYRLKSRLGELKLRLNQA------TATPELLLQLENfDERIERAREEQEAANAEVERLQSELRQARKRRDq 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2571 AAEKLR---------KLAQEEAEK------------LRKQVSEETQK-KRLAEEELKHKSEAERKAANEKQKALEDLE-- 2626
Cdd:pfam12128 504 ASEALRqasrrleerQSALDELELqlfpqagtllhfLRKEAPDWEQSiGKVISPELLHRTDLDPEVWDGSVGGELNLYgv 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2627 NLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAEnvSKLEESLKQEHGTVLQLQQDAERLRKQQED 2706
Cdd:pfam12128 584 KLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN--GELEKASREETFARTALKNARLDLRRLFDE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2707 AENAREEAERELEKWRQKANEALRlRLQAEEEAHKKSLAQEEaekqkeeadrEAKKRSKAEESALKQRDMAENELERQRR 2786
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANERLN-SLEAQLKQLDKKHQAWL----------EEQKEQKREARTEKQAYWQVVEGALDAQ 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2787 LA---ESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQ---LKSR 2860
Cdd:pfam12128 731 LAllkAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlQRRP 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2861 AEKETMSNTEKSKQLLEAEATKLrdlaEEASKLRaiaeEAKHQRQLAEEDAARQRAEAE----RILKEKLAAIS-DATRL 2935
Cdd:pfam12128 811 RLATQLSNIERAISELQQQLARL----IADTKLR----RAKLEMERKASEKQQVRLSENlrglRCEMSKLATLKeDANSE 882
|
570 580 590
....*....|....*....|....*....|.
gi 1655274895 2936 KTEAEIALKEKEAENERLRRQAEDEAYQRKI 2966
Cdd:pfam12128 883 QAQGSIGERLAQLEDLKLKRDYLSESVKKYV 913
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4206-4244 |
5.30e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 5.30e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 4206 LLDAQMTTGGIIDPVKSHRVPHDVACNRSYFDDEMKQHL 4244
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2612-2965 |
5.51e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.83 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2612 RKAANEKQKAlEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQS--AAAELRSKQMSFAENVSKLEESLKQEhgt 2689
Cdd:pfam17380 281 QKAVSERQQQ-EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELERIRQE--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2690 vlQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAeeeahkkslaqeeaekqkeeadreAKKRSKAEEs 2769
Cdd:pfam17380 357 --ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA------------------------ARKVKILEE- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2770 alkqrdmaenelERQRRLAESTAQ-QKLAAEQELIRlradfdnaEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVR 2848
Cdd:pfam17380 410 ------------ERQRKIQQQKVEmEQIRAEQEEAR--------QREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2849 SEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLA-EEDAARQRAEAER---ILKE 2924
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1655274895 2925 KLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 2965
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3038-3441 |
6.24e-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: 62.22 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3038 LKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKkiaaaeeeaaRQRKAAQEELDRLQKkadEVRKQKEEADK 3117
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE----------RQRRELESRVAELKE---ELRQSREKHEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3118 EAEKQivaAQQAALKCNMAEQQvqSVLAQQKEDSmmQNKLKEEYEKAKALARDA-------EAAKERAEREAALLRQqaE 3190
Cdd:pfam07888 99 LEEKY---KELSASSEELSEEK--DALLAQRAAH--EARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKE--E 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3191 EAERQKVAAEQEaanqakaQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKklaeqtLKQKFQVEQELTKVK 3270
Cdd:pfam07888 170 EAERKQLQAKLQ-------QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK------LTTAHRKEAENEALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3271 LQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEEL------MKLKVRieeENQRLMKKDKDNTQKFL 3344
Cdd:pfam07888 237 EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLtlqladASLALR---EGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3345 VEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEasrLKAEAEMLQRQKDLAQEQAQKL 3424
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQEL 390
|
410
....*....|....*..
gi 1655274895 3425 LEDKQLMQQRLDEETEE 3441
Cdd:pfam07888 391 LEYIRQLEQRLETVADA 407
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2425-2642 |
6.46e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2425 TDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklrmQEEVSKRETAAVDAEKQKQN 2504
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2505 IQLELHELKNLSEQQIKD--------------KSQQVDEALKsRLRIEEEIHLIRIQLETTVKQKSnaeDELKQLRDRAD 2570
Cdd:COG4942 95 LRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVR-RLQYLKYLAPARREQAEELRADL---AELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 2571 AAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENL--RMQAEEAERQVKQA 2642
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTP 244
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2220-2701 |
6.46e-09 |
|
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: 62.45 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2220 KKMRAEAEAEQPVFDSLEEELKKASavsdkmsrvhsERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYY 2299
Cdd:pfam05557 69 EALREQAELNRLKKKYLEALNKKLN-----------EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2300 RESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQLAKEKKLLEEIEKNKDkvdecqkyakaYIDIIKDYELQLvaykAQ 2379
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEK----QQSSLAEAEQRIKELEFEIQSQEQ-----------DSEIVKNSKSEL----AR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2380 VEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSElmtltsqyikfitDTQRRLEDEEKAAEKLKAEEQKKmAEMQAELDKQ 2459
Cdd:pfam05557 199 IPELEKELERLREHNKHLNENIENKLLLKEEVE-------------DLKRKLEREEKYREEAATLELEK-EKLEQELQSW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2460 KQLAEAHAKAIAKAEKEAQELKLRMQEEV--SKRETAAVDAEKQKQNIQLELHE-----LKNLSEQQIKDKSQqvdEALK 2532
Cdd:pfam05557 265 VKLAQDTGLNLRSPEDLSRRIEQLQQREIvlKEENSSLTSSARQLEKARRELEQelaqyLKKIEDLNKKLKRH---KALV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2533 SRLR-----IEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAE-KLRKQVSEET---QKKRLAEEE 2603
Cdd:pfam05557 342 RRLQrrvllLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEmEAQLSVAEEElggYKQQAQTLE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2604 LKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEK-ERQIQVAHVAAQQSAAAElRSKQMSFAEN-VSKLEE 2681
Cdd:pfam05557 422 RELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKnELEMELERRCLQGDYDPK-KTKVLHLSMNpAAEAYQ 500
|
490 500
....*....|....*....|
gi 1655274895 2682 SLKQEHGtvlQLQQDAERLR 2701
Cdd:pfam05557 501 QRKNQLE---KLQAEIERLK 517
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5379-5416 |
7.67e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 7.67e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1655274895 5379 QRLLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMV 5416
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3036-3220 |
8.52e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.01 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3036 NKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEdkvkkiaaaeeeaarQRKAAQEEldrlQKKADEVRKQKEEA 3115
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE---------------QRAAAEKA----AKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3116 DKEAE--KQIVAAQQAALKCNMAEQQVQSVLAQQKEdsmmQNKLKEEYEKAKALARDAEA-----AKERAEREAallRQQ 3188
Cdd:TIGR02794 118 QKQAEeaKAKQAAEAKAKAEAEAERKAKEEAAKQAE----EEAKAKAAAEAKKKAEEAKKkaeaeAKAKAEAEA---KAK 190
|
170 180 190
....*....|....*....|....*....|..
gi 1655274895 3189 AEEAERQKVAAEQEAANQAKAQDDAERLRKDA 3220
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAA 222
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1117-1225 |
8.74e-09 |
|
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: 56.43 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1117 KKTFTKWVNKHLIKSQ---------RHVTDLYEDLRDGHNLISLLEVLSGDTLlSERdvarsvRLPREKGRMRFHKLQNV 1187
Cdd:cd21217 3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTI-DER------KLNKKKPKNIFEATENL 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 1188 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21217 76 NLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2441-2643 |
1.36e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.04 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2441 LKAEEQKKMAEMQAELDKQKQLAEAHA-KAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQ--KQNIQLELHELKNLSE 2517
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAkkKAEERREAETARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2518 QQIKDKSQQVDEAlksrlrIEEEIHLIRIQLETTVKQKSNAEDELKQLRD---RADaAEKLRKLAQEEAEKlrkqvsEET 2594
Cdd:COG2268 266 AAYEIAEANAERE------VQRQLEIAEREREIELQEKEAEREEAELEADvrkPAE-AEKQAAEAEAEAEA------EAI 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655274895 2595 QKKRLAEEELKhksEAERKAANEKQKALEDLENLRMQAEEAERQVKQAE 2643
Cdd:COG2268 333 RAKGLAEAEGK---RALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3046-3220 |
1.41e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.59 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3046 QQSKLRAEEEAEKLRRLVLEEEMRRKEAEdkvkkiaaaeeeaaRQRKAAQEEldrlQKKADEVRKQKEEADKEAEKQIVA 3125
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLE--------------KERLAAQEQ----KKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3126 AQQAALKCNMAEQQVQSVLAQQKEDSmmqnklKEEYEKAKALARDAEAAKERAEREAAllrQQAEEAERQKVAAEQEAAN 3205
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAE------AKKKAEAEAAKKAAAEAKKKAEAEAA---AKAAAEAKKKAEAEAKKKA 211
|
170
....*....|....*
gi 1655274895 3206 QAKAQDDAERLRKDA 3220
Cdd:PRK09510 212 AAEAKKKAAAEAKAA 226
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2758-3644 |
1.52e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQRdmaeNELERQRRlaestaqqKLAAEQE-LIRLRADFDNAEQQRSLLEDELYRLK---NEVIAA 2833
Cdd:PRK04863 276 RHANERRVHLEEALELR----RELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2834 QQERKQLEdelskvRSEMDILiQLKSRAEKETMSNTEKSKQLLEAEATKlrDLAEEaSKLRAIAEEAKHQRQLaeeDAAR 2913
Cdd:PRK04863 344 LRQQEKIE------RYQADLE-ELEERLEEQNEVVEEADEQQEENEARA--EAAEE-EVDELKSQLADYQQAL---DVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2914 QRAEAERilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQ---ANQHKLEIEEKIVLLKKSSD 2990
Cdd:PRK04863 411 TRAIQYQ---QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvAQAAHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2991 aEMERQKAivDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNK---LKNIAEETQQSKLRAEEEAEKLRRLVLEEE 3067
Cdd:PRK04863 488 -EVSRSEA--WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3068 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRkqkeeadkeaekqivAAQQAALKcnMAEQQVQSVLAQQ 3147
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL---------------AAQDALAR--LREQSGEEFEDSQ 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3148 KEDSMMQNKLkeEYEKAKALARD-AEAAKERAEREAALLRQ-QAEEAERQKVAaeqeaanqakaqddAER--------LR 3217
Cdd:PRK04863 628 DVTEYMQQLL--ERERELTVERDeLAARKQALDEEIERLSQpGGSEDPRLNAL--------------AERfggvllseIY 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3218 KDAEFeaaklaqaeaaalkqkQQADEEMAKHKKLAEQTlkqkfqVEQELTKVKLQLEETDkqkSLLDD------ELQRLK 3291
Cdd:PRK04863 692 DDVSL----------------EDAPYFSALYGPARHAI------VVPDLSDAAEQLAGLE---DCPEDlyliegDPDSFD 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3292 DEVDDAmrqkasveEELFKVKIQMEELMKLKV-RIEEEnQRLMKKDKDNTQKFLVEEAEnmkKLAEDAARLSIEAQEAAR 3370
Cdd:PRK04863 747 DSVFSV--------EELEKAVVVKIADRQWRYsRFPEV-PLFGRAAREKRIEQLRAERE---ELAERYATLSFDVQKLQR 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3371 LRQIAEDDLNQQRTLA-----EKMLKEKMQAIQEASRLKAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQ 3432
Cdd:PRK04863 815 LHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHEsqeqQQRSQLEQAKEGLSalnrllprlNLLADETL-A 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3433 QRLDEETEEYQRSLEAERK--------RQLEIIAEA--------EKLKLQVSQLseaQAKAEEEAKKFKKQADTIAARLH 3496
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFvqqhgnalAQLEPIVSVlqsdpeqfEQLKQDYQQA---QQTQRDAKQQAFALTEVVQRRAH 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3497 eteiatkeqmtevkkmefekLNTSKEADDLRKAITELEKEKARLKkEAEEHQNKSKEM---ADAQQKQIEREMTVLQQTF 3573
Cdd:PRK04863 971 --------------------FSYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQlrqAQAQLAQYNQVLASLKSSY 1029
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 3574 LTEKEMLlkKEKLIEDEKKKLESQFEEEIKkAKALKDE-------QDRQRQQMEEEKLKLKATMDAALNKQKEAEKDI 3644
Cdd:PRK04863 1030 DAKRQML--QELKQELQDLGVPADSGAEER-ARARRDElharlsaNRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3031-3460 |
1.73e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3031 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQK------- 3103
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllpl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3104 -----KADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvLAQQKEDSMMQNKL--KEEYEKAKALARDAEAAKE 3176
Cdd:COG4717 131 yqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAE-LQEELEELLEQLSLatEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3177 RAEREAALLRQQAEEAERQkvaaEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEM----------- 3245
Cdd:COG4717 210 ELEEELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3246 -----AKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELmk 3320
Cdd:COG4717 286 lallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3321 LKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLsieAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEA 3400
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3401 -SRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEA 3460
Cdd:COG4717 441 lEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2943-3678 |
2.25e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.22 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2943 LKEKEAENERLR---RQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTL--KQRRVVEEEIRIL 3017
Cdd:TIGR00606 250 LKNRLKEIEHNLskiMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVreKERELVDCQRELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3018 KLNFEKA--SSGKLDLELELNKLKNIAEETQ-QSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKK-IAAAEEEAARQRKA 3093
Cdd:TIGR00606 330 KLNKERRllNQEKTELLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFERGPFSERQIKNfHTLVIERQEDEAKT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3094 AQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQ-QKEDSMMQNKLKEEYEKAKALaRDAE 3172
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElQQLEGSSDRILELDQELRKAE-RELS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3173 AAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAER-LRKDAEFEAAKLAQAEAAALKQKQQADEEMAK---- 3247
Cdd:TIGR00606 489 KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTtTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgy 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3248 --HKKLAEQTL----KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDevddamrQKASVEEELFKV-KIQMEE--L 3318
Cdd:TIGR00606 569 fpNKKQLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE-------QLSSYEDKLFDVcGSQDEEsdL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3319 MKLKVRIEEEN-QRLMKKDKDNTQKFLVEEAENMKK----LAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEK 3393
Cdd:TIGR00606 642 ERLKEEIEKSSkQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3394 MQAIQEasrLKAEAEMLQRQKDLAQEQAQKLLEDkqlmQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEA 3473
Cdd:TIGR00606 722 EKRRDE---MLGLAPGRQSIIDLKEKEIPELRNK----LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3474 QAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNT-SKEADDLRKAITELEKEKARLKKEAEEHQNKSK 3552
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3553 EMADA-QQKQIEREMTVLQQTFLTE--KEMLLKKEKLIEDE--KKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLK 3627
Cdd:TIGR00606 875 QIGTNlQRRQQFEEQLVELSTEVQSliREIKDAKEQDSPLEtfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH 954
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3628 ATMDAALNKQKEAEKDILnKQKEMQelerkrLEQERVLADENQKLREKLQQ 3678
Cdd:TIGR00606 955 GYMKDIENKIQDGKDDYL-KQKETE------LNTVNAQLEECEKHQEKINE 998
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2094-2642 |
2.29e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2094 IRKPVEKEPLKECIQKTAE-QAKVQVELEGLKKDLDKVSTKTQDILNSpqpsatapVLRSELELTVQKMDHAYMLSsvyl 2172
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKnIDKFLTEIKKKEKELEKLNNKYNDLKKQ--------KEELENELNLLEKEKLNIQK---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2173 eKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKE-VETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMS 2251
Cdd:TIGR04523 188 -NIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKqNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2252 RVHSERDAELDQHRQHLSSL-------------------QDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIAD 2312
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELekqlnqlkseisdlnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2313 AKQRQENIQavpiTDSKTLKEQLAKEKKLLEEIEK-NKDKVDECQKYAKAyidiIKDYELQLVAYKAQVEPLTSPLKKtk 2391
Cdd:TIGR04523 347 LKKELTNSE----SENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQ----INDLESKIQNQEKLNQQKDEQIKK-- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2392 LDSASDNIIQEYvtlrTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIA 2471
Cdd:TIGR04523 417 LQQEKELLEKEI----ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2472 KAEKEAQELKlrmqEEVSKRETAAVDAEKQKQNIQLELHELKNlseqQIKDKSQQVDEaLKSRLrIEEEIHLIRIQLETT 2551
Cdd:TIGR04523 493 SKEKELKKLN----EEKKELEEKVKDLTKKISSLKEKIEKLES----EKKEKESKISD-LEDEL-NKDDFELKKENLEKE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2552 VKQKSNAEDELKQLRDRADAA--EKLRKLAQEEAEK--LRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLEN 2627
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKqeEKQELIDQKEKEKkdLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
570
....*....|....*
gi 1655274895 2628 LRMQAEEAERQVKQA 2642
Cdd:TIGR04523 643 LKQEVKQIKETIKEI 657
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2553-2795 |
2.48e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2553 KQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKhKSEAERKAANEKqkaledLENLRMQA 2632
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAE------LAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2633 EEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSkqmsfAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENARE 2712
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2713 EAERELEKWRQ--KANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAES 2790
Cdd:COG4942 168 ELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 1655274895 2791 TAQQK 2795
Cdd:COG4942 248 FAALK 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2801-3564 |
2.58e-08 |
|
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: 61.01 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2801 ELIRlraDFDNAEQQRS-LLEDELYRlknEVIaaQQERKQLEDELSKVRSemdILIQLKSRAEKETMSNTEKSKQLLEAE 2879
Cdd:pfam12128 123 ELGR---FMKNAGIQRTnLLNTREYR---SII--QNDRTLLGRERVELRS---LARQFALCDSESPLRHIDKIAKAMHSK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2880 ATKLRDL----AEEASKLRAIAEEAKHQRQ-----LAEEDAARqRAEAERILKEKLAAISDaTRLKTEAEIALKEKEAEN 2950
Cdd:pfam12128 192 EGKFRDVksmiVAILEDDGVVPPKSRLNRQqvehwIRDIQAIA-GIMKIRPEFTKLQQEFN-TLESAELRLSHLHFGYKS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2951 ERLRRQAEDEAYQ--RKILEDQANQHKLEIEEKIVLL---KKSSDAEMERQKAIVDDTLKQRRVVEEE-IRILKLNFEKA 3024
Cdd:pfam12128 270 DETLIASRQEERQetSAELNQLLRTLDDQWKEKRDELngeLSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3025 SSGKLDLElELNKLKNIAEETQQSklrAEEEAEKLRRLVLEEEMRrkEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKK 3104
Cdd:pfam12128 350 PSWQSELE-NLEERLKALTGKHQD---VTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3105 -ADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMqNKLKEEYEKAKALARDA--EAAKERAERE 3181
Cdd:pfam12128 424 lREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERI-ERAREEQEAANAEVERLqsELRQARKRRD 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3182 AALLRQQAEEA---ERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHkklaeqtlkq 3258
Cdd:pfam12128 503 QASEALRQASRrleERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDG---------- 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3259 kfQVEQELT--KVKLQLEETDKQKSL-LDDELQRLKDEVDDAMRQKASVEEElfkvkiQMEELMKLKVRIeeenqrlmkk 3335
Cdd:pfam12128 573 --SVGGELNlyGVKLDLKRIDVPEWAaSEEELRERLDKAEEALQSAREKQAA------AEEQLVQANGEL---------- 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3336 dkDNTQKFLVEEAENMKKLAEDAARLSIEAQeaarlrqiaeddlNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQR-QK 3414
Cdd:pfam12128 635 --EKASREETFARTALKNARLDLRRLFDEKQ-------------SEKDKKNKALAERKDSANERLNSLEAQLKQLDKkHQ 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3415 DLAQEQAQKLLEDKQLMQQrldeeteeYQRSLEAERKRQLEIIAEAeKLKLQVS---QLSEAQAKAEEEAKKFKKQADTI 3491
Cdd:pfam12128 700 AWLEEQKEQKREARTEKQA--------YWQVVEGALDAQLALLKAA-IAARRSGakaELKALETWYKRDLASLGVDPDVI 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3492 AARlhETEIATKEQ------------------MTEVKKMEFEKLNTSKEadDLRKAITELEKEKARLKKEAEEHQNKSKE 3553
Cdd:pfam12128 771 AKL--KREIRTLERkieriavrrqevlryfdwYQETWLQRRPRLATQLS--NIERAISELQQQLARLIADTKLRRAKLEM 846
|
810
....*....|.
gi 1655274895 3554 MADAQQKQIER 3564
Cdd:pfam12128 847 ERKASEKQQVR 857
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2431-3390 |
2.84e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.12 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2431 LEDEEKAAEKLKAEEQKKMAEMQAELDKQK----------QLAEAH----AKAIAKAEK--------EAQELKLRMQEEV 2488
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMARELEELSaresdleqdyQAASDHlnlvQTALRQQEKieryqedlEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2489 skRETAA---VDAEKQKQNIQLELHELKNlseqQIKDKSQQVDEaLKSRlrieeeihliRIQLETTVKQKSNAEdELKQL 2565
Cdd:COG3096 370 --VEEAAeqlAEAEARLEAAEEEVDSLKS----QLADYQQALDV-QQTR----------AIQYQQAVQALEKAR-ALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2566 RD-RADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEelkhkseaerkAANEKQKALEDLENLrmqaeeaerqvkQAEV 2644
Cdd:COG3096 432 PDlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA-----------ARRQFEKAYELVCKI------------AGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2645 EKERqiqvAHVAAQQsAAAELRSKQMsFAENVSKLEESLKqEHGTVLQLQQDAERLRKQQEDAENareeaerelekwRQK 2724
Cdd:COG3096 489 ERSQ----AWQTARE-LLRRYRSQQA-LAQRLQQLRAQLA-ELEQRLRQQQNAERLLEEFCQRIG------------QQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2725 ANEALRLRLQAEEEAHKKSLAqeeaekqkeeadrEAKKRSKAEESALKQRdmaENELERQRRLAESTAQQKLAAEQELIR 2804
Cdd:COG3096 550 DAAEELEELLAELEAQLEELE-------------EQAAEAVEQRSELRQQ---LEQLRARIKELAARAPAWLAAQDALER 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2805 LRadfdnaEQQRSLLEDelyrlKNEVIAAQQERKQLEDELSKVRSEmdiLIQLKSRAEKETmsnteksKQLLE---AEAT 2881
Cdd:COG3096 614 LR------EQSGEALAD-----SQEVTAAMQQLLEREREATVERDE---LAARKQALESQI-------ERLSQpggAEDP 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2882 KLRDLAE-----------------EASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAIS-------DATRLKT 2937
Cdd:COG3096 673 RLLALAErlggvllseiyddvtleDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2938 EAEIALKEKEAENE-RLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSdaeMERQKaivddtlkQRRVVEeeiri 3016
Cdd:COG3096 753 ELEDAVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKAS---FDVQK--------LQRLHQ----- 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3017 lklNFEKASSGKLDLELELNklkniaeetqqsklrAEEEAEKLRRlvleeemRRKEAEDKVKKIAAAEEEAARQRKAAQE 3096
Cdd:COG3096 817 ---AFSQFVGGHLAVAFAPD---------------PEAELAALRQ-------RRSELERELAQHRAQEQQLRQQLDQLKE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3097 ELDRLQKKADEVRKQKEE--ADK--EAEKQIVAAQQAAL---KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALAR 3169
Cdd:COG3096 872 QLQLLNKLLPQANLLADEtlADRleELREELDAAQEAQAfiqQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQR 951
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3170 D----AEAAKERAEREAALLRQQAEEaerqkvaaeqeaaNQAKAQDDAERLRKDAEfeaaklaqaeaaalkqkqQADEEM 3245
Cdd:COG3096 952 RlkqqIFALSEVVQRRPHFSYEDAVG-------------LLGENSDLNEKLRARLE------------------QAEEAR 1000
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3246 AKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVE-----EELFKVKIQMEELMK 3320
Cdd:COG3096 1001 REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRrdelhEELSQNRSRRSQLEK 1080
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 3321 LKVRIEEE----NQRLMKKDKDNTQkfLVEEAENMKKLAEDAARLSIEAQEAARL--RQIAEDDLNQQRTLAEKML 3390
Cdd:COG3096 1081 QLTRCEAEmdslQKRLRKAERDYKQ--EREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSADELRSMSDKAL 1154
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3043-3690 |
2.91e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3043 EETQQSKLRAEEEAEKLRRLVLEEEmRRKEAEDKVKKIAAAEEEAARQRkaAQEELDRLQKKADEVRKQKEEADKEAEKQ 3122
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3123 IVAAQQAALKCNMAEQQVQSVLAQQKEDsmmqnkLKEEyekakalARDAEAAKERAEREAALLRQQAEEAErqkvaaeqe 3202
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQ------LERE-------IERLERELEERERRRARLEALLAALG--------- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3203 aANQAKAQDDAERLRKDAEfeaaklaqaeaaalKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSL 3282
Cdd:COG4913 373 -LPLPASAEEFAALRAEAA--------------ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3283 LDDELQRLKDEVDDAMRQKasvEEELFKVKiqmeELMklKVRIEEEN-----QRLMkkdkdNTQKF--LVEEAenmkklA 3355
Cdd:COG4913 438 IPARLLALRDALAEALGLD---EAELPFVG----ELI--EVRPEEERwrgaiERVL-----GGFALtlLVPPE------H 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3356 EDAARLSIEA-QEAARLR--QIAEDDLNQQR------TLAEKM-LKE-------KMQAIQEASRLKAEAE---------- 3408
Cdd:COG4913 498 YAAALRWVNRlHLRGRLVyeRVRTGLPDPERprldpdSLAGKLdFKPhpfrawlEAELGRRFDYVCVDSPeelrrhprai 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3409 ----MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKF 3484
Cdd:COG4913 578 tragQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3485 KKQADTIAArlhETEIATKE-QMTEVKK--MEFEKLNtsKEADDLRKAITELEKEKARLKKEAEEHQnksKEMADAQQkQ 3561
Cdd:COG4913 658 WDEIDVASA---EREIAELEaELERLDAssDDLAALE--EQLEELEAELEELEEELDELKGEIGRLE---KELEQAEE-E 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3562 IEREMTVLQQtfLTEKEMLLKKEKLieDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAE 3641
Cdd:COG4913 729 LDELQDRLEA--AEDLARLELRALL--EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET 804
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3642 KDILNKQKEMQELER--KRLEQERvLADENQKLREKLQQMEEAQKSTLITE 3690
Cdd:COG4913 805 ADLDADLESLPEYLAllDRLEEDG-LPEYEERFKELLNENSIEFVADLLSK 854
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2435-2663 |
3.23e-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: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2435 EKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKREtaavdAEKQKQNIQLELHELKN 2514
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2515 LSEQQIKDKSQQvDEALKSRLRIEEEIHliriQLETTVKQKSNAEDELKQLRDRADAAEKlrklAQEEAEKLRKQVSEET 2594
Cdd:TIGR02794 124 AKAKQAAEAKAK-AEAEAERKAKEEAAK----QAEEEAKAKAAAEAKKKAEEAKKKAEAE----AKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 2595 QKKRLAEEElKHKSEAERKAANEKQKAledlenlrmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAA 2663
Cdd:TIGR02794 195 KAKAEAAKA-KAAAEAAAKAEAEAAAA---------AAAEAERKADEAELGDIFGLASGSNAEKQGGAR 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2057-2997 |
3.29e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.83 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2057 RSMEKGQQDETLCKNYISEVKDLRLRI------EDCEARTVARirKPVEKEPLKECIQKTAEQAKVQVELEGLKKDLDKV 2130
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQItskeaqLESSREIVKS--YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2131 STKTQDilnspqpsatapvLRSELEltvQKMDHAYmlssvyleklktvemvirntQGAEGVLKQYEnclrevHTVPNDVK 2210
Cdd:TIGR00606 278 KKQMEK-------------DNSELE---LKMEKVF--------------------QGTDEQLNDLY------HNHQRTVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2211 EVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSlqdrwkavftqidlrQRELD 2290
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLAT---------------RLELD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2291 QLGRQLGYYREsydwLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDiIKDYE 2370
Cdd:TIGR00606 381 GFERGPFSERQ----IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE-KKQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2371 LQLVAYKAQvepltsplkktKLDSASDNIIQEYVTLRTRYSELMTL-TSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKM 2449
Cdd:TIGR00606 456 LKFVIKELQ-----------QLEGSSDRILELDQELRKAERELSKAeKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2450 AEMQAELDKQKQLaEAHAKAIAKAEKEAQELKLRMQEEVskreTAAVDAEKQKQNIQLELHELKNlSEQQIKDKSQQVDE 2529
Cdd:TIGR00606 525 EQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSRHSDEL----TSLLGYFPNKKQLEDWLHSKSK-EINQTRDRLAKLNK 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2530 ALKSrlrIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLaQEEAEKLRKQVSEETQKKRLAE---EELKH 2606
Cdd:TIGR00606 599 ELAS---LEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERL-KEEIEKSSKQRAMLAGATAVYSqfiTQLTD 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2607 KSEA-------ERKAANEKQKALEDLENLRMQA----EEAERQVKQaeVEKERQIQVAHVAAQQS-------AAAELRSK 2668
Cdd:TIGR00606 675 ENQSccpvcqrVFQTEAELQEFISDLQSKLRLApdklKSTESELKK--KEKRRDEMLGLAPGRQSiidlkekEIPELRNK 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2669 QMSFAENVSKLEESLKQEH---GTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEA-----------LRLRLQ 2734
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQEtllGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdldrtvqqVNQEKQ 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2735 AEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQ 2814
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDS 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2815 -QRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKL 2893
Cdd:TIGR00606 913 pLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKH 992
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2894 RA-IAEEAKHQRQlaEEDAARQRaeaERILKEKLaaisdaTRLKTEAEIalkekeAENERLRRQAEDEAYQRKILEDQAN 2972
Cdd:TIGR00606 993 QEkINEDMRLMRQ--DIDTQKIQ---ERWLQDNL------TLRKRENEL------KEVEEELKQHLKEMGQMQVLQMKQE 1055
|
970 980
....*....|....*....|....*
gi 1655274895 2973 QHKLeiEEKIVLLKKSSDAEMERQK 2997
Cdd:TIGR00606 1056 HQKL--EENIDLIKRNHVLALGRQK 1078
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2841-3455 |
3.30e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2841 EDELSKVRSEMDiliQLKSR-AEKEtmsNTEKSKQLLEAEaTKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAE 2919
Cdd:PRK02224 179 ERVLSDQRGSLD---QLKAQiEEKE---EKDLHERLNGLE-SELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2920 RIlKEKLAAISDATRLKTEAEialKEKEAENERLRRQAEdeayQRKILEDQANQHKLEIEekivllkkSSDAEMERQKAI 2999
Cdd:PRK02224 252 EL-ETLEAEIEDLRETIAETE---REREELAEEVRDLRE----RLEELEEERDDLLAEAG--------LDDADAEAVEAR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3000 VDDTLKQRRVVEEEIrilklnfekassgkldlelelnklkniaEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKK 3079
Cdd:PRK02224 316 REELEDRDEELRDRL----------------------------EECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3080 IAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEAD-------------------------------KEAEKQIVAAQQ 3128
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPvdlgnaedfleelreerdelrereaeleatlRTARERVEEAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3129 --AALKCNMAEQQVqsvlaqqkEDSMMQNKLKEEYEKAKALARDAEAAK-ERAEREAALLR-QQAEEAERQkvaaeqeAA 3204
Cdd:PRK02224 448 llEAGKCPECGQPV--------EGSPHVETIEEDRERVEELEAELEDLEeEVEEVEERLERaEDLVEAEDR-------IE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3205 NQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEqtlkqkfQVEQELTKVKLQLEETDKQKSLLD 3284
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAELK 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3285 DELQRLKDEVDdamrqkasveeelfkvkiQMEELMKLKVRIEEENQRLMKKDKDNTQK--FLVEEAENMKKLAE--DAAR 3360
Cdd:PRK02224 586 ERIESLERIRT------------------LLAAIADAEDEIERLREKREALAELNDERreRLAEKRERKRELEAefDEAR 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3361 LSiEAQEAarlRQIAEDDLNQqrtLAEKM--LKEKMQAIQeaSRLKAEAEMLQRQKDLAQEQAQklLEDKQLMQQRLDEE 3438
Cdd:PRK02224 648 IE-EARED---KERAEEYLEQ---VEEKLdeLREERDDLQ--AEIGAVENELEELEELRERREA--LENRVEALEALYDE 716
|
650 660
....*....|....*....|.
gi 1655274895 3439 TEEYQ---RSLEAE-RKRQLE 3455
Cdd:PRK02224 717 AEELEsmyGDLRAElRQRNVE 737
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3062-3254 |
4.32e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3062 LVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEEldrlQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQ 3141
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK----QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3142 SVLAQQKEDsmmqNKLKEEYEKAKALARDAE--AAKERAEREAALLRQQAEEAERQKvaaeqeaANQAKAQDDAERLRKD 3219
Cdd:TIGR02794 123 EAKAKQAAE----AKAKAEAEAERKAKEEAAkqAEEEAKAKAAAEAKKKAEEAKKKA-------EAEAKAKAEAEAKAKA 191
|
170 180 190
....*....|....*....|....*....|....*
gi 1655274895 3220 AEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQ 3254
Cdd:TIGR02794 192 EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE 226
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1242-1344 |
4.34e-08 |
|
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: 54.79 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1242 QSEDMSAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLG 1319
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1655274895 1320 VTRLLDPEDVDVPHPDEKSIITYVS 1344
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2434-2671 |
4.61e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2434 EEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAhakaiakaEKEAQELKLRMQEEvskretaavdaEKQKQNIQlelhelk 2513
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQ--------ERLKQLEKERLAAQ-----------EQKKQAEE------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2514 nlSEQQIKDKSQQVDEALKSRLRieeeihliriqlettvKQKSNAEDELKQLRDRA-DAAEKLRKLAQEEAEK-----LR 2587
Cdd:PRK09510 123 --AAKQAALKQKQAEEAAAKAAA----------------AAKAKAEAEAKRAAAAAkKAAAEAKKKAEAEAAKkaaaeAK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2588 KQVSEETQKKRLAEEELKHKSEAERKAANE-KQKAledlenlrmqAEEAERQVKQAEVEKERQIQVAhvAAQQSAAAELR 2666
Cdd:PRK09510 185 KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEaKKKA----------AAEAKAAAAKAAAEAKAAAEKA--AAAKAAEKAAA 252
|
....*
gi 1655274895 2667 SKQMS 2671
Cdd:PRK09510 253 AKAAA 257
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3304-3663 |
5.16e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.78 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3304 VEEELFKVKIQMEELMKLKVRIEEENQRLMKKDkdntQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQR 3383
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKR----IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3384 TLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQR-SLEAERKRQLEIIAEAEK 3462
Cdd:pfam13868 77 ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3463 LKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLheteiATKEQMTEVKKMEFEKLNtskeaddLRKAITELE-KEKARLK 3541
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEEKEREIARL-----RAQQEKAQDEKAERDELR-------AKLYQEEQErKERQKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3542 KEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMllkKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEE 3621
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEE---FERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1655274895 3622 EKLKLKAtmdaalnkQKEAEKDILNKQKEMQELERKRLEQER 3663
Cdd:pfam13868 302 REEQRAA--------EREEELEEGERLREEEAERRERIEEER 335
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
1095-1228 |
5.28e-08 |
|
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: 55.01 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1095 SLGEPEEK--TWpNFIEDERDrvQKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVLSGDTllserDVARSVRL 1172
Cdd:cd21331 3 ALTKPENQdiDW-TLLEGETR--EERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIKVPV-----DWNKVNKP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 1173 PREKGRMRFHKLQNVQIALDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21331 73 PYPKLGANMKKLENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRY 129
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
1118-1224 |
5.64e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 53.88 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1118 KTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTLLSERDVarsvrlPREKGRMrfhkLQNVQIALDFLR 1195
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGC------PRSQSQM----IENVDVCLSFLA 72
|
90 100
....*....|....*....|....*....
gi 1655274895 1196 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21286 73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2426-2967 |
5.84e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2426 DTQRRLEdEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIA-----KAEKEAQELKLRMQEEVSKRETAAVDAEK 2500
Cdd:PRK04863 524 ELEQRLR-QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLEslsesVSEARERRMALRQQLEQLQARIQRLAARA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2501 QK-QNIQLELHELKNLSEQQIKDkSQQVDEALKSRLRIEEEIHLIRIQLETTVK----------QKSNAEDE-LKQLRDR 2568
Cdd:PRK04863 603 PAwLAAQDALARLREQSGEEFED-SQDVTEYMQQLLERERELTVERDELAARKQaldeeierlsQPGGSEDPrLNALAER 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2569 -------------------------------------ADAAEKLRKL-------------------AQEEAEKLRKQVSE 2592
Cdd:PRK04863 682 fggvllseiyddvsledapyfsalygparhaivvpdlSDAAEQLAGLedcpedlyliegdpdsfddSVFSVEELEKAVVV 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2593 ETQKK-----RLAEEELKHkseaerKAANEKQkaledLENLRMQAEEAERQVKQA--EVEK-ERQIQV--------AHVA 2656
Cdd:PRK04863 762 KIADRqwrysRFPEVPLFG------RAAREKR-----IEQLRAEREELAERYATLsfDVQKlQRLHQAfsrfigshLAVA 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2657 AQQSAAAELRSKQmsfaENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAE 2736
Cdd:PRK04863 831 FEADPEAELRQLN----RRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEA 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2737 EEA------HKKSLAQEEAEKQKEEAD-------REAKKRSKAEESALKQRDMAENELeRQRR--LAESTAQQKLAAEQE 2801
Cdd:PRK04863 907 EEAkrfvqqHGNALAQLEPIVSVLQSDpeqfeqlKQDYQQAQQTQRDAKQQAFALTEV-VQRRahFSYEDAAEMLAKNSD 985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2802 L-IRLRADFDNAEQQRSLLEDEL------YRLKNEVI--------AAQQERKQLEDELSK--VRSEMDILIQLKSRAEK- 2863
Cdd:PRK04863 986 LnEKLRQRLEQAEQERTRAREQLrqaqaqLAQYNQVLaslkssydAKRQMLQELKQELQDlgVPADSGAEERARARRDEl 1065
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2864 -ETMSNT-------EKSKQLLEAEAT----KLRDLAEEASKLRAIAEEAKHQRQLAeEDAARQRAEAERILKEKLAAISd 2931
Cdd:PRK04863 1066 hARLSANrsrrnqlEKQLTFCEAEMDnltkKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHRRELAYLS- 1143
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1655274895 2932 ATRLKTEAEI---ALKEKEAENERLR---RQAEDEAY-QRKIL 2967
Cdd:PRK04863 1144 ADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRpERKVQ 1186
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2234-2967 |
6.81e-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: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2234 DSLEEELKKASAVSdkmsrvhSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESydwlIRWIADA 2313
Cdd:COG3096 357 EELTERLEEQEEVV-------EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQA----VQALEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2314 KQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKyAKAYIDiiKDYELqlvaykaqVEPLTSPLKKTKLD 2393
Cdd:COG3096 426 RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA-ARRQFE--KAYEL--------VCKIAGEVERSQAW 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2394 SASDNIIQEYVTLRTRYSELMTLTSQYikfiTDTQRRLEdEEKAAEKLKAEEQKKMA----------EMQAELDKQK--- 2460
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQL----AELEQRLR-QQQNAERLLEEFCQRIGqqldaaeeleELLAELEAQLeel 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2461 --QLAEAHAKAIAkAEKEAQELKLRMQeEVSKRETAAVDAekqkqniQLELHELKNLSEQQIKDkSQQVDEALKSRLRIE 2538
Cdd:COG3096 570 eeQAAEAVEQRSE-LRQQLEQLRARIK-ELAARAPAWLAA-------QDALERLREQSGEALAD-SQEVTAAMQQLLERE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2539 EEIHLIRIQLETT----------VKQKSNAED-ELKQLRDR-------------------------------------AD 2570
Cdd:COG3096 640 REATVERDELAARkqalesqierLSQPGGAEDpRLLALAERlggvllseiyddvtledapyfsalygparhaivvpdlSA 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2571 AAEKLRKL-------------AQEEAEKLRkqVSEETQKK---RLAEEELKHKSEAER----KAANEKQkaledLENLRM 2630
Cdd:COG3096 720 VKEQLAGLedcpedlyliegdPDSFDDSVF--DAEELEDAvvvKLSDRQWRYSRFPEVplfgRAAREKR-----LEELRA 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2631 QAEEAERQVKQAEVEKERQIQVAH-----------VAAQQSAAAELRSKQMSFAEnvskLEESLKQEHGTVLQLQQDAER 2699
Cdd:COG3096 793 ERDELAEQYAKASFDVQKLQRLHQafsqfvgghlaVAFAPDPEAELAALRQRRSE----LERELAQHRAQEQQLRQQLDQ 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2700 LRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEA------HKKSLAQEEAEKQKEEAD-------REAKKRSKA 2766
Cdd:COG3096 869 LKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLEPLVAVLQSDpeqfeqlQADYLQAKE 948
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2767 EESALKQRDMAENELeRQRR--LAESTAQQKLAAEQELI-RLRADFDNAEQQRSLLEDELYRLKNEVI------------ 2831
Cdd:COG3096 949 QQRRLKQQIFALSEV-VQRRphFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSqynqvlaslkss 1027
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2832 --AAQQERKQLEDELS------------KVRSEMDILIQL--KSRAEKetmSNTEKSKQLLEAE----ATKLRDLAEEAS 2891
Cdd:COG3096 1028 rdAKQQTLQELEQELEelgvqadaeaeeRARIRRDELHEElsQNRSRR---SQLEKQLTRCEAEmdslQKRLRKAERDYK 1104
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2892 KLRAIAEEAK-------------------HQRQLAEEDAarqraeaerilkEKLAAISDatrlktEAEIALKEKEAENER 2952
Cdd:COG3096 1105 QEREQVVQAKagwcavlrlardndverrlHRRELAYLSA------------DELRSMSD------KALGALRLAVADNEH 1166
|
890
....*....|....*....
gi 1655274895 2953 LR---RQAEDEAY-QRKIL 2967
Cdd:COG3096 1167 LRdalRLSEDPRRpERKVQ 1185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3257-3715 |
6.83e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3257 KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEV-------DDAMRQKASVEEELFKVKIQM----EELMKLKVRI 3325
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELeklnnkyNDLKKQKEELENELNLLEKEKlniqKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3326 EEENQRLMK-KDKDNTQKFLVEEAENMKK----LAEDAARLSIEAQEAARLRQIAEDDLNQ---QRTLAEKMLKEKMQAI 3397
Cdd:TIGR04523 197 LKLELLLSNlKKKIQKNKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3398 QEASRLKAEAEmlqrqkDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEaERKRQLEI-IAEAEK----LKLQVSQLSE 3472
Cdd:TIGR04523 277 EQNNKKIKELE------KQLNQLKSEISDLNNQKEQDWNKELKSELKNQE-KKLEEIQNqISQNNKiisqLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3473 AQAKAeeeakkfkkqadtiaarlhETEIATKEQMTEVKKMEFEKLNtsKEADDLRKAITELEKEKARLKKEAEEHQNKSK 3552
Cdd:TIGR04523 350 ELTNS-------------------ESENSEKQRELEEKQNEIEKLK--KENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3553 EMaDAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKlESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA 3632
Cdd:TIGR04523 409 QK-DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ-DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3633 ALN--KQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLitEKHVTVVETVLNGQNAGDVLD 3710
Cdd:TIGR04523 487 KQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEID 564
|
....*
gi 1655274895 3711 GVEKR 3715
Cdd:TIGR04523 565 EKNKE 569
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
1108-1228 |
6.98e-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: 54.13 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1108 IEDERDRVQ--KKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTL-LSERdvarsvrlpREKGRMRFHKL 1184
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVpLHEY---------HLTPSTDDEKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655274895 1185 QNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21222 78 HNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
1109-1227 |
7.89e-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: 53.66 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1109 EDERDrvqKKTFTKWVNKHLIKSqrHVTDLYEDLRDGhnlISLLEVLsgDTLLSERDVARSVRLPREKgrMRFHKLQNVQ 1188
Cdd:cd21299 1 ETSRE---ERCFRLWINSLGIDT--YVNNVFEDVRDG---WVLLEVL--DKVSPGSVNWKHANKPPIK--MPFKKVENCN 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274895 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1227
Cdd:cd21299 69 QVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2429-2968 |
8.00e-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: 58.98 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2429 RRLEDEEKAAEKLK---AEEQKKMAEMQAELDK-QKQLAEAHAKAiaKAEKEAQELKLRMQEEVSK----RETAAVDAEK 2500
Cdd:pfam05557 27 RARIELEKKASALKrqlDRESDRNQELQKRIRLlEKREAEAEEAL--REQAELNRLKKKYLEALNKklneKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2501 QKQNIQLELHELKnlseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEdelKQLRDRADAAEKLRKLAQ 2580
Cdd:pfam05557 105 VISCLKNELSELR----RQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLE---KQQSSLAEAEQRIKELEF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2581 EEAEKLRKQVSEETQKKRLA-----EEELK-HKSEAERKAANEKQKAL--EDLENLR--------MQAEEAERQVKQAEV 2644
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSELAripelEKELErLREHNKHLNENIENKLLlkEEVEDLKrklereekYREEAATLELEKEKL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2645 EKERQiqvAHVAAQQSAAAELRS-------------KQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenar 2711
Cdd:pfam05557 258 EQELQ---SWVKLAQDTGLNLRSpedlsrrieqlqqREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK-------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2712 eeaeRELEKWRQKANEALRLRLQ-------AEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQ 2784
Cdd:pfam05557 327 ----IEDLNKKLKRHKALVRRLQrrvllltKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2785 RRLAESTA----QQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAqqERKQLEDELSKVRSEMDiliqlksR 2860
Cdd:pfam05557 403 LSVAEEELggykQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEL--ERQRLREQKNELEMELE-------R 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2861 AEKETMSNTEKSKQLleaeatKLRDlaEEASKLRAIAEEAKHQRQlAEEDAARQRAEAERILKEKLAAISDATRLKTEAE 2940
Cdd:pfam05557 474 RCLQGDYDPKKTKVL------HLSM--NPAAEAYQQRKNQLEKLQ-AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKE 544
|
570 580
....*....|....*....|....*...
gi 1655274895 2941 IALKEKEAENERLRRQAEDEAYQRKILE 2968
Cdd:pfam05557 545 VLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2758-3216 |
8.35e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 58.76 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQrdMAENELERQRRLA--ESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQ 2835
Cdd:COG5278 82 EEARAEIDELLAELRS--LTADNPEQQARLDelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2836 ERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQR 2915
Cdd:COG5278 160 LLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2916 AEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMER 2995
Cdd:COG5278 240 LALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2996 QKAIVDDTLKQRRVVEEEIRIlklnfekassgkLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAED 3075
Cdd:COG5278 320 AAAAALAALLALALATALAAA------------AAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEA 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3076 KVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQN 3155
Cdd:COG5278 388 VELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3156 KLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERL 3216
Cdd:COG5278 468 LAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2209-2644 |
9.19e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2209 VKEVETYRTNLKKMRAE-AEAEQPVFDSLEEELKKASAVSDKMSRVHSERdaelDQHRQHLSSLQDRWKAVFTQIDLRQR 2287
Cdd:pfam15921 316 MRQLSDLESTVSQLRSElREAKRMYEDKIEELEKQLVLANSELTEARTER----DQFSQESGNLDDQLQKLLADLHKREK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2288 ELDQLGRQLGYYRE-------SYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAK 2360
Cdd:pfam15921 392 ELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2361 AYIDIIKDYELQLVAYKAQVEP-------LTSPLKKTKLDSASDNiiQEYVTLRTRYsELMTLTSQYIKFITDTQRRLED 2433
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESsertvsdLTASLQEKERAIEATN--AEITKLRSRV-DLKLQELQHLKNEGDHLRNVQT 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2434 EEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAI-------AKAEKEAQELKLRMQE---EVSKRETAAVDAEKQKQ 2503
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVS 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2504 NIQLELHELKNLSEQQ---IKDKSQQVDEAL------KSRLR-IEEEIHLIRI-------QLETTVK----QKSNAEDEL 2562
Cdd:pfam15921 629 DLELEKVKLVNAGSERlraVKDIKQERDQLLnevktsRNELNsLSEDYEVLKRnfrnkseEMETTTNklkmQLKSAQSEL 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2563 KQLRDRADAAEKLRKLAQEEAEKLRKQVSEE---------------------TQKKRLAEEELKHKSEAERKAANEKQKA 2621
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqidalqskiqfleeamtnaNKEKHFLKEEKNKLSQELSTVATEKNKM 788
|
490 500
....*....|....*....|...
gi 1655274895 2622 LEDLENLRMQAEEAERQVKQAEV 2644
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANMEV 811
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2629-3118 |
9.42e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2629 RMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAE 2708
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2709 NAREEAEreleKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLA 2788
Cdd:PRK02224 255 TLEAEIE----DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2789 ESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDIL--------IQLKSR 2860
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELrerfgdapVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2861 AE-----KETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIA---------EEAKHQRQLAEEDAARQRAEAERilkEKL 2926
Cdd:PRK02224 411 EDfleelREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvEGSPHVETIEEDRERVEELEAEL---EDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2927 AAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEkivLLKKSSDAEMERQKAIVDDTLKQ 3006
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE---LRERAAELEAEAEEKREAAAEAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3007 RRVVEEEIRILKLNFEKASsgkLDLELE-LNKLKNIAEETQQSKLRAEEEAEKL---------RRLVLEEEM-RRKEAED 3075
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAE---LKERIEsLERIRTLLAAIADAEDEIERLREKRealaelndeRRERLAEKReRKRELEA 641
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1655274895 3076 KVKKIAAAEEEAARQRkaAQEELDRLQKKADEVRKQKEEADKE 3118
Cdd:PRK02224 642 EFDEARIEEAREDKER--AEEYLEQVEEKLDELREERDDLQAE 682
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5105-5141 |
9.77e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 9.77e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1655274895 5105 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEM 5141
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2329-2980 |
1.22e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2329 KTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQvepltsplkKTKLDSASDNIIQEYVTLRT 2408
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE---------KLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2409 RYSELMTLTSQYiKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAhakaIAKAEKEAQELKlRMQEE 2487
Cdd:TIGR04523 202 LLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtQTQLNQL----KDEQNKIKKQLS-EKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2488 VSKRETAAVDAEKQKQNIQLELHELKNlseqqikDKSQQVDEALKSRLRIEEEihliriQLETTVKQKSNAEDELKQLrd 2567
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNN-------QKEQDWNKELKSELKNQEK------KLEEIQNQISQNNKIISQL-- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2568 radaaeklrklaQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQV-KQAEVEK 2646
Cdd:TIGR04523 341 ------------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2647 ERQIQVahvaaqqsaaaelrskqmsfaenvskleESLKQEHgtvLQLQQDAERLRKQqedaenareeaerelekwRQKAN 2726
Cdd:TIGR04523 409 QKDEQI----------------------------KKLQQEK---ELLEKEIERLKET------------------IIKNN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2727 EALRlRLQAEEEAHKKSLaqeeaekqkeeadREAKKRSKAEESALKqrdmaenELERQRRLAESTAQQKlaaEQELIRLR 2806
Cdd:TIGR04523 440 SEIK-DLTNQDSVKELII-------------KNLDNTRESLETQLK-------VLSRSINKIKQNLEQK---QKELKSKE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2807 ADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDiliQLKSRAEKEtmsNTEKSKQLLEAEatkLRDL 2886
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS---DLEDELNKD---DFELKKENLEKE---IDEK 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2887 AEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIAlkekEAENERLRRQAEDEAYQRKI 2966
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA----KKENEKLSSIIKNIKSKKNK 642
|
650
....*....|....
gi 1655274895 2967 LEDQANQHKLEIEE 2980
Cdd:TIGR04523 643 LKQEVKQIKETIKE 656
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2434-2616 |
1.62e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 57.71 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2434 EEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELK 2513
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2514 NlSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQ--LETTVKQKSNAEDELKQlrdRADAAEKLRKLAQEEAEKLRKQVS 2591
Cdd:pfam05262 259 N-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKknDEEALKAKDHKAFDLKQ---ESKASEKEAEDKELEAQKKREPVA 334
|
170 180
....*....|....*....|....*.
gi 1655274895 2592 EETQK-KRLAEEELKHKSEAERKAAN 2616
Cdd:pfam05262 335 EDLQKtKPQVEAQPTSLNEDAIDSSN 360
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3392-3685 |
1.65e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3392 EKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKqlmqqrldEETEEYQRSLEAERKRQL-EIIAEAEKLKLQVSQL 3470
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER--------EKAERYQALLKEKREYEGyELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3471 SEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMefeklnTSKEADDLRKAITELEKEKARLKKEAEEHQNK 3550
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3551 SKEMADAQQK-QIEREMTVLQQTFLTEK--EMLLKKEKLIE------DEKKKLESQFEEEIKKAKALKDEQDRQRQQME- 3620
Cdd:TIGR02169 317 LEDAEERLAKlEAEIDKLLAEIEELEREieEERKRRDKLTEeyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEk 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3621 --EEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLE--------QERVLADEnQKLREKLQQMEEAQKS 3685
Cdd:TIGR02169 397 lkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEleeekedkALEIKKQE-WKLEQLAADLSKYEQE 470
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
1247-1349 |
1.65e-07 |
|
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: 52.77 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1247 SAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1655274895 1326 PEDVDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3376-3650 |
1.80e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.46 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3376 EDDLNQQRTLAEKMLKEKMQAIQEasrLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSleaeRKRQLE 3455
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDE---LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL----KEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3456 IIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAA--RLHETEIATKEQ----MTEVKKMEfEKLNTSKEADDLRKA 3529
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERleWRQQTEVLSPEEekelVEKIKELE-KELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3530 ITELEKEKARLKKEAEEHQNKSKEMADAQQKqieremTVLQQTFLTEKEMLLKKEkliEDEKKKlesQFEEEIKKAKALK 3609
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQE------LHEEMIELYKEADELRKE---ADELHK---EIVEAQEKADELH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1655274895 3610 DEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE 3650
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2994-3680 |
1.91e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2994 ERQKAIvDDTLKQRRVveEEIRilklnfEKASSGKLDLELELNKLKNIAEETQqSKLRAEEEAEKLRRLVlEEEMRRKEA 3073
Cdd:PRK02224 150 DRQDMI-DDLLQLGKL--EEYR------ERASDARLGVERVLSDQRGSLDQLK-AQIEEKEEKDLHERLN-GLESELAEL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3074 EDKVKKIAAAEEEAARQRKAA----------QEELDRLQKKADEVRKQKEEADKEAEkqivaaqqaALKCNMAEQQVQsv 3143
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEAdevleeheerREELETLEAEIEDLRETIAETERERE---------ELAEEVRDLRER-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3144 laqqkedsmmqnklKEEYEKAKALARdAEAAKERAEREAALLRQQAEEAERQKVAA--EQEAANQAKAQDDAERLRKDAE 3221
Cdd:PRK02224 288 --------------LEELEEERDDLL-AEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQAHNEEAESLREDAD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3222 feaaklaqaeaaalkqkqqADEEMAKHKKLAEQTLkqkfqvEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQK 3301
Cdd:PRK02224 353 -------------------DLEERAEELREEAAEL------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3302 ASVEEELFKVKIQMEEL----MKLKVRIE------EENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARL 3371
Cdd:PRK02224 408 GNAEDFLEELREERDELrereAELEATLRtarervEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3372 RQIAEDdlnqqrtlaekmLKEKMQAIQEASRLKAEAEMLQRQKDLAQEqaqkLLEDKQlmqqrldEETEEYQRSLEAERK 3451
Cdd:PRK02224 488 EEEVEE------------VEERLERAEDLVEAEDRIERLEERREDLEE----LIAERR-------ETIEEKRERAEELRE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3452 RQLEIIAEAEklklqvsQLSEAQAKAeeeakkfkkqadtiaarlhetEIATKEQMTEVKKMEfEKLNTSKEADDLRKAIT 3531
Cdd:PRK02224 545 RAAELEAEAE-------EKREAAAEA---------------------EEEAEEAREEVAELN-SKLAELKERIESLERIR 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3532 ELEKEKARLKKEAEEHQNKSKEMADAQQKQIERemtvlqqtfLTEKemllkkekliEDEKKKLESQFEEE-IKKAKALKD 3610
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELNDERRER---------LAEK----------RERKRELEAEFDEArIEEAREDKE 656
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3611 EQDRQRQQMEEEKlklkatmdaalnKQKEAEKDILNKQKEMQELERKRLEQervLADENQKLREKLQQME 3680
Cdd:PRK02224 657 RAEEYLEQVEEKL------------DELREERDDLQAEIGAVENELEELEE---LRERREALENRVEALE 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3458-3668 |
1.93e-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: 57.08 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3458 AEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEfeklntsKEADDLRKAITELEKEK 3537
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3538 ARLKKEAEEHQNKSKEMADAQQK-----------------QIEREMTVLQQtFLTEKEMLLKKEKLIEDEKKKLESQFEE 3600
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRlgrqpplalllspedflDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3601 EIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELER--KRLEQERVLADE 3668
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2074-2594 |
1.94e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2074 SEVKDLRLRIEDCEARTVARIRK-PVEKEPLKECIQKtaeQAKVQVELEGLKKDLDKvSTKTQDILNSPQPSATAPV--L 2150
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKtKLQDENLKELIEK---KDHLTKELEDIKMSLQR-SMSTQKALEEDLQIATKTIcqL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2151 RSELELTVQKMDHAYMLSSVYLEKLKTVEMVIrntqgaegvlkqyENCLR-EVHTVPNDVKEVETYRTNLKKMRAEAEAE 2229
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSL-------------EELLRtEQQRLEKNEDQLKIITMELQKKSSELEEM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2230 QPVFDSLEEELkkasavsDKMSRVHSERDAELDQHRQH---LSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWL 2306
Cdd:pfam05483 397 TKFKNNKEVEL-------EELKKILAEDEKLLDEKKQFekiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2307 IRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEE-------IEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQ 2379
Cdd:pfam05483 470 LKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtleLKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2380 VEPLTSPLK------KTKLDSASDN---IIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLED---EEKAAEKLKAEEQK 2447
Cdd:pfam05483 550 LESVREEFIqkgdevKCKLDKSEENarsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElhqENKALKKKGSAENK 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2448 KMAEMQAELDK-QKQLAEAHAK---AIAKAEKEAQELKL---RMQEEVSKRETAAVDAEKQKQNIQLEL-HELKNLSEQQ 2519
Cdd:pfam05483 630 QLNAYEIKVNKlELELASAKQKfeeIIDNYQKEIEDKKIseeKLLEEVEKAKAIADEAVKLQKEIDKRCqHKIAEMVALM 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 2520 IKDKsQQVDEALKSRlriEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEET 2594
Cdd:pfam05483 710 EKHK-HQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3317-3681 |
2.01e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3317 ELMKLKVRIEEENQRLMkkdkdNTQKFLVEEAENMKKLAED----AARLSIeAQEAARLR-QI--AEDDLNQqrtlAEKM 3389
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLEE----LEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3390 LKEKMQAIQEASRlkaEAEMLQRQKDLAQEQAQKLleDKQL--MQQRLDEETE---EYQRSLEA-ERKRQLeiiaeaekl 3463
Cdd:PRK04863 364 LEEQNEVVEEADE---QQEENEARAEAAEEEVDEL--KSQLadYQQALDVQQTraiQYQQAVQAlERAKQL--------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3464 kLQVSQLSeaqakaeeeakkfkkqADTIAARLHETEIATKEQMTEVKKMEfEKLNTSKEADD--------LRKAITELEK 3535
Cdd:PRK04863 430 -CGLPDLT----------------ADNAEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSqfeqayqlVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3536 EKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTF---------LTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAK 3606
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLrqqqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3607 ALKDEQDRQRQQMEEEKLKLKA-------------TMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLR 3673
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQAriqrlaarapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
....*...
gi 1655274895 3674 EKLQQMEE 3681
Cdd:PRK04863 652 ARKQALDE 659
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2769-2973 |
2.04e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2769 SALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSK-- 2846
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2847 --------VRSEMDILIQLKSRAEkeTMSNTEKSKQLLEAEatklRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEA 2918
Cdd:COG3883 93 ralyrsggSVSYLDVLLGSESFSD--FLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 2919 ERILKEKLAAISDATRLKteAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQ 2973
Cdd:COG3883 167 EAAKAELEAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3352-3684 |
2.19e-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: 56.47 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3352 KKLAEDAARLSIEAQEAARLRQIAEDDlnQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLM 3431
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3432 QQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKK 3511
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3512 MEFEKLNTSKEADDLRKAitelEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFltEKEMLLKKEKLIEDek 3591
Cdd:pfam13868 184 REIARLRAQQEKAQDEKA----ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR--EEQIELKERRLAEE-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3592 KKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKlkatmdaalnKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK 3671
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL----------EHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
330
....*....|...
gi 1655274895 3672 LREKLQQMEEAQK 3684
Cdd:pfam13868 326 ERRERIEEERQKK 338
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2825-3571 |
2.27e-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: 57.72 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2825 RLKNEVIAAQQERKQLEDELSKVRSEM--------DILIQLKSRAEKETMSNTE------KSKQL---LEAEATKLRDLA 2887
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELknkekelkNLDKNLNKDEEKINNSNNKikileqQIKDLndkLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2888 EEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEaeiaLKEKEAENERLRRQAEDEAYQRKIL 2967
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2968 EDQanqhKLEIEEKIvllkkssdaemerqkaivDDTLKQRRVVEEEIRILKLNFEKASSgkldLELELNKLKNiaeetQQ 3047
Cdd:TIGR04523 179 EKE----KLNIQKNI------------------DKIKNKLLKLELLLSNLKKKIQKNKS----LESQISELKK-----QN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3048 SKLraEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAE---KQIV 3124
Cdd:TIGR04523 228 NQL--KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnNQKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3125 AAQQAALKCNMAEQQVQSVLAQQKEDSMMQ--NKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQE 3202
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3203 AANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEmakHKKLAEQTLKQKFQV---EQELTKVKLQLEETDKQ 3279
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE---IERLKETIIKNNSEIkdlTNQDSVKELIIKNLDNT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3280 KSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKdkdntQKFLVEEAENMKKLaedaa 3359
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK-----ISSLKEKIEKLESE----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3360 RLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEasrLKAEAEMLQRqkdlAQEQAQKLLEDKQLMQQRLDEET 3439
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKK----KQEEKQELIDQKEKEKKDLIKEI 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3440 EEYQRSLEaERKRQLEII-AEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVkkmefekln 3518
Cdd:TIGR04523 606 EEKEKKIS-SLEKELEKAkKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI--------- 675
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3519 tskeaDDLRKAITELEKEK-ARLKKEAEEH-QNKSKEMADAQQKQIEREMTVLQQ 3571
Cdd:TIGR04523 676 -----DDIIELMKDWLKELsLHYKKYITRMiRIKDLPKLEEKYKEIEKELKKLDE 725
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3037-3214 |
2.47e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3037 KLKNIAEETQQSKLRAEEEAEKLRRLVLEEEmRRKEAEDKVKKIAAAEEEAARQRKA---AQEELDRLQKKADEVRKQKE 3113
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEKE-RLAAQEQKKQAEEAAKQAALKQKQAeeaAAKAAAAAKAKAEAEAKRAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3114 EADK--EAEKQIVAAQQAALKcnmAEQQvqsvlAQQKEDSMMQNKLKEEYEK---AKALARDAEAAKERAEREAALLRQQ 3188
Cdd:PRK09510 158 AAAKkaAAEAKKKAEAEAAKK---AAAE-----AKKKAEAEAAAKAAAEAKKkaeAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
170 180
....*....|....*....|....*.
gi 1655274895 3189 AEEAERQKVAAEQEAANQAKAQDDAE 3214
Cdd:PRK09510 230 AAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2885-3122 |
2.77e-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: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2885 DLAEEASKLRAIAEEAKHQRQLAEEdAARQRAEAERILKEKLAAISDATRL--KTEAEIALKEKEAE--NERLRRQAEDE 2960
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2961 AYQRKILEDQ-ANQHKLEIEEKIVLLKKSSDA-EMERQKAIVDDTLKQRRVveeeirilklnfekassgkldlelELNKL 3038
Cdd:COG4942 100 EAQKEELAELlRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARRE------------------------QAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3039 KNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKE 3118
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....
gi 1655274895 3119 AEKQ 3122
Cdd:COG4942 236 AAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3263-3683 |
3.49e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3263 EQELTKVKLQLEETDKQKslldDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQK 3342
Cdd:PRK02224 212 ESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3343 FLVEEAENMKKLAE-DAARLSIEAQEAARlrqiaeDDLNQQRTLAEKMLKEKMQAIQEAsrlKAEAEMLQRQKDLAQEQA 3421
Cdd:PRK02224 288 LEELEEERDDLLAEaGLDDADAEAVEARR------EELEDRDEELRDRLEECRVAAQAH---NEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3422 QKLLEDKQlmqqRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETE-- 3499
Cdd:PRK02224 359 EELREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEat 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3500 -------IATKEQMTEVKK-----MEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAqqKQIEREMT 3567
Cdd:PRK02224 435 lrtarerVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3568 VLQQTFLTEKEMLLKKEKLIE----------DEKKKLESQFEEEIKKAKALKDEQDRQRQQ---MEEEKLKLKATMDAaL 3634
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEekreraeelrERAAELEAEAEEKREAAAEAEEEAEEAREEvaeLNSKLAELKERIES-L 591
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3635 NKQKEAEKDILNKQKEMQEL----------------------ERKRLEQERVLADENQKLREKLQQMEEAQ 3683
Cdd:PRK02224 592 ERIRTLLAAIADAEDEIERLrekrealaelnderrerlaekrERKRELEAEFDEARIEEAREDKERAEEYL 662
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3259-3689 |
3.72e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.16 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3259 KFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEE-LFKVKIQMEELMKLKVRIEEENQR---LMK 3334
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3335 KDKDNTQKFLVEEA----ENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRT-LAEKMLKEKMQAIQEASRLKAEAEM 3409
Cdd:pfam12128 369 KHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESeLREQLEAGKLEFNEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3410 LQRQKDLAQeqaqklLEDKQLMQQRL-DEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEaqakaeeeakkfkkqa 3488
Cdd:pfam12128 449 LKLRLNQAT------ATPELLLQLENfDERIERAREEQEAANAEVERLQSELRQARKRRDQASE---------------- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3489 dtiaaRLHETEIATKEQMT---EVKKMEFEKLNT-----SKEADDLRKAI-----------TELEKEK------------ 3537
Cdd:pfam12128 507 -----ALRQASRRLEERQSaldELELQLFPQAGTllhflRKEAPDWEQSIgkvispellhrTDLDPEVwdgsvggelnly 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3538 -ARLKKEAEEHqnksKEMADAQQkQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQR 3616
Cdd:pfam12128 582 gVKLDLKRIDV----PEWAASEE-ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLR 656
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3617 QqmeeeklklkatmdaaLNKQKEAEKDILNKQKEmqelERKRLEQERV--LADENQKLREKLQQMEEAQKSTLIT 3689
Cdd:pfam12128 657 R----------------LFDEKQSEKDKKNKALA----ERKDSANERLnsLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3238-3684 |
3.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3238 KQQADEEMAKHKKLAEQTLKQKfQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEE 3317
Cdd:COG4717 93 LQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3318 LMKLKVRIEEENQRLmkkdkdntqkfLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRtlaekmlkekmqai 3397
Cdd:COG4717 172 LAELQEELEELLEQL-----------SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE-------------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3398 QEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLmqqrldeeteeyqrSLEAERKRQLEIIAE-AEKLKLQVSQLSEAQAK 3476
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALL--------------ALLGLGGSLLSLILTiAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3477 AEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEhqnkskemad 3556
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE---------- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3557 AQQKQIEREMT-VLQQTFLTEKEMLLKKEKL------IEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKlkat 3629
Cdd:COG4717 363 LQLEELEQEIAaLLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALDEEELEEELEELE---- 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 3630 mdaalNKQKEAEKDILNKQKEMQELER--KRLEQERVLADENQKLREKLQQMEEAQK 3684
Cdd:COG4717 439 -----EELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAE 490
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2980-3685 |
4.02e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.16 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2980 EKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILK-----------------------LNFEKASSGKLDLELELN 3036
Cdd:pfam12128 182 DKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRqqvehwirdiqaiagimkirpefTKLQQEFNTLESAELRLS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3037 KLK-NIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLqkkaDEVRKQKEEA 3115
Cdd:pfam12128 262 HLHfGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL----EDQHGAFLDA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3116 DKEAEKQivAAQQAALKCNMAEQQVQSVLAQQKEdsmmQNKLKEEYEKAKA-----LARDAEAAKERAE--REAALLRQQ 3188
Cdd:pfam12128 338 DIETAAA--DQEQLPSWQSELENLEERLKALTGK----HQDVTAKYNRRRSkikeqNNRDIAGIKDKLAkiREARDRQLA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3189 AEEAERQKVAA---EQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaalKQKQQADEEMAkhkklAEQTLKQKFQVEQE 3265
Cdd:pfam12128 412 VAEDDLQALESelrEQLEAGKLEFNEEEYRLKSRLG--------------ELKLRLNQATA-----TPELLLQLENFDER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3266 LTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKD----KDNTQ 3341
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEapdwEQSIG 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3342 KFL-------------VEEAENMKKLAEDAARLSIEA----------QEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQ 3398
Cdd:pfam12128 553 KVIspellhrtdldpeVWDGSVGGELNLYGVKLDLKRidvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANG 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3399 EASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEaERKRQLEiiAEAEKLKLQVSQLSEaqakae 3478
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQLKQLDKKHQAWLE------ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3479 eeakkfkkqadtiaarlheteiATKEQMTEvkkmefeklNTSKEADDLRKAITELEKEKARLKKEAEehqnKSKEMADAQ 3558
Cdd:pfam12128 704 ----------------------EQKEQKRE---------ARTEKQAYWQVVEGALDAQLALLKAAIA----ARRSGAKAE 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3559 QKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE--SQFEEEIKKAkalkdeQDRQRQQMEEEKLKLKATMDAALNK 3636
Cdd:pfam12128 749 LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIEriAVRRQEVLRY------FDWYQETWLQRRPRLATQLSNIERA 822
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3637 QKEAEKDiLNKQKEMQELERKRLEQER-------VLADEN-QKLR---EKLQQMEEAQKS 3685
Cdd:pfam12128 823 ISELQQQ-LARLIADTKLRRAKLEMERkasekqqVRLSENlRGLRcemSKLATLKEDANS 881
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3089-3285 |
4.10e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3089 RQRKAAQEELDRLQKKADEVRKQKE------EADKEAEKQIVAAQQAalkcnmAEQQVQSVLAQQKEDSMMQNKLKEEYE 3162
Cdd:PRK09510 81 RKKKEQQQAEELQQKQAAEQERLKQlekerlAAQEQKKQAEEAAKQA------ALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3163 KAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaalKQKQQAD 3242
Cdd:PRK09510 155 RAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA--------------EAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655274895 3243 EEMAKHKKLAEQtlKQKFQVEQELTKVKLQLEETDKQKSLLDD 3285
Cdd:PRK09510 221 AEAKAAAAKAAA--EAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
1242-1349 |
4.42e-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: 51.63 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1242 QSEDMSAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLGV 1320
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1655274895 1321 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2564-2801 |
4.92e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2564 QLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRlaeeelkhKSEAERKAANEKQKaledlenlrmQAEEAERQVKQAE 2643
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLK--------QLEKERLAAQEQKK----------QAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2644 VEKERQIQVAHVAAQQSAAAElrskQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAenareeaerelekwrq 2723
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAE----AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEA---------------- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2724 KANEALRLRLQAEEEAHKKSlaqeeaekqkeeaDREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQE 2801
Cdd:PRK09510 192 AAKAAAEAKKKAEAEAKKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2993-3593 |
5.14e-07 |
|
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: 56.68 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2993 MERQKAIVDDTLKQRRVVEEEIRILKlnfekassgkldlelelnklkniaEETQQSKLRAEEEAEKLRRLVLEEEMRRKE 3072
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLR------------------------ETSLQQKMRLEAQAMELDALAVAEKAGQAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3073 AEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQA------ALKCNMAEQQVQSVLAq 3146
Cdd:pfam07111 117 AEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGlekslnSLETKRAGEAKQLAEA- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3147 QKEDSMMQNKLKEEYEKAKALARDAEAAKER-AEREAALLRQQAEEAERQKVAAEQEAANQAKA--QDDAERLRKDAEFE 3223
Cdd:pfam07111 196 QKEAELLRKQLSKTQEELEAQVTLVESLRKYvGEQVPPEVHSQTWELERQELLDTMQHLQEDRAdlQATVELLQVRVQSL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3224 AAKLAQAEAAALKQKQQAD----EEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQkslLDDELQRLKDEVDDAMR 3299
Cdd:pfam07111 276 THMLALQEEELTRKIQPSDslepEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQ---LRGQVAELQEQVTSQSQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3300 QKASVEEELFKVKIQME------ELMKLKVRIEEENQRLMKKDKDNTQ---KFLVEEAEN--------MKKLAEDAAR-- 3360
Cdd:pfam07111 353 EQAILQRALQDKAAEVEvermsaKGLQMELSRAQEARRRQQQQTASAEeqlKFVVNAMSStqiwlettMTRVEQAVARip 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3361 -LSIEAQEAAR---------LRQIAEDDLNQQRT--------LAEKMLKEKMQAIQEASRLKAE----AEMLQRQKDLAQ 3418
Cdd:pfam07111 433 sLSNRLSYAVRkvhtikglmARKVALAQLRQESCpppppappVDADLSLELEQLREERNRLDAElqlsAHLIQQEVGRAR 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3419 EQAQklLEDKQLMQ--QRLDEETEEYQRS-------LEAERKRQLEIIAEAEKLKLQVSQlseaqakaeeeakKFKKQAD 3489
Cdd:pfam07111 513 EQGE--AERQQLSEvaQQLEQELQRAQESlasvgqqLEVARQGQQESTEEAASLRQELTQ-------------QQEIYGQ 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3490 TIAARLHETEIATKEQMTEVKKmefeKLNTSKEadDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVL 3569
Cdd:pfam07111 578 ALQEKVAEVETRLREQLSDTKR----RLNEARR--EQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRV 651
|
650 660
....*....|....*....|....*.
gi 1655274895 3570 QQTFLTEKEML--LKKEKLIEDEKKK 3593
Cdd:pfam07111 652 QELERDKNLMLatLQQEGLLSRYKQQ 677
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
3274-3642 |
5.32e-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: 56.56 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3274 EETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVK---IQMEELMKLKVRIEEENQRLMKKDKDNT----QKFLVE 3346
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKlsdIKTEYLYELNVLKEKSEAELTSKTKKELdaafEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3347 EAENMKKLAEdAARLSIEAQEAARLRQiaEDDLNQQRTLAEKMLKEKmqaIQEASRLKAEAEMlqrqkDLAQEQAQKLLE 3426
Cdd:NF033838 134 TLEPGKKVAE-ATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELE---IAESDVEVKKAEL-----ELVKEEAKEPRD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3427 DKQLMQQRLDEETEEyqrsleAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETeiATKEQM 3506
Cdd:NF033838 203 EEKIKQAKAKVESKK------AEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG--VLGEPA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3507 TEVKKMEFEKLNTSKEADDL--------RKAITELEKEKARLKKEAEEHQNKSKE-MADAQQKQIEREMTVLQQTfLTEK 3577
Cdd:NF033838 275 TPDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVEEAKKKAKDQKEEDRRnYPTNTYKTLELEIAESDVK-VKEA 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 3578 EMLLKKE--KLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALnKQKEAEK 3642
Cdd:NF033838 354 ELELVKEeaKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKV-KEKPAEQ 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3236-3452 |
5.62e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3236 KQKQ----QADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKV 3311
Cdd:COG4942 23 AEAEaeleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3312 KIQMEELMKLKVRIEEENQRLMKKDKDNTQKFlVEEAENMKKLAE-DAARLSIEAQEAARLRQIaEDDLNQQRTLAEKML 3390
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPaRREQAEELRADLAELAAL-RAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3391 KEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKR 3452
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3508-3686 |
5.72e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3508 EVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQ-------QTFLTEKEML 3580
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3581 lkkEKLIEDEKKKLESQfeeeikkaKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLE 3660
Cdd:COG3883 125 ---SKIADADADLLEEL--------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
170 180
....*....|....*....|....*.
gi 1655274895 3661 QERVLADENQKLREKLQQMEEAQKST 3686
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2892-3684 |
6.24e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.59 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2892 KLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIAlKEKEAENERLRRQaedeayQRKILEDQA 2971
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKNR------LKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2972 NQHKLEIEekivlLKKSSDAEMERQKAIVDDTLKQRRV---VEEEIRILKLNfeKASSGKLDLELELNKLKNIAEETQQS 3048
Cdd:TIGR00606 263 KIMKLDNE-----IKALKSRKKQMEKDNSELELKMEKVfqgTDEQLNDLYHN--HQRTVREKERELVDCQRELEKLNKER 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3049 KLRAEEEAEklrrlvLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 3128
Cdd:TIGR00606 336 RLLNQEKTE------LLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3129 AALkcNMAEQQVQSVLAQQKEDSMMQNKlkeeyekaKALARDAEAAKERAEREAALLR---QQAEEAERQKVAAEQEAAN 3205
Cdd:TIGR00606 410 AAQ--LCADLQSKERLKQEQADEIRDEK--------KGLGRTIELKKEILEKKQEELKfviKELQQLEGSSDRILELDQE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3206 QAKAQDDAERLRKDAEFEAAKLAQAEAAALK-----QKQQADEEMAK---HKKLAEQTL---KQKFQVEQELTKVKLQle 3274
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQNEKadldrKLRKLDQEMEQlnhHTTTRTQMEmltKDKMDKDEQIRKIKSR-- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3275 ETDKQKSLLDD--ELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLveEAENMK 3352
Cdd:TIGR00606 558 HSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF--DVCGSQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3353 KLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASR-LKAEAEMLQRQKDLaqEQAQKLLEDKQlm 3431
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDL--QSKLRLAPDKL-- 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3432 qqrldEETEEYQRSLEAERKRQLEII-AEAEKLKLQVSQLSEAQAKAEEEakkfkkqadtiaarlhETEIATKEQMTEVK 3510
Cdd:TIGR00606 712 -----KSTESELKKKEKRRDEMLGLApGRQSIIDLKEKEIPELRNKLQKV----------------NRDIQRLKNDIEEQ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3511 KMEFEKLNTSKE-ADDLRKAITELEkekaRLKKEAEEHQNK-SKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIE 3588
Cdd:TIGR00606 771 ETLLGTIMPEEEsAKVCLTDVTIME----RFQMELKDVERKiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3589 DEKKKLESQFEE---------EIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRL 3659
Cdd:TIGR00606 847 LNRKLIQDQQEQiqhlksktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810 820
....*....|....*....|....*
gi 1655274895 3660 EQERVLADENQKLREKLQQMEEAQK 3684
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVK 951
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1706-1798 |
6.45e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.79 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1706 HAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFTA 1785
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1655274895 1786 ALQTQWSWILQLC 1798
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2426-2646 |
7.44e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.85 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2426 DTQRRLEDEEKAAEKLKAEEQKKMAEM--QAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAvdAEKQKQ 2503
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2504 NiqlelhELKNLSEQQIKDKSQQvdealksrlrieeeihliriqlettVKQKSNAEDELKQLRDRADAAEKLRKLAQEE- 2582
Cdd:TIGR02794 146 E------EAAKQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 2583 ---AEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDL--ENLRMQAEEAERQVKQAEVEK 2646
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2827-3220 |
7.77e-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: 55.80 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2827 KNEVIAAQQERKQLEDELSKVRSEMdiliqlksraeketmsnTEKSKQLLEAEATKLRDLAEEASKLRAIaEEAKH--QR 2904
Cdd:pfam05701 27 KAHRIQTVERRKLVELELEKVQEEI-----------------PEYKKQSEAAEAAKAQVLEELESTKRLI-EELKLnlER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2905 QLAEEDAARQRAE-AERILKEKLAAISDatrlktEAEIALKEK-EAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKI 2982
Cdd:pfam05701 89 AQTEEAQAKQDSElAKLRVEEMEQGIAD------EASVAAKAQlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2983 VLLKKSSDAEMERQKAivddtlkQRRVVEEEIRILKLNFEKASSGKLDLELELNKLkNIAEETQQSKLR-------AEEE 3055
Cdd:pfam05701 163 IAIKRAEEAVSASKEI-------EKTVEELTIELIATKESLESAHAAHLEAEEHRI-GAALAREQDKLNwekelkqAEEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3056 AEKLR-RLVLEEEMRRK-----------------EAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADK 3117
Cdd:pfam05701 235 LQRLNqQLLSAKDLKSKletasallldlkaelaaYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3118 EAEKQIVAAqqAALKCNMAEQQVQSVLAQQKED--SMMQNKLKEEYEKAK---ALARDAE-AAKERAEREAALLRQQAEE 3191
Cdd:pfam05701 315 EVNCLRVAA--ASLRSELEKEKAELASLRQREGmaSIAVSSLEAELNRTKseiALVQAKEkEAREKMVELPKQLQQAAQE 392
|
410 420
....*....|....*....|....*....
gi 1655274895 3192 AERQKVAAEQEAANQAKAQDDAERLRKDA 3220
Cdd:pfam05701 393 AEEAKSLAQAAREELRKAKEEAEQAKAAA 421
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3521-3691 |
7.93e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3521 KEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEE 3600
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3601 EIKKAKALKdEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNK-QKEMQELERKRLEQERVLADENQKLREKLQQM 3679
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|..
gi 1655274895 3680 EEAQKSTLITEK 3691
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2788-3002 |
8.39e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.80 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2788 AESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEViaaqqerKQLEDELSKVRSEMDILIQLKSRAEK---- 2863
Cdd:pfam05667 323 VETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNEELEKQYKVKKKtldl 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2864 --ETMSNTEKSKQLLEAEATKLRDLAEEASKLRA--IAEEAKHQRQLAE-EDAARQRAEAERILKEKLAAISDATRLKTE 2938
Cdd:pfam05667 396 lpDAEENIAKLQALVDASAQRLVELAGQWEKHRVplIEEYRALKEAKSNkEDESQRKLEEIKELREKIKEVAEEAKQKEE 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 2939 AeiaLKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIE-EKIVLLKKSSDAEM-------ERQKAIVDD 3002
Cdd:pfam05667 476 L---YKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEInsltgklDRTFTVTDE 544
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3146-3691 |
8.49e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.00 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3146 QQKEDSMMQNKLKEEYEkakalARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAA 3225
Cdd:pfam12128 277 RQEERQETSAELNQLLR-----TLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3226 KLAQAEAAALKQKQQADeemaKHKKLAEQTLKQKFQVEQELT--------KVKLQLEETDKQKSLLDDELQRLKDEVDDA 3297
Cdd:pfam12128 352 WQSELENLEERLKALTG----KHQDVTAKYNRRRSKIKEQNNrdiagikdKLAKIREARDRQLAVAEDDLQALESELREQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3298 MRQ---KASVEEELFKVKIQMEELMKLKVRIEEEnqrlMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQI 3374
Cdd:pfam12128 428 LEAgklEFNEEEYRLKSRLGELKLRLNQATATPE----LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3375 AEDDLNQqrtlAEKMLKEKMQAIQEA-SRLKAEA----EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRS---- 3445
Cdd:pfam12128 504 ASEALRQ----ASRRLEERQSALDELeLQLFPQAgtllHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGgeln 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3446 -----LEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEiatkeqmtevKKMEFEKLNTS 3520
Cdd:pfam12128 580 lygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS----------REETFARTALK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3521 KEADDLRKAITELEKEKARLKKEAEEHQ---NKSKEMADAQQKQIEREMTVL----QQTFLTEKEMLLKKEKLIEDEKKK 3593
Cdd:pfam12128 650 NARLDLRRLFDEKQSEKDKKNKALAERKdsaNERLNSLEAQLKQLDKKHQAWleeqKEQKREARTEKQAYWQVVEGALDA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3594 LESQFEEEIKKAKAlkdEQDRQRQQMEEEklklkatMDAALNKQKEAEKDILNKQKEMQELERKrLEQERVLADENQKLR 3673
Cdd:pfam12128 730 QLALLKAAIAARRS---GAKAELKALETW-------YKRDLASLGVDPDVIAKLKREIRTLERK-IERIAVRRQEVLRYF 798
|
570
....*....|....*...
gi 1655274895 3674 EKLQQMEEAQKSTLITEK 3691
Cdd:pfam12128 799 DWYQETWLQRRPRLATQL 816
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3284-3464 |
9.00e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3284 DDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmKKDKDNTQKFLVEEAENMKKLAEDAARLSI 3363
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3364 EAQEAARLRQIAE--------DDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRL 3435
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|..
gi 1655274895 3436 DEETEEYQR---SLEAERKRQLEIIAEAEKLK 3464
Cdd:COG3883 174 EAQQAEQEAllaQLSAEEAAAEAQLAELEAEL 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2777-2998 |
9.74e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2777 AENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIq 2856
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2857 lksRAEKETMSNTEKSKQLLEAEatklrDLAEEASKLRAIAEEAKHQRQL------AEEDAARQRAEAERILKEKLAAIS 2930
Cdd:COG3883 93 ---RALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2931 DATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKA 2998
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2430-2663 |
1.14e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2430 RLEDEEKAAEKLKAEEQKKMAEMQAELdKQKQLAEahakaiakAEKEAQELKLRMQEEvskretaavdaEKQKQNIQlel 2509
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEEL-QQKQAAE--------QERLKQLEKERLAAQ-----------EQKKQAEE--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2510 helknlSEQQIKDKSQQVDEALKSRLRieeeihliriqlettvKQKSNAEDELKQLRDRA-DAAEKLRKLAQEEAEklrK 2588
Cdd:PRK09510 123 ------AAKQAALKQKQAEEAAAKAAA----------------AAKAKAEAEAKRAAAAAkKAAAEAKKKAEAEAA---K 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 2589 QVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAA 2663
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2559-2926 |
1.15e-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: 54.54 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2559 EDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAE----EELKHKSEAERKAANEKQKALEDLENLRMQAEE 2634
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEmmeeERERALEEEEEKEEERKEERKRYRQELEEQIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2635 AERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQehgtvLQLQQDAERLRKQQEDAENAREEA 2714
Cdd:pfam13868 85 REQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEF-----NEEQAEWKELEKEEEREEDERILE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2715 ERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEaekqkeeadrEAKKRSKAEESALKQRDMAENELERQRRLAESTAQQ 2794
Cdd:pfam13868 160 YLKEKAEREEEREAEREEIEEEKEREIARLRAQQ----------EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2795 KLAAEQELIRLRadfdnaeqqrslleDELYRLKNEVIAAQQERKQLEDELskvrsemdILIQLKSRAEKETMsNTEKSKQ 2874
Cdd:pfam13868 230 KARQRQELQQAR--------------EEQIELKERRLAEEAEREEEEFER--------MLRKQAEDEEIEQE-EAEKRRM 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 2875 LLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKL 2926
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2175-2647 |
1.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2175 LKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVH 2254
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2255 serdaELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYdwlirwIADAKQRQENIQAvpitDSKTLKEQ 2334
Cdd:COG4717 150 -----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQ----RLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2335 LAKEKKLLEEIEKNKDKVdECQKYAKAYIDIIKDYELQLVAYKAQVEpltsplkktkLDSASDNIIQEYVTLRTRYSELM 2414
Cdd:COG4717 215 LEEAQEELEELEEELEQL-ENELEAAALEERLKEARLLLLIAAALLA----------LLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2415 TLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETA 2494
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2495 AVDAEKQKQNIQLELHELKNLSE-QQIKDKSQQVDEALKSRLRIEEEIHLIR--IQLETTVKQKSNAEDELKQLRDRADA 2571
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 2572 AEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQ-KALEDLENLRMQAEEAERQVKQAEVEKE 2647
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEwAALKLALELLEEAREEYREERLPPVLER 520
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5208-5236 |
1.57e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.57e-06
10 20
....*....|....*....|....*....
gi 1655274895 5208 IVDPETGKEMTVYEAYRKGLIDHQTYIEL 5236
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2210-2636 |
1.62e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2210 KEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKA-SAVSDKMSRVhSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRE 2288
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEArEAVEDRREEI-EELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2289 LDQLGRQLGYYResydwlirwiadakqrqeniqavpiTDSKTLKEQLAKEKKLLEEieknkDKVDECQKYAK--AYIDII 2366
Cdd:PRK02224 421 RDELREREAELE-------------------------ATLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2367 KDYELQ---LVAYKAQVEPLTSPLKKtKLDSASDniiqeYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKA 2443
Cdd:PRK02224 471 EEDRERveeLEAELEDLEEEVEEVEE-RLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2444 EEQKKMAEMQ---AELDKQKQLAEAHAKAIAKAEKEAQELKLRMqEEVSKRETAAVDAEKQKQNIQL------ELHELKN 2514
Cdd:PRK02224 545 RAAELEAEAEekrEAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERlrekreALAELND 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2515 LSEQQIKDKSQQVDEalksrlrIEEEIHLIRIqlETTVKQKSNAEDELkqlrdrADAAEKLRKLAQEEAEKLRKQVSEET 2594
Cdd:PRK02224 624 ERRERLAEKRERKRE-------LEAEFDEARI--EEAREDKERAEEYL------EQVEEKLDELREERDDLQAEIGAVEN 688
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1655274895 2595 QKKRLaeEELKHkseaERKAANEKQKALEDLENlrmQAEEAE 2636
Cdd:PRK02224 689 ELEEL--EELRE----RREALENRVEALEALYD---EAEELE 721
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3038-3197 |
1.73e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3038 LKNIAEETQQSKlRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADK 3117
Cdd:COG2268 191 RRKIAEIIRDAR-IAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3118 EAEkqIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAaKERAEREAALLRQQAE-EAERQK 3196
Cdd:COG2268 270 IAE--ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEA-EAEAEAEAIRAKGLAEaEGKRAL 346
|
.
gi 1655274895 3197 V 3197
Cdd:COG2268 347 A 347
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4993-5031 |
1.92e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.32 E-value: 1.92e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1655274895 4993 YLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTAFEL 5031
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2822-3194 |
1.95e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2822 ELYRLKNEVIAAQQERKQLEDELSKVRSEMdiliQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEAS-KLRAIAEEA 2900
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIEL----EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEeALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2901 KHQRQLAE------EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDE-----AYQRKILED 2969
Cdd:pfam05557 79 RLKKKYLEalnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLkakasEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2970 QANQHKL-EIEEKI--------------VLLKKSSD-----AEMERQKAIVDDTLKQRRVVEEEIRILK----------L 3019
Cdd:pfam05557 159 EKQQSSLaEAEQRIkelefeiqsqeqdsEIVKNSKSelariPELEKELERLREHNKHLNENIENKLLLKeevedlkrklE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3020 NFEKASSGKLDLELELNKL-------KNIAEET-----------------QQSKLRAEEEAEKLRRLVLEEEMRRKEAED 3075
Cdd:pfam05557 239 REEKYREEAATLELEKEKLeqelqswVKLAQDTglnlrspedlsrrieqlQQREIVLKEENSSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3076 KVKKIAAAEEEAARQRKAAQEELDRLQKKA-------DEVRKQKEEADKEAeKQIVAAQQAALKCNMAEQQVQSVLAQQK 3148
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkerDGYRAILESYDKEL-TMSNYSPQLLERIEEAEDMTQKMQAHNE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1655274895 3149 EDSMMQNKLKEEYEKAKALArdaeaakERAEREAALLRQQAEEAER 3194
Cdd:pfam05557 398 EMEAQLSVAEEELGGYKQQA-------QTLERELQALRQQESLADP 436
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3240-3494 |
1.97e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3240 QADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM 3319
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3320 klkvrieeenQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLS-IEAQEAARLrqiaeDDLNQQRTLAEKMLKEKMQAIQ 3398
Cdd:COG3883 93 ----------RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkIADADADLL-----EELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3399 EASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAE 3478
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|....*.
gi 1655274895 3479 EEAKKFKKQADTIAAR 3494
Cdd:COG3883 238 AAAAAAASAAGAGAAG 253
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2821-3407 |
2.00e-06 |
|
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: 55.06 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2821 DELYRLKNEVIAAQQERKQLEDELSKVRS-------EMDILIQLKSRAEKETMSN-----TEKSKQLLEAEATKLRDLAE 2888
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKALEEIKKksenyidEIKAQINDLEDVADKAISNddpeeIEKKIENIVTKIDKKKNIYD 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2889 EASKL-RAIAEEAKHQRQLAE-----------------EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAEN 2950
Cdd:TIGR01612 1191 EIKKLlNEIAEIEKDKTSLEEvkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2951 ERLRRQ-----AEDEAYQRKILEDQANQHKLEIEEKIvlLKKSSDAEMERQKAIVDDTLkQRRVVEEEIRILKLNFEKAS 3025
Cdd:TIGR01612 1271 DIKAEMetfniSHDDDKDHHIISKKHDENISDIREKS--LKIIEDFSEESDINDIKKEL-QKNLLDAQKHNSDINLYLNE 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3026 SGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLR-RLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKK 3104
Cdd:TIGR01612 1348 IANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKEL 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3105 ADEVRKQKEEADKEAEKQIVAAQQAALKCN---MAEQQVQSVLAQQKEDSMMQ-----NKLKEEYEKAKALARDAEAAKE 3176
Cdd:TIGR01612 1428 KNHILSEESNIDTYFKNADENNENVLLLFKnieMADNKSQHILKIKKDNATNDhdfniNELKEHIDKSKGCKDEADKNAK 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3177 RAEREAALLRQQaeeaeRQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKklaeqtl 3256
Cdd:TIGR01612 1508 AIEKNKELFEQY-----KKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIK------- 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3257 KQKFQVEQELTK--------VKLQLEETDKQKSLLddELQRLKDEVDDAMRQKASVEEELFKVKIQMEElMKLKvrieee 3328
Cdd:TIGR01612 1576 KEKFRIEDDAAKndksnkaaIDIQLSLENFENKFL--KISDIKKKINDCLKETESIEKKISSFSIDSQD-TELK------ 1646
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3329 nqrlMKKDKDNTQKFLVEEAENMKKLAEDAARlsiEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEA 3407
Cdd:TIGR01612 1647 ----ENGDNLNSLQEFLESLKDQKKNIEDKKK---ELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIES 1718
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2432-2675 |
2.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2432 EDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEevskretAAVDAEKQKQNIQLELHE 2511
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-------LQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2512 LKN-LSEQQIKDKSQQVDEALKSRLRIEEEIHliRIQLETTVKQKSNaeDELKQLRDRADAAEKLRKLAQEEAEKLRKQV 2590
Cdd:COG3883 88 LGErARALYRSGGSVSYLDVLLGSESFSDFLD--RLSALSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2591 SEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQM 2670
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
....*
gi 1655274895 2671 SFAEN 2675
Cdd:COG3883 244 ASAAG 248
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3253-3610 |
2.26e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3253 EQTLKQKFQVEQELTKVKLQLEETDKQK-----SLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEE 3327
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3328 ENQRLMKKDKDNTQKFLVEEAENMKKLaEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEA 3407
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYK-QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3408 EMLQRQ-KDLAQEQAQKLLEDKQL------MQQRLDEETEEY---QRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKA 3477
Cdd:TIGR04523 436 IKNNSEiKDLTNQDSVKELIIKNLdntresLETQLKVLSRSInkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3478 EEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFE--KLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMA 3555
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 3556 DAQQ---KQIEREMTVL----QQTFLTEKE----------MLLKKEKL------IEDEKKKLESQFEEEIKKAKALKD 3610
Cdd:TIGR04523 596 KEKKdliKEIEEKEKKIssleKELEKAKKEneklssiiknIKSKKNKLkqevkqIKETIKEIRNKWPEIIKKIKESKT 673
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2547-2970 |
2.32e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.14 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2547 QLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLE 2626
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2627 NLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQED 2706
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2707 AENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRR 2786
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2787 LAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDElyrlkNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETM 2866
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE-----AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2867 SNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEK 2946
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1655274895 2947 EAENERLRRQAEDEAYQRKILEDQ 2970
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
1101-1225 |
2.33e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 50.43 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1101 EKTWPNFIEDErdrvqKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSVR 1171
Cdd:cd21323 15 EGTQHSYSEEE-----KVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTI-DERAINKKKL 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 1172 LPrekgrmrFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21323 89 TP-------FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3584-3772 |
2.36e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.45 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3584 EKLIEdekkKLESQ---FEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE--------MQ 3652
Cdd:PRK00409 519 NELIA----SLEELereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikeLR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3653 ELERKRLEQ--ERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVETV--LNGQNAGDVLdgvEKRPDPMA---FDGIR 3725
Cdd:PRK00409 595 QLQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVkyLSLGQKGEVL---SIPDDKEAivqAGIMK 671
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655274895 3726 DKVPASRLLDIGVLPKKEfdllKNGKTTAKELGETENLRKILKGKNS 3772
Cdd:PRK00409 672 MKVPLSDLEKIQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMRY 714
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3157-3566 |
2.37e-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: 53.38 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3157 LKEEYEKAKALARDAEAAKERAEREAallrqQAEEAERQkvaaeqeaanqaKAQDDAERLRKDAEfeaaklaqaeaAALK 3236
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDA-----QIAEKKRI------------KAEEKEEERRLDEM-----------MEEE 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3237 QKQQADEEMAKHKKLAEQTLKQKFQVEQeltkvklQLEETDKQKSLLDDELQRLKDEVDDAMRQKAsvEEELFKVKIQME 3316
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEE-------QIEEREQKRQEEYEEKLQEREQMDEIVERIQ--EEDQAEAEEKLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3317 ELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLsiEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQA 3396
Cdd:pfam13868 124 KQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAERE--EEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3397 IQEASRLK-AEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRqleiiAEAEKLKLQVSQLseaqa 3475
Cdd:pfam13868 202 ERDELRAKlYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAER-----EEEEFERMLRKQA----- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3476 kaeeeakkfkkqadtiaarlhetEIATKEQMTEVKKMEFEKlntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMA 3555
Cdd:pfam13868 272 -----------------------EDEEIEQEEAEKRRMKRL----EHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
410
....*....|.
gi 1655274895 3556 DAQQKQIEREM 3566
Cdd:pfam13868 325 AERRERIEEER 335
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4992-5028 |
2.43e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.43e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1655274895 4992 KYLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTA 5028
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3047-3716 |
2.48e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3047 QSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRL--------------QKKA------- 3105
Cdd:PRK04863 341 QTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyqqaldvqQTRAiqyqqav 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3106 ---DEVRKQKEEADKEAEK------QIVA-AQQAALKCNMAEQQVQSVLA--QQKEDSM-MQNKL------KEEYEKAKA 3166
Cdd:PRK04863 421 qalERAKQLCGLPDLTADNaedwleEFQAkEQEATEELLSLEQKLSVAQAahSQFEQAYqLVRKIagevsrSEAWDVARE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3167 LARDAEAAKERAEREAAlLRQQAEEAERQkvaaeqeaanqAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMA 3246
Cdd:PRK04863 501 LLRRLREQRHLAEQLQQ-LRMRLSELEQR-----------LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3247 KHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSL---LDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKV 3323
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERD 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3324 RIEEENQRLmKKDKDNTQKFLVEEAENMKKLAED--AARLS-----IEAQEAA-------RLRQ-IAEDDLNQ-QRTLA- 3386
Cdd:PRK04863 649 ELAARKQAL-DEEIERLSQPGGSEDPRLNALAERfgGVLLSeiyddVSLEDAPyfsalygPARHaIVVPDLSDaAEQLAg 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 -----------------------EKMLKEKMQAIQEA------SRLKAE-----------AEMLQRQKDLAQEQAQKLLE 3426
Cdd:PRK04863 728 ledcpedlyliegdpdsfddsvfSVEELEKAVVVKIAdrqwrySRFPEVplfgraarekrIEQLRAEREELAERYATLSF 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3427 DKQLMQ--------------------------QRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEE 3480
Cdd:PRK04863 808 DVQKLQrlhqafsrfigshlavafeadpeaelRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLL 887
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3481 AKkfkkqaDTIAARLHETEiatkEQMTEVKKMEfeklntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQK 3560
Cdd:PRK04863 888 AD------ETLADRVEEIR----EQLDEAEEAK-------RFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQT 950
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3561 QiereMTVLQQTF-LTE-------------KEMLLKKEKLIEDEKKKLE------SQFEEEIKKAKA-----------LK 3609
Cdd:PRK04863 951 Q----RDAKQQAFaLTEvvqrrahfsyedaAEMLAKNSDLNEKLRQRLEqaeqerTRAREQLRQAQAqlaqynqvlasLK 1026
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3610 DEQDRQRQQMEEEKLKLKA---TMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENqkLREKLQQMEEAQKST 3686
Cdd:PRK04863 1027 SSYDAKRQMLQELKQELQDlgvPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAE--MDNLTKKLRKLERDY 1104
|
810 820 830
....*....|....*....|....*....|....*..
gi 1655274895 3687 LITEKHVTvvetvlnGQNAG--DVLD-----GVEKRP 3716
Cdd:PRK04863 1105 HEMREQVV-------NAKAGwcAVLRlvkdnGVERRL 1134
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2428-2668 |
2.62e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.38 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2428 QRRLEDEEKAAEKLKA--EEQKKMAEMQAELDKQ-KQLAEAHAKAIAKAEKEAQELKLRMQEEVSK---RETAAVDAEKQ 2501
Cdd:pfam13868 65 EERKEERKRYRQELEEqiEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2502 KQNIQLELHELKNLseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQE 2581
Cdd:pfam13868 145 LEKEEEREEDERIL--EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2582 EAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQvkqaEVEKERQIQVAHVAAQQSA 2661
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE----EAEKRRMKRLEHRRELEKQ 298
|
....*..
gi 1655274895 2662 AAELRSK 2668
Cdd:pfam13868 299 IEEREEQ 305
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2977-3293 |
3.75e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2977 EIEEKIVLLKKSSDAEMERQKAIVDDTLKQR-RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLR-AEE 3054
Cdd:pfam13868 23 ERDAQIAEKKRIKAEEKEEERRLDEMMEEEReRALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQeREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3055 EAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADE------VRKQKEEADKEAEKQIVAAQQ 3128
Cdd:pfam13868 103 MDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDErileylKEKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3129 AALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEkAKALARDAEAAKERAEREAALLRQQAEEAErqkvaaeqeaanqAK 3208
Cdd:pfam13868 183 EREIARLRAQQEKAQDEKAERDELRAKLYQEEQE-RKERQKEREEAEKKARQRQELQQAREEQIE-------------LK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3209 AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQ-KFQVEQELTKVKLQLEETDKQKSLLDDEL 3287
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQiEEREEQRAAEREEELEEGERLREEEAERR 328
|
....*.
gi 1655274895 3288 QRLKDE 3293
Cdd:pfam13868 329 ERIEEE 334
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2582-3193 |
3.88e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.59 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2582 EAEKLRKQVSEETQKKRLAEEELKHKS---EAERKAANEKQkaleDLEnlrmqaEEAERQvkqaeveKERQIQVAHVAAQ 2658
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRariELEKKASALKR----QLD------RESDRN-------QELQKRIRLLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2659 QSAAAELRSKQMsfaenvskleeslkqehgtvlqlqqdaerlrkqqedaenareeaerelekwrqkanEALRLRLQAEEE 2738
Cdd:pfam05557 64 EAEAEEALREQA--------------------------------------------------------ELNRLKKKYLEA 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2739 AHKKslaqEEAEKQKEEADREAKKRSKAEESALKQrdmaenELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSL 2818
Cdd:pfam05557 88 LNKK----LNEKESQLADAREVISCLKNELSELRR------QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2819 LEDELYRLKneviAAQQERKQLEDELSKvrSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLraiaE 2898
Cdd:pfam05557 158 LEKQQSSLA----EAEQRIKELEFEIQS--QEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLL----K 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2899 EAKH--QRQLAEEDAARQRAEAERILKEKLAA-------ISDATRLKTEAEIALKEK--EAENERLRRQAEDEAYQRKIL 2967
Cdd:pfam05557 228 EEVEdlKRKLEREEKYREEAATLELEKEKLEQelqswvkLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSAR 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2968 EDQANQHKLEIeEKIVLLKKSSDAEM--ERQKAIVDDTLKQRRVVEEEIRILK---------LNFEKASSGKLDLELELN 3036
Cdd:pfam05557 308 QLEKARRELEQ-ELAQYLKKIEDLNKklKRHKALVRRLQRRVLLLTKERDGYRailesydkeLTMSNYSPQLLERIEEAE 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3037 KL------KNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKaaqeELDRLQKKADEVRK 3110
Cdd:pfam05557 387 DMtqkmqaHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRR----KLETLELERQRLRE 462
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3111 QKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKER-----------AE 3179
Cdd:pfam05557 463 QKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQvlrlpettstmNF 542
|
650
....*....|....
gi 1655274895 3180 REAALLRQQAEEAE 3193
Cdd:pfam05557 543 KEVLDLRKELESAE 556
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3024-3281 |
4.33e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3024 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRlvleeemRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQK 3103
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK-------QLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3104 KADEVRKQKEEADKEAEKQIVAAQQaalkcnMAEQQVQSVLAQQkeDSMMQNKLKEEYEKAKALARDAEAAKERAEREAa 3183
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYR------LGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3184 lLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDaefeaaklaqaeaaalkqKQQADEEMAKHKKLAEQTLKQKFQVE 3263
Cdd:COG4942 162 -LAALRAELEAERAELEALLAELEEERAALEALKAE------------------RQKLLARLEKELAELAAELAELQQEA 222
|
250
....*....|....*...
gi 1655274895 3264 QELTKVKLQLEETDKQKS 3281
Cdd:COG4942 223 EELEALIARLEAEAAAAA 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2506-2863 |
4.50e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2506 QLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAeklrklaQEEAEK 2585
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL-------EEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2586 LRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEkerqiqvahVAAQQSAAAEL 2665
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE---------IAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2666 RSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLA 2745
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2746 QEEAEKQKEEADREAKKRSKAEESALKQRDMAENE--LERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDEL 2823
Cdd:COG4372 236 SALLDALELEEDKEELLEEVILKEIEELELAILVEkdTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655274895 2824 YRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEK 2863
Cdd:COG4372 316 ALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2205-2379 |
5.44e-06 |
|
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: 50.91 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2205 VPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEElkkasavSDKMSRVHSErdaELDQHRQHLSSLQDRWKAVFTQIDL 2284
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHP---DAEEIQERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2285 RQRELDQLGRQLGYYRESYDwLIRWIADAKQRQENIQavPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYID 2364
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1655274895 2365 IIKDYELQLVAYKAQ 2379
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2993-3183 |
5.68e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2993 MERQKAIVDDTLKQRRVVEEEiRILKLNFEKASSGKLDLELELNKLKniaeETQQSKLRAEEEAEKLRRLVLEEEMRRKE 3072
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-QAEELQQKQAAEQERLKQLEKERLA----AQEQKKQAEEAAKQAALKQKQAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3073 AEDKVKKIAAAEEEAARQRKAAQEELDRlQKKADEVRKQKEEADK--EAEKQIVAAQQAALKCNMAEQQVQSVLAQQKED 3150
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKKAAAEAKK-KAEAEAAKKAAAEAKKkaEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|...
gi 1655274895 3151 SMMQNKLKEEYEKAKALARDAEAAKERAEREAA 3183
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2772-3107 |
5.70e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2772 KQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM 2851
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2852 DILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQ----LAEEDAARQRAEAERILKEKLA 2927
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2928 AISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQR 3007
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3008 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEA 3087
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1655274895 3088 ARQRKAAQEELDRLQKKADE 3107
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2516-2728 |
5.76e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2516 SEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVseetq 2595
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2596 KKRLAE--------------------EELKHKSEAERKAANEKQKALEDLENLRMQAEEaerqvKQAEVEKERQIQVAHV 2655
Cdd:COG3883 89 GERARAlyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-----KKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2656 AAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEA 2728
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2339-2669 |
5.77e-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: 53.09 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2339 KKLLEEIEKNKDKVDECQKYA--KAYIDIIKDY--ELQLVAYKAQVEpLTSPLKKtKLDSASDniiqeyvtlrtryselm 2414
Cdd:NF033838 68 EKILSEIQKSLDKRKHTQNVAlnKKLSDIKTEYlyELNVLKEKSEAE-LTSKTKK-ELDAAFE----------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2415 tltsqyiKFITDTqrrLEDEEKAAEKlkaeeQKKMAEMQAELDKQKQ-----------------LAEAHAKaIAKAEKE- 2476
Cdd:NF033838 129 -------QFKKDT---LEPGKKVAEA-----TKKVEEAEKKAKDQKEedrrnyptntyktleleIAESDVE-VKKAELEl 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2477 -AQELKLRMQEEVSKRETAAVDAEKQkqniqlELHELKNlseqqIKDKSQQVDEALKSRLRIEEEihliriqlETTVKQK 2555
Cdd:NF033838 193 vKEEAKEPRDEEKIKQAKAKVESKKA------EATRLEK-----IKTDREKAEEEAKRRADAKLK--------EAVEKNV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2556 SNAE-DELKQLRDRADAAEKLRKLAQEEAEKLR-KQVSEET-------QKKRLAEEElKHKSEAERKAANEKQkalEDLE 2626
Cdd:NF033838 254 ATSEqDKPKRRAKRGVLGEPATPDKKENDAKSSdSSVGEETlpspslkPEKKVAEAE-KKVEEAKKKAKDQKE---EDRR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2627 N--------LRMQAEEAERQVKQAEVE--KERQIQVAHVAAQQSAAAELRSKQ 2669
Cdd:NF033838 330 NyptntyktLELEIAESDVKVKEAELElvKEEAKEPRNEEKIKQAKAKVESKK 382
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3093-3296 |
5.78e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3093 AAQEELDRLQ-KKADEVRKQKEEaDKEAEKQI------VAAQQAALKC----NMAEQQVQSVLAQQKEDSMMQNKLKEEy 3161
Cdd:PRK09510 59 AVVEQYNRQQqQQKSAKRAEEQR-KKKEQQQAeelqqkQAAEQERLKQlekeRLAAQEQKKQAEEAAKQAALKQKQAEE- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3162 EKAKALARDAEAAKERAEREAALLRQQAEEAERQ-KVAAEQEAANQAKAQDDAERLRKDAEfeaaklAQAEAAALKQKQQ 3240
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKaEAEAAKKAAAEAKKKAEAEAAAKAAA------EAKKKAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 3241 ADEEmAKHKKLAEqtlkQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDD 3296
Cdd:PRK09510 211 AAAE-AKKKAAAE----AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2610-3039 |
6.35e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.13 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2610 AERKAANEK----QKALEDLENLRMQAeeaeRQVKQAEVEKERQIQvahvAAQQSAAAELRSKQMSfaenvSKLeesLKQ 2685
Cdd:PRK10929 58 EERKGSLERakqyQQVIDNFPKLSAEL----RQQLNNERDEPRSVP----PNMSTDALEQEILQVS-----SQL---LEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2686 EHgtvlQLQQDAERLRK---------QQEDAEnareeaerelekwRQKANEALRlRLQA-------EEEAHKKSLaqeea 2749
Cdd:PRK10929 122 SR----QAQQEQDRAREisdslsqlpQQQTEA-------------RRQLNEIER-RLQTlgtpntpLAQAQLTAL----- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2750 ekqkeeadreakkrsKAEESALKQRdmaENELErqrrLAESTAQQKlaaeQELIRLRAdfdnaeqqrslledELYrlkne 2829
Cdd:PRK10929 179 ---------------QAESAALKAL---VDELE----LAQLSANNR----QELARLRS--------------ELA----- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2830 viaaQQERKQLEDELSKVRSemdiliQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEE 2909
Cdd:PRK10929 214 ----KKRSQQLDAYLQALRN------QLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2910 DAARQRAEAERILKEKLAaisdatrLKTEAEIA--LKEKEAENERLRRQAED--EAYQRKILEDQANQ---HKLEIEEki 2982
Cdd:PRK10929 284 IASQQRQAASQTLQVRQA-------LNTLREQSqwLGVSNALGEALRAQVARlpEMPKPQQLDTEMAQlrvQRLRYED-- 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 2983 vLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLK 3039
Cdd:PRK10929 355 -LLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGDTLILELTKLK 410
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2876-3462 |
6.84e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2876 LEAEATKLRDLAEEASKLRAIAEEAKHQR-QLAEEDAARQRAEAERILKEKLAAISDATRLKTeAEIALKEKEAENERLR 2954
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIeLLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2955 RQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERqkaivddtlkqrrvVEEEIRilklnfekassgklDLELE 3034
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--------------LEREIE--------------RLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3035 LNKLKNiaeetqqsklRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLqkKADEVRKQKEE 3114
Cdd:COG4913 354 LEERER----------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA--EAALRDLRREL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3115 ADKEAEKQIVAAQQAALKCNMaeQQVQSVLAQQ---KEDSM------MQNKLKEEyekakalarDAEAAKERA------- 3178
Cdd:COG4913 422 RELEAEIASLERRKSNIPARL--LALRDALAEAlglDEAELpfvgelIEVRPEEE---------RWRGAIERVlggfalt 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3179 -----EREAALLR-----QQAEEAERQKVAAEQEAANQAKAQDD--AERLR-KDAEFEAAKLAQAEAAALKQKQQADEEM 3245
Cdd:COG4913 491 llvppEHYAAALRwvnrlHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDfKPHPFRAWLEAELGRRFDYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3246 AKHKK--LAEQTLKQKFQVEQELTKVKLQLE-----ETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEEL 3318
Cdd:COG4913 571 RRHPRaiTRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3319 MKLKVRIEEEnqrlmkKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQiAEDDLNQQRTLAEKMLKEKMQAIQ 3398
Cdd:COG4913 651 QRLAEYSWDE------IDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELE 723
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3399 EASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEK 3462
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3540-3684 |
7.03e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3540 LKKEAEEHQNKSKEMADAQQKQIEREMTVLqqtfltekemllKKEKLIE--DEKKKLESQFEEEIKKAKALKDEQDRQRQ 3617
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAI------------KKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3618 QMEEeklKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLrEKLQQM--EEAQK 3684
Cdd:PRK12704 93 QKEE---NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2499-2932 |
7.27e-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: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2499 EKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLEttvkqksNAEDELKQLRDRADAAEKLRKL 2578
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA-------ELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2579 AQEEAEKLRKQVS-----EETQKKRLAEEELKHKSEAERKAANEKqkaleDLENLRMQAEEAERQVKQAEVEKErQIQva 2653
Cdd:pfam07888 106 LSASSEELSEEKDallaqRAAHEARIRELEEDIKTLTQRVLERET-----ELERMKERAKKAGAQRKEEEAERK-QLQ-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2654 hvAAQQSAAAELRSKQMSFAEnvskLEESLKQEHGTVLQLQQDAERLrkqqedaenareeaerelekwRQKANEAlrLRL 2733
Cdd:pfam07888 178 --AKLQQTEEELRSLSKEFQE----LRNSLAQRDTQVLQLQDTITTL---------------------TQKLTTA--HRK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2734 QAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAeeSALKQRDMAENELERQRRLAestAQQKLAAEQELIRLRADFDNAE 2813
Cdd:pfam07888 229 EAENEALLEELRSLQERLNASERKVEGLGEELS--SMAAQRDRTQAELHQARLQA---AQLTLQLADASLALREGRARWA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2814 QQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEmdiliqlksRAEKETMSNTEKSKQLLEAEATKlRDLAEEASKL 2893
Cdd:pfam07888 304 QERETLQQSAEADKDRIEKLSAELQRLEERLQEERME---------REKLEVELGREKDCNRVQLSESR-RELQELKASL 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 1655274895 2894 RAIAEEakhQRQLAEEdaARQRAEAERILKEKLAAISDA 2932
Cdd:pfam07888 374 RVAQKE---KEQLQAE--KQELLEYIRQLEQRLETVADA 407
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2421-2663 |
7.74e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2421 IKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKaIAKAEKEAQELKLRMQEEVSKRETAAVDAE 2499
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElQAELEALQAE-IDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2500 KQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLA 2579
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2580 QEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQ 2659
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
....
gi 1655274895 2660 SAAA 2663
Cdd:COG3883 257 AAAG 260
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3379-3770 |
8.27e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3379 LNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLqrqKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERK--RQLEI 3456
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLL---TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3457 IAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIAT-KEQMTEVKKMEFEKLNTSKEADDLRKAIteLEK 3535
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAhIKAVTQIEQQAQRIHTELQSKMRSRAKL--LMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3536 EKARLKKEAEEHQNKS---------KEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAK 3606
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRllqtlhsqeIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3607 ALKDEQDRQRQQMEEEKLKLKATMDAalnKQKEAEKDILNKQKEMQELERKRLEQERVladeNQKLREKLQQMEEAQKST 3686
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTAQCEKLEKIHLQES----AQSLKEREQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3687 LITEKHVTVVETVLNGQNAGD-VLDGVEKRPDPMAFDGIRDKVPASRLLDIGVLPKKefdLLKNGKTTAKELGETENLRK 3765
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPcPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ---LETSEEDVYHQLTSERKQRA 559
|
....*
gi 1655274895 3766 ILKGK 3770
Cdd:TIGR00618 560 SLKEQ 564
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
3273-3709 |
9.19e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.22 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3273 LEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEelfkvkiqMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENmK 3352
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDE--------LEALIDQWLAELEQVIALRRAGGLEAALALVRSGEG-K 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3353 KLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQ 3432
Cdd:COG5278 149 ALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3433 QRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKM 3512
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3513 EFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKK 3592
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3593 KLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKL 3672
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430
....*....|....*....|....*....|....*..
gi 1655274895 3673 REKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVL 3709
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
3239-3464 |
1.13e-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: 51.95 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3239 QQADEEMAKHKKLAEQTLKQ-KFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEvddaMRQkasVEEELFKVKIQMEE 3317
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEElQQQREEELEELQEQLEDLESSIQELEKEIKKLESS----IKQ---VEEELEELKEQNEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3318 LmklkvrieEENQRLMKKdkdnTQKFLVEEAENMKKL----AEDAARL-SIEAQ-EAARLRQIAEddlnqQRTLAEKMLK 3391
Cdd:pfam05667 382 L--------EKQYKVKKK----TLDLLPDAEENIAKLqalvDASAQRLvELAGQwEKHRVPLIEE-----YRALKEAKSN 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3392 EKMqaiqEASRLKAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQQrLDEETEEYQRSleAERKRQLEIIAEAEKLK 3464
Cdd:pfam05667 445 KED----ESQRKLEEIKELREKiKEVAEEAKQKEELYKQLVAE-YERLPKDVSRS--AYTRRILEIVKNIKKQK 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2934-3427 |
1.20e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2934 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKivllkKSSDAEMERQKAIVDDTLKQRRVVEEE 3013
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3014 IRILKLNFEKASsgkldLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKA 3093
Cdd:COG4717 125 LQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3094 AQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQ---------SVLAQQKEDSMMQNKLKEEYEKA 3164
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3165 KALARDAEAAKERAEREAALLRQQAEEAERQkvaAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEE 3244
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQAL---PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3245 MAKHKKLAEQTLKQKFQveQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELfKVKIQMEELMKLKVR 3324
Cdd:COG4717 357 EELEEELQLEELEQEIA--ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL-EELLEALDEEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3325 IEEENQRLMkkdkdntqkflvEEAENMKKLAEDAARLSieaqeaARLRQIAEDDLNQQRTLAEKMLKEKMQ-AIQEASRL 3403
Cdd:COG4717 434 LEELEEELE------------ELEEELEELREELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAAL 495
|
490 500
....*....|....*....|....*
gi 1655274895 3404 KAEAEMLQR-QKDLAQEQAQKLLED 3427
Cdd:COG4717 496 KLALELLEEaREEYREERLPPVLER 520
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3508-3676 |
1.21e-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: 50.31 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3508 EVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQI--EREMTVLQQtfltEKEMLLKKEK 3585
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVrnNKEYEALQK----EIESLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3586 LIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEeklklkatmdaalnKQKEAEKDILNKQKEMQELERKRLEQERVL 3665
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEE--------------KKAELDEELAELEAELEELEAEREELAAKI 172
|
170
....*....|.
gi 1655274895 3666 ADENQKLREKL 3676
Cdd:COG1579 173 PPELLALYERI 183
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2420-2996 |
1.34e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2420 YIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKqlaeaHAKAIAKAEKEAQELKLRMQEEVSKretaavdAE 2499
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESEIKT-------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2500 KQKQNIQLELHELKNLSEQQIKDKSqqvDEALKSRLRIEEEIHLIRiQLETTVKQKSNAEDELKQLRDradaaeklrklA 2579
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHA-----------I 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2580 QEEAEKLRKQVSEETQKKRlAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQ--AEVEKERQIQVAHVAA 2657
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKS-RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2658 QQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEAL-RLRLQAE 2736
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKsRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2737 EEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRA--------- 2807
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkledldsk 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2808 --DFDNAEQQRSLLEDELYRLKNEVIAAQQerKQLEDELSKVRSEMDiliqlksraekETMSNTEKSKQLLEAEATKLRD 2885
Cdd:PRK01156 567 rtSWLNALAVISLIDIETNRSRSNEIKKQL--NDLESRLQEIEIGFP-----------DDKSYIDKSIREIENEANNLNN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2886 LAEEASKLRAIAEEAKHQRQLAEEDAARQRaEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 2965
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
570 580 590
....*....|....*....|....*....|.
gi 1655274895 2966 ILEDQANQHKLEIEEKIVLLKKSSDAEMERQ 2996
Cdd:PRK01156 713 ELSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2904-3128 |
1.35e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2904 RQLAEEDAARQRAEAERILKEklaAISDATRLKTEAEIALKEkeaENERLRRQAEDEAYQR----KILEDQANQHKLEIE 2979
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERrnelQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2980 EKIVLLKKSsDAEMERQKAIVDDTLKQRRVVEEEIRILKLNfekassgkldlelELNKLKNIAEETQqsklraeEEAEKL 3059
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEE-------------QLQELERISGLTA-------EEAKEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3060 RRLVLEEEMRRkEAEDKVKKIaaaeeeaarqrkaaqEEldrlqkkadevrKQKEEADKEAEKQIVAAQQ 3128
Cdd:PRK12704 159 LLEKVEEEARH-EAAVLIKEI---------------EE------------EAKEEADKKAKEILAQAIQ 199
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2144-2566 |
1.58e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2144 SATAPVLRSELE---LTVQKMDHayMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTnLK 2220
Cdd:pfam15921 411 SITIDHLRRELDdrnMEVQRLEA--LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT-AK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2221 KMRAEAeAEQPVFD---SLEEELKKASAVSDKMSRVHSERDAELdQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLG 2297
Cdd:pfam15921 488 KMTLES-SERTVSDltaSLQEKERAIEATNAEITKLRSRVDLKL-QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2298 YYRESYDWLIRWIADAKQRQENIQavpiTDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYK 2377
Cdd:pfam15921 566 ILRQQIENMTQLVGQHGRTAGAMQ----VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2378 AQVEPLTSPLKKTKldsasDNIIQEYVTLRtrySELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELD 2457
Cdd:pfam15921 642 SERLRAVKDIKQER-----DQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2458 KQKQL--AEAHAKAIA-------------------------KAEKEAQELKLRMQEEVSK--RETAAVDAEKQKQNIQLE 2508
Cdd:pfam15921 714 TLKSMegSDGHAMKVAmgmqkqitakrgqidalqskiqfleEAMTNANKEKHFLKEEKNKlsQELSTVATEKNKMAGELE 793
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 2509 LheLKNlSEQQIKDKSQQVDEAL-KSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLR 2566
Cdd:pfam15921 794 V--LRS-QERRLKEKVANMEVALdKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3510-3687 |
1.60e-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: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3510 KKMEFEKLNTSKEADD-LRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTflTEKEMLLKKEKLiE 3588
Cdd:pfam15709 321 SKALLEKREQEKASRDrLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQR--RFEEIRLRKQRL-E 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3589 DEKKKLEsqfEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAalNKQKEAEKDILNKQKEMQELERKRLEQERVLADE 3668
Cdd:pfam15709 398 EERQRQE---EEERKQRLQLQAAQERARQQQEEFRRKLQELQRK--KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMA 472
|
170
....*....|....*....
gi 1655274895 3669 NQKLREKLQQMEEAQKSTL 3687
Cdd:pfam15709 473 EEERLEYQRQKQEAEEKAR 491
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2491-2832 |
1.66e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2491 RETAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRAD 2570
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2571 AAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQI 2650
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2651 QVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEA-L 2729
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEViL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2730 RLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADF 2809
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340
....*....|....*....|...
gi 1655274895 2810 DNAEQQRSLLEDELYRLKNEVIA 2832
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLS 360
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2564-2820 |
1.78e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2564 QLRDRADAAEKLRKLAQEEAEKLRKQVSE-ETQKKRLAEEELKHKSEAERKAANEKQKALED-LENLRMQAEEAERQVKQ 2641
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEaEAALEEFRQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2642 AEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRkqqedaenareeaerelekw 2721
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR-------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2722 RQKANEALRLRLQAEeeahkkslaqeeaekqkeeadreakkrskAEESALKQRdmaENELERQRRLAESTAQQKLAAEQE 2801
Cdd:COG3206 305 AQLQQEAQRILASLE-----------------------------AELEALQAR---EASLQAQLAQLEARLAELPELEAE 352
|
250 260
....*....|....*....|
gi 1655274895 2802 LIRLRADFDNAEQQ-RSLLE 2820
Cdd:COG3206 353 LRRLEREVEVARELyESLLQ 372
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
3364-3684 |
1.81e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.02 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3364 EAQEAARLRQiaeddlNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQ 3443
Cdd:pfam02029 3 DEEEAARERR------RRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3444 RSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKE-QMTEVKKMEFEKLNTSKE 3522
Cdd:pfam02029 77 KRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREkEYQENKWSTEVRQAEEEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3523 ADDLRKAITELEKEKARLKKEAEEHQNKSKEMADA-------QQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE 3595
Cdd:pfam02029 157 EEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKyeskvflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3596 SQFEEEIKKAKALKDEQDRQRQQMEEEKL-KLKatmdaalNKQKEAEKdilnkqkEMQELERKRLEQERVLADENQKLRE 3674
Cdd:pfam02029 237 EEEAEVFLEAEQKLEELRRRRQEKESEEFeKLR-------QKQQEAEL-------ELEELKKKREERRKLLEEEEQRRKQ 302
|
330
....*....|
gi 1655274895 3675 klqqmEEAQK 3684
Cdd:pfam02029 303 -----EEAER 307
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
1116-1225 |
1.82e-05 |
|
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: 48.13 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1116 QKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSVRLPrekgrmrFHKLQN 1186
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTI-DERAINKKKLTP-------FIIQEN 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274895 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21325 97 LNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2632-3062 |
1.83e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2632 AEEAERQVKQA-EVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQ--EHgtvLQLQQDAERLRKQQEDAE 2708
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasDH---LNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2709 NAREeaerelekwrqKANEALRLRLQAEEEAHkkslaqeeaekqKEEADREAKKRSkAEESAlkqrDMAENEL-ERQRRL 2787
Cdd:PRK04863 355 ADLE-----------ELEERLEEQNEVVEEAD------------EQQEENEARAEA-AEEEV----DELKSQLaDYQQAL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2788 aesTAQQKLA-----AEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELS---KVRSEMDILIQLKS 2859
Cdd:PRK04863 407 ---DVQQTRAiqyqqAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2860 RAEKETMSNT--EKSKQLLEaEATKLRDLAEEASKLRAIAEEAKhQRQLAEEDAARQRAEAERILKEKLAAISDATRLkt 2937
Cdd:PRK04863 484 KIAGEVSRSEawDVARELLR-RLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-- 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2938 eaeiaLKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEkivLLKKS-----SDAEMERQKAIVDDTLKQRRVVEE 3012
Cdd:PRK04863 560 -----QEELEARLESLSESVSEARERRMALRQQLEQLQARIQR---LAARApawlaAQDALARLREQSGEEFEDSQDVTE 631
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3013 EIRILKLNFEKASSGKLDLELELNKLKNIAEETQQsklRAEEEAEKLRRL 3062
Cdd:PRK04863 632 YMQQLLERERELTVERDELAARKQALDEEIERLSQ---PGGSEDPRLNAL 678
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
3090-3678 |
1.97e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3090 QRKAAQEELDRLQKKADEVRKQKEE----------ADKEAEKQIVAAQQAalkcnmaEQQVQSVLAQQKEdsmmqnkLKE 3159
Cdd:PRK10246 192 QHKSARTELEKLQAQASGVALLTPEqvqsltaslqVLTDEEKQLLTAQQQ-------QQQSLNWLTRLDE-------LQQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3160 EYEKAKALARDAEAAKERAEREAALL--------------RQQAEEAE----RQKVAAEQEAANQAKAQddAERLRKDAE 3221
Cdd:PRK10246 258 EASRRQQALQQALAAEEKAQPQLAALslaqparqlrphweRIQEQSAAlahtRQQIEEVNTRLQSTMAL--RARIRHHAA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3222 FEAAKLAQAEAAALKQKQQADEEMAKHKKLA--EQTLKQKFQVEQELTKVKLQL-EETDKQKSLLDDELQRLKDEVDDAM 3298
Cdd:PRK10246 336 KQSAELQAQQQSLNTWLAEHDRFRQWNNELAgwRAQFSQQTSDREQLRQWQQQLtHAEQKLNALPAITLTLTADEVAAAL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3299 RQKAS---VEEELFKVKIQMEELMKLKVRIEEENQRL-------------MKKD-KDNTQKF-----LVEEAENMKKLAE 3356
Cdd:PRK10246 416 AQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVtqeqtqrnaalneMRQRyKEKTQQLadvktICEQEARIKDLEA 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3357 DAARL---------------SIEAQEAARLrqiaedDLNQQRTLAekMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQA 3421
Cdd:PRK10246 496 QRAQLqagqpcplcgstshpAVEAYQALEP------GVNQSRLDA--LEKEVKKLGEEGAALRGQLDALTKQLQRDESEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3422 QKLLEDkqlmQQRLDEETEEYQRSLEAERKRQLEI---IAEAEKLKLQVSQLSEAQAKAEeeakkfkkqadTIAArlHET 3498
Cdd:PRK10246 568 QSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEEHERQLRLLSQRHELQG-----------QIAA--HNQ 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3499 EIATKEQMTEVKKMEFEKlntskEADDLRKAITELEKEKARL---KKEAEEHQNKSKEMADAQQK--QIEREMTVLQQTF 3573
Cdd:PRK10246 631 QIIQYQQQIEQRQQQLLT-----ALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRiqQLTPLLETLPQSD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3574 LTEKE---MLLKKEKLIEDEKKKLESQFEeeikkakALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEA-------EKD 3643
Cdd:PRK10246 706 DLPHSeetVALDNWRQVHEQCLSLHSQLQ-------TLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAflaalldEET 778
|
650 660 670
....*....|....*....|....*....|....*
gi 1655274895 3644 ILNKQKEMQELERKRLEQERVLADENQKLREKLQQ 3678
Cdd:PRK10246 779 LTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQH 813
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2772-2965 |
2.05e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2772 KQRDMAENELERQRRLAESTA--QQKLAAEQEliRLRADfdnaEQQRslledelyrlknevIAAQQERKQLEDELSKVRS 2849
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEelQQKQAAEQE--RLKQL----EKER--------------LAAQEQKKQAEEAAKQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2850 EmdiliqlKSRAEKETMSNTEKSKQLLEAEATKLRDLA---EEASKLRAIAEEAKHQRQLAEEDA-----------ARQR 2915
Cdd:PRK09510 130 K-------QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAkkaAAEAKKKAEAEAAKKAAAEAKKKAeaeaaakaaaeAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2916 AEAERilKEKLAAISD---ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 2965
Cdd:PRK09510 203 AEAEA--KKKAAAEAKkkaAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2880-3196 |
2.14e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2880 ATKLRDLAEEASKLRA----IAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRR 2955
Cdd:pfam07888 29 AELLQNRLEECLQERAellqAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2956 QAEDEAYQRKILEDQANQHK---LEIEEKIVLLKKSS---DAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKL 3029
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEariRELEEDIKTLTQRVlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3030 DLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVleEEMRRKEAEDKVKKiaaaeeeaaRQRKAAQEELDRLQKKADEVR 3109
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL--TTAHRKEAENEALL---------EELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3110 KQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEeyekakALARDAEAAKERAEREAALLRQ-- 3187
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERE------TLQQSAEADKDRIEKLSAELQRle 331
|
330
....*....|..
gi 1655274895 3188 ---QAEEAERQK 3196
Cdd:pfam07888 332 erlQEERMEREK 343
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2429-2532 |
2.28e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2429 RRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHA-KAIAKAEKEAQELKLRMQEevSKRETAAVDAEKQKQNIQL 2507
Cdd:PRK00409 537 EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAqQAIKEAKKEADEIIKELRQ--LQKGGYASVKAHELIEARK 614
|
90 100
....*....|....*....|....*
gi 1655274895 2508 ELHElKNLSEQQIKDKSQQVDEALK 2532
Cdd:PRK00409 615 RLNK-ANEKKEKKKKKQKEKQEELK 638
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2991-3463 |
2.31e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2991 AEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELnKLKNIAEETQQSKLRAEEEAEKLRRLvleeEMRR 3070
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEEL----EERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3071 KEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAqQKED 3150
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-QLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3151 SMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQA 3230
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3231 EAAALKQKQQADEEMAKhKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKsllddELQRLKDEVDDAMRQ-KASVEEELF 3309
Cdd:COG4717 315 ELEEEELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEaGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3310 KVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENmkkLAEDAARLSIEAQEAARLRqiaeDDLNQQRTLAEKM 3389
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELEELEEELEELEEEL----EELREELAELEAE 461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3390 LKEkMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLledkQLMQQRLDEETEEYqrsleaERKRQLEIIAEAEKL 3463
Cdd:COG4717 462 LEQ-LEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEY------REERLPPVLERASEY 524
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2236-2669 |
2.31e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2236 LEEELKKASAVSDKmSRVHSERDAELDQHRQHLSS-LQD----RWKAVFTQIDLRQrELDQLGRQLGYYRESYDWLIRWI 2310
Cdd:pfam05483 263 LEESRDKANQLEEK-TKLQDENLKELIEKKDHLTKeLEDikmsLQRSMSTQKALEE-DLQIATKTICQLTEEKEAQMEEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2311 ADAKQRQENIQAVPITDSKTLKEQLAKEKKLLE-----------EIEKNKDKVDECQKYAKAyidiiKDYELQ------- 2372
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEknedqlkiitmELQKKSSELEEMTKFKNN-----KEVELEelkkila 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2373 ----LVAYKAQVEPLTSPLKKTKldsasdniiQEYV-TLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQK 2447
Cdd:pfam05483 416 edekLLDEKKQFEKIAEELKGKE---------QELIfLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2448 KMaEMQAELDKqkqLAEAHAKAIAKAEKEAQELKlRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQV 2527
Cdd:pfam05483 487 NI-ELTAHCDK---LLLENKELTQEASDMTLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2528 DEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETqkKRLAEEELK-H 2606
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN--KQLNAYEIKvN 639
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 2607 KSEAERKAANEK--------QKALEDL----ENLRMQAEEAERQVKQA-EVEKERQIQVAHVAAQQSAAAELRSKQ 2669
Cdd:pfam05483 640 KLELELASAKQKfeeiidnyQKEIEDKkiseEKLLEEVEKAKAIADEAvKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3272-3661 |
2.31e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3272 QLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELfkvKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENM 3351
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3352 KKLAEDAARLSIEAQEAARLRQIAEDdlnqQRTLAEKMLKEKMqaiqEASRLKAEAEMLQRQKdlAQEQAQKllEDKQLM 3431
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEED----IKTLTQRVLERET----ELERMKERAKKAGAQR--KEEEAER--KQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3432 QQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAkaeeeakkfkkqadtiAARLHETEI-ATKEQMTEVK 3510
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT----------------TAHRKEAENeALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3511 kmefEKLNTSKEA-----DDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQ------QKQIEREMTVLQQTFLTEKEM 3579
Cdd:pfam07888 244 ----ERLNASERKveglgEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASlalregRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3580 LLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELerKRL 3659
Cdd:pfam07888 320 IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYI--RQL 397
|
..
gi 1655274895 3660 EQ 3661
Cdd:pfam07888 398 EQ 399
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2369-2848 |
2.36e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 51.12 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2369 YELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKK 2448
Cdd:COG4995 6 LLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2449 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVD 2528
Cdd:COG4995 86 ALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2529 EALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKS 2608
Cdd:COG4995 166 LALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2609 EAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHG 2688
Cdd:COG4995 246 AAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2689 TVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAhkkslaqeeaekqkeEADREAKKRSKAEE 2768
Cdd:COG4995 326 LLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLA---------------LLLEALLLLLLALL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2769 SALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELY---RLKNEVIAaqqerkQLEDELS 2845
Cdd:COG4995 391 AALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYafvQLYQLLIA------PIEAELP 464
|
...
gi 1655274895 2846 KVR 2848
Cdd:COG4995 465 GIK 467
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4791-4827 |
2.39e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 2.39e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1655274895 4791 LNLLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEI 4827
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2329-2806 |
2.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2329 KTLKEQLAKEKKLLEEIEKNKDKVDECQkyakAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRt 2408
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2409 rySELMTLTSQYiKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEV 2488
Cdd:COG4717 139 --AELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2489 SKRETAAVDAEKQKQNIQLELHELKNlsEQQIKDKSQ------------QVDEALKSRLRIEEEIHLIRIQLETTVKQ-K 2555
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAAL--EERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLlL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2556 SNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKqvseetqkkrlaeeELKHKSEAERKAANEKQKALEDLENLRMQAEEA 2635
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLA--------------ALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2636 ERQVKQAEVEKERQIQVAhvAAQQSAAAELRSKQMSFAENVSKLEEslkqehgtvlqLQQDAERLRKQQEDAENAREEAE 2715
Cdd:COG4717 360 EEELQLEELEQEIAALLA--EAGVEDEEELRAALEQAEEYQELKEE-----------LEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2716 RELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAkkrskaeESALKQRDMAENELER--QRRLAESTAQ 2793
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL-------AELLQELEELKAELRElaEEWAALKLAL 499
|
490
....*....|...
gi 1655274895 2794 QKLAAEQELIRLR 2806
Cdd:COG4717 500 ELLEEAREEYREE 512
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1269-1346 |
2.72e-05 |
|
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: 46.14 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1269 DNFTTSWRDGKLFNAVIHK------NYPRLIdmgkvyRQTNLENLEQAFNvAEKDLGVTRLLDPEDVDVPHPDEKSIITY 1342
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNAlggsvpGWPNLD------PEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAY 92
|
....
gi 1655274895 1343 VSSL 1346
Cdd:cd21185 93 AAQL 96
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2799-3192 |
2.86e-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: 50.98 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2799 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDiliqlksraEKETMSNtEKSKQLLE- 2877
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLE---------EKESFLN-KKTKQLQDl 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2878 --------AEATKLRDLAEeaSKLRAIAEEAKHQRQLAEE--DAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKE 2947
Cdd:pfam10174 372 teekstlaGEIRDLKDMLD--VKERKINVLQKKIENLQEQlrDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2948 AENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLL------KKSSDAEM-ERQKAIVDDTLKQrrvvEEEIRILKLN 3020
Cdd:pfam10174 450 RIIERLKEQREREDRERLEELESLKKENKDLKEKVSALqpelteKESSLIDLkEHASSLASSGLKK----DSKLKSLEIA 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3021 FEKASSGKLDLELELNKLKNIAEETQQSklraEEEAEKLRRLVLE-----EEMRRKEAE----------------DKVKK 3079
Cdd:pfam10174 526 VEQKKEECSKLENQLKKAHNAEEAVRTN----PEINDRIRLLEQEvarykEESGKAQAEverllgilreveneknDKDKK 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3080 IAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMmqnKLKE 3159
Cdd:pfam10174 602 IAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDAT---KARL 678
|
410 420 430
....*....|....*....|....*....|...
gi 1655274895 3160 EYEKAKALARDAEAAKERAEReaallRQQAEEA 3192
Cdd:pfam10174 679 SSTQQSLAEKDGHLTNLRAER-----RKQLEEI 706
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2677-3001 |
3.20e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2677 SKLEESLkQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKwrqkaneALRLRLQAEEEAHKKSLAQEEAEKQKEEA 2756
Cdd:pfam07888 34 NRLEECL-QERAELLQAQEAANRQREKEKERYKRDREQWERQRR-------ELESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2757 DREAKKRSKAEESALKqrDMAENELERQRRLAE---STAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAA 2833
Cdd:pfam07888 106 LSASSEELSEEKDALL--AQRAAHEARIRELEEdikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2834 QQERKQLEDELSKVRSEMD----ILIQLKSRAEKETMSNTEKSKQLLEAEATK--LRDLAEEASKLRAIAEEAKhqRQLA 2907
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2908 EEDAARQRAEAErILKEKLAAISDATRLkTEAEIALKEKEA----ENERLRRQAEDEayQRKILEDQANQHKLEieekiv 2983
Cdd:pfam07888 262 SMAAQRDRTQAE-LHQARLQAAQLTLQL-ADASLALREGRArwaqERETLQQSAEAD--KDRIEKLSAELQRLE------ 331
|
330
....*....|....*...
gi 1655274895 2984 llKKSSDAEMERQKAIVD 3001
Cdd:pfam07888 332 --ERLQEERMEREKLEVE 347
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5201-5229 |
3.40e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 3.40e-05
10 20
....*....|....*....|....*....
gi 1655274895 5201 VRKRRVVIVDPETGKEMTVYEAYRKGLID 5229
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
3261-3453 |
3.48e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 50.37 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3261 QVEQELTKVKLQLEETDKqkSLLDDELQRLKDEVDDAMRQKASveeelfkvkiqmeelmklkvriEEENQRLMKKDKDNT 3340
Cdd:pfam13779 467 EVADLLWELALRIEDGDL--SDAERRLRAAQERLSEALERGAS----------------------DEEIAKLMQELREAL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3341 QKFLVEEAENMKKLAEDAARLSIEAQeaarlRQIAEDDLnqqrtlaEKMlkekMQAIQEASRL--KAEA-EML------- 3410
Cdd:pfam13779 523 DDYMQALAEQAQQNPQDLQQPDDPNA-----QEMTQQDL-------QRM----LDRIEELARSgrRAEAqQMLsqlqqml 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3411 --------QRQKDLAQEQAQKLLEDKQLM---QQRLDEETeeyQRSLEAERKRQ 3453
Cdd:pfam13779 587 enlqagqpQQQQQQGQSEMQQAMDELGDLlreQQQLLDET---FRQLQQQGGQQ 637
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3591-3700 |
3.63e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3591 KKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLkLKATmDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQ 3670
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|
gi 1655274895 3671 KLREKLQQMEEAQKSTLITEKHVTVVETVL 3700
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3155-3684 |
4.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3155 NKLKEEYEKAKALARDAEAAKERAEreaaLLRQQAEEAERQKvaaeqeaanqaKAQDDAERLRK-DAEFEAAKLAQAEAA 3233
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIE----LLEPIRELAERYA-----------AARERLAELEYlRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3234 ALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDkqksllDDELQRLKDEVDDAMRQKASVEEELfkvKI 3313
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRR---AR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3314 QMEELMKLKVRIEEEnqrlmkkdkdntqkflveeaenmkklAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEkmlKEK 3393
Cdd:COG4913 364 LEALLAALGLPLPAS--------------------------AEEFAALRAEAAALLEALEEELEALEEALAEAE---AAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3394 MQAIQEASRLKAEAEMLQRQK---DLAQEQAQKLLEDK------------QLMQQRLDEET-----EEYQRSL------E 3447
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKsniPARLLALRDALAEAlgldeaelpfvgELIEVRPEEERwrgaiERVLGGFaltllvP 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3448 AERKRQ-LEIIaEAEKLKLQVSqlSEAQAKAEEEAKKFKKQADTIAARL--HETEIAT--KEQMTEvkKMEFEKLNTSKE 3522
Cdd:COG4913 495 PEHYAAaLRWV-NRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLdfKPHPFRAwlEAELGR--RFDYVCVDSPEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3523 ADDLRKAIT-----------------------------------ELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMT 3567
Cdd:COG4913 570 LRRHPRAITragqvkgngtrhekddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERREA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3568 --VLQQTFLTEKEMLLKKEKL--IEDEKKKLES------QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQ 3637
Cdd:COG4913 650 lqRLAEYSWDEIDVASAEREIaeLEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1655274895 3638 KEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQK 3684
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID 776
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3516-3653 |
4.88e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3516 KLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKskemadaqqkqieremtvLQQTFLTEKEMLLKKEKLIEdEKKKLE 3595
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEAL------------------LKEAEKLKEELEEKKEKLQE-EEDKLL 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 3596 SQFEEEIKKA-KALKDEQD------RQRQQMEEEKLKLKATMDA--ALNKQKEAEKDILNKQKEMQE 3653
Cdd:PRK00409 569 EEAEKEAQQAiKEAKKEADeiikelRQLQKGGYASVKAHELIEArkRLNKANEKKEKKKKKQKEKQE 635
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3521-3681 |
5.06e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3521 KEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQIEREMTVLQQtfltekemllkkekLIEDEKKKLESqfee 3600
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEA--------------RIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3601 eIKKAKALK------DEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLRE 3674
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 1655274895 3675 KLQQMEE 3681
Cdd:COG1579 164 EREELAA 170
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5068-5099 |
5.24e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 5.24e-05
10 20 30
....*....|....*....|....*....|..
gi 1655274895 5068 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 5099
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
1116-1225 |
5.25e-05 |
|
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: 46.50 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1116 QKKTFTKWVN---------KHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARsvrlpreKGRMRFHKLQN 1186
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTI-DERAINK-------KKLTVFTIHEN 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274895 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21292 97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3300-3560 |
5.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3300 QKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKfLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDL 3379
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3380 NQQRTLAEKMLKeKMQAIQEASRLKaeaeMLQRQKDLAQeqAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAE 3459
Cdd:COG4942 100 EAQKEELAELLR-ALYRLGRQPPLA----LLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3460 AEKLKLQVSQLseaqakaeeeakkfkkqadtiAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKAR 3539
Cdd:COG4942 173 RAELEALLAEL---------------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|.
gi 1655274895 3540 LKKEAEEHQNKSKEMADAQQK 3560
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALK 252
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2411-2621 |
5.45e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.22 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2411 SELMTLTSQYIKFITD---TQRRLEDEEKAAE---KLKAEEQKKMAEM---QAELDKQKQLA-----EAHAKAIaKAEKE 2476
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAEAdrqRLEQEKQQQLAAIsgsQSQLESTDQNAletngQAQRDAI-LEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2477 A--QELKLRMQ--EEVSKRETAAVD---------AEKQKQNIQLELHELKNLS-------EQQIKDKSQQVDEALKsrlr 2536
Cdd:NF012221 1617 AvtKELTTLAQglDALDSQATYAGEsgdqwrnpfAGGLLDRVQEQLDDAKKISgkqladaKQRHVDNQQKVKDAVA---- 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2537 ieeeihliriQLETTVKQ----KSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEelKHKSEAER 2612
Cdd:NF012221 1693 ----------KSEAGVAQgeqnQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGE--QDASAAEN 1760
|
....*....
gi 1655274895 2613 KAANEKQKA 2621
Cdd:NF012221 1761 KANQAQADA 1769
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4167-4203 |
5.55e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 5.55e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1655274895 4167 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 4203
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2722-3110 |
5.65e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2722 RQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAK---KRSKAEESALKQRdMAENELERQRRLAESTAQQKLaa 2798
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgQGGLDEEEAFLDR-TAKREERRQKRLQEALERQKE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2799 eqelirlradfdnaeqqrsllEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEa 2878
Cdd:pfam02029 89 ---------------------FDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2879 eaTKLRDLAEEASKLRAIAEEAKHQRqlaEEDAARQRAEAERILKEKlaaisdatRLKTEAEIALKEKEAENERLRRQAE 2958
Cdd:pfam02029 147 --TEVRQAEEEGEEEEDKSEEAEEVP---TENFAKEEVKDEKIKKEK--------KVKYESKVFLDQKRGHPEVKSQNGE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2959 DEAYQRKILEDQANQHKLEIEEKivllKKSSDAEMERQKAIvdDTLKQRRVVEEEirilkLNFEKASSGKLDLELELNKL 3038
Cdd:pfam02029 214 EEVTKLKVTTKRRQGGLSQSQER----EEEAEVFLEAEQKL--EELRRRRQEKES-----EEFEKLRQKQQEAELELEEL 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3039 KNIAEEtqqsklraeeeaeklRRLVLEEEMRRKEAEDKVKKIaaAEEEAARQRKaaqEELDRLQKKADEVRK 3110
Cdd:pfam02029 283 KKKREE---------------RRKLLEEEEQRRKQEEAERKL--REEEEKRRMK---EEIERRRAEAAEKRQ 334
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2400-3098 |
5.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2400 IQEYVTLRTRYSELMTLTSQYIK---FITDTQRRLEDEEK--------AAEKLKAEEQKKMAEMQAELDKQK-------- 2460
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEAlelrrelyTSRRQLAAEQYRLVEMARELAELNeaesdleq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2461 ------------QLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAA---VDAEKQKQNIQLELHELKN-LSE-QQIKDK 2523
Cdd:PRK04863 329 dyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNEVVEEADeqqEENEARAEAAEEEVDELKSqLADyQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2524 SQ----QVDEALKSRLRIEEEIHLIRIQLEttvkqksNAEDELKQLRDRADAA-EKLRKLAQeeaeKLRkqVSEE--TQK 2596
Cdd:PRK04863 409 QQtraiQYQQAVQALERAKQLCGLPDLTAD-------NAEDWLEEFQAKEQEAtEELLSLEQ----KLS--VAQAahSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2597 KRLAEEELKHKSEAERKAANEK-QKALEDLENLRMQAEEAE-RQVKQAEVEKERQIQvahvAAQQSAAAELRSKQMSFAE 2674
Cdd:PRK04863 476 EQAYQLVRKIAGEVSRSEAWDVaRELLRRLREQRHLAEQLQqLRMRLSELEQRLRQQ----QRAERLLAEFCKRLGKNLD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2675 NVSKLEEsLKQEHGTVL--------QLQQDAERLRKQQEDAENAREEAERELEKWRQkANEAL-RLRLQAEE-------- 2737
Cdd:PRK04863 552 DEDELEQ-LQEELEARLeslsesvsEARERRMALRQQLEQLQARIQRLAARAPAWLA-AQDALaRLREQSGEefedsqdv 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2738 -EAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAEneLERQRRLAE--------------------------- 2789
Cdd:PRK04863 630 tEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSE--DPRLNALAErfggvllseiyddvsledapyfsalyg 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2790 -----------STAQQKLAA---------------------------------------------------------EQE 2801
Cdd:PRK04863 708 parhaivvpdlSDAAEQLAGledcpedlyliegdpdsfddsvfsveelekavvvkiadrqwrysrfpevplfgraarEKR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2802 LIRLR------------ADFDNAEQQRsLLEDeLYRLKN-------------EVIAAQQERKQLEDELSKVRSEmdiLIQ 2856
Cdd:PRK04863 788 IEQLRaereelaeryatLSFDVQKLQR-LHQA-FSRFIGshlavafeadpeaELRQLNRRRVELERALADHESQ---EQQ 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2857 LKSRAEKetmsntekSKQLLEAeatkLRDLAEEASKLraiaEEAKHQRQLAEEDAARQRAE-AERILKEKLAAISdatRL 2935
Cdd:PRK04863 863 QRSQLEQ--------AKEGLSA----LNRLLPRLNLL----ADETLADRVEEIREQLDEAEeAKRFVQQHGNALA---QL 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2936 KTEAEiALKEKEAENERLRRQAEDEAYQRKILEDQA--------NQHKLEIEEKIVLLKKSSDAEmERQKAIVDDTLKQR 3007
Cdd:PRK04863 924 EPIVS-VLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfaltevvqRRAHFSYEDAAEMLAKNSDLN-EKLRQRLEQAEQER 1001
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3008 RVVEEEIRILKLNFEKASSGKLDLELELNK----LKNIAEETQQSKLRAEEEAEK---LRRLVLEEEM-----RRKEAED 3075
Cdd:PRK04863 1002 TRAREQLRQAQAQLAQYNQVLASLKSSYDAkrqmLQELKQELQDLGVPADSGAEErarARRDELHARLsanrsRRNQLEK 1081
|
890 900
....*....|....*....|...
gi 1655274895 3076 KVKKIAAAEEEAARQRKAAQEEL 3098
Cdd:PRK04863 1082 QLTFCEAEMDNLTKKLRKLERDY 1104
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
1116-1225 |
5.85e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 46.54 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1116 QKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSVRLPrekgrmrFHKLQN 1186
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTI-DERTINKKKLTP-------FTIQEN 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274895 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21324 97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2799-2949 |
5.96e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2799 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKEtMSNTEKSKQL--L 2876
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEYeaL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2877 EAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRlKTEAEIALKEKEAE 2949
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA-ELEAELEELEAERE 166
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
3091-3470 |
6.32e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.67 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3091 RKAAQEELDRLQKKADEVRK--QKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSmmqNKLKEEYEKAKALA 3168
Cdd:PRK10929 60 RKGSLERAKQYQQVIDNFPKlsAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKS---RQAQQEQDRAREIS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3169 rDAeaakeraereAALLRQQAEEAERQkvaaeqeaanqakaQDDAERLRKdaefEAAKLAQAEAAALKQKQQAdeEMAKH 3248
Cdd:PRK10929 137 -DS----------LSQLPQQQTEARRQ--------------LNEIERRLQ----TLGTPNTPLAQAQLTALQA--ESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3249 K-KLAEQTLKQ-KFQVEQELTKVKLQLEEtdKQKSLLDDELQRLKDEVDDAMRQKAsvEEELfkvkiqmeelmklkvrie 3326
Cdd:PRK10929 186 KaLVDELELAQlSANNRQELARLRSELAK--KRSQQLDAYLQALRNQLNSQRQREA--ERAL------------------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3327 eENQRLMKKDKDNTQKFLVEEAENMKKLAEDaarLSIEAQE----AARLRQIAEDDLNQQRTLAekMLKEKMQ------A 3396
Cdd:PRK10929 244 -ESTELLAEQSGDLPKSIVAQFKINRELSQA---LNQQAQRmdliASQQRQAASQTLQVRQALN--TLREQSQwlgvsnA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3397 IQEASRLKAE--AEMLQRQK---DLAQEQAQKLLEDKQLMQQRLDEE---------TEEYQRSLEAERKRQLEI------ 3456
Cdd:PRK10929 318 LGEALRAQVArlPEMPKPQQldtEMAQLRVQRLRYEDLLNKQPQLRQirqadgqplTAEQNRILDAQLRTQRELlnslls 397
|
410
....*....|....*....
gi 1655274895 3457 -----IAEAEKLKLQVSQL 3470
Cdd:PRK10929 398 ggdtlILELTKLKVANSQL 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3355-3607 |
6.35e-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: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3355 AEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQR 3434
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3435 LDEETEEYqrsleAERKRQLEIIAEAEKLKLQVSQlseaqakaeeeakKFKKQADTIAARLHETEIATKEQMTEVKkmef 3514
Cdd:COG4942 99 LEAQKEEL-----AELLRALYRLGRQPPLALLLSP-------------EDFLDAVRRLQYLKYLAPARREQAEELR---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3515 eklntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQiEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKL 3594
Cdd:COG4942 157 ------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 1655274895 3595 ESQFEEEIKKAKA 3607
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2424-2917 |
6.46e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.80 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2424 ITDTQRRLEDEEKAAEKLKAEEqkkMAEMQAELDKQK----QLAEAHAKAIAKAEKEAQ--ELKLRMQEEVSKRETAAVD 2497
Cdd:PRK10246 389 LTHAEQKLNALPAITLTLTADE---VAAALAQHAEQRplrqRLVALHGQIVPQQKRLAQlqVAIQNVTQEQTQRNAALNE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2498 AEKQKQNIQLELHELKNLSEQQIKDKSQqvdEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRdrADAAEKLRK 2577
Cdd:PRK10246 466 MRQRYKEKTQQLADVKTICEQEARIKDL---EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSR--LDALEKEVK 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2578 LAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAER----------KAANEKQKALEDLENLRMQAEEAERQVKQAEVEKE 2647
Cdd:PRK10246 541 KLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQaltqqwqavcASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2648 RQIQVA-HVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRkqqedaenareeaereleKWRQKAN 2726
Cdd:PRK10246 621 LQGQIAaHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQ------------------SWQQRQN 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2727 EALRLRLQAEEEAHKKSLAQEEAEKQKEEAD------REAKKRSKAEESALKQrdMAENELERQRRLAESTAQQKLAAEQ 2800
Cdd:PRK10246 683 ELTALQNRIQQLTPLLETLPQSDDLPHSEETvaldnwRQVHEQCLSLHSQLQT--LQQQDVLEAQRLQKAQAQFDTALQA 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2801 ELIRLRADFDNA---EQQRSLLEDELYRLKNEVIAAQ----QERKQLEDELSKVRSEMDiliqlksraekeTMSNTEKSK 2873
Cdd:PRK10246 761 SVFDDQQAFLAAlldEETLTQLEQLKQNLENQRQQAQtlvtQTAQALAQHQQHRPDGLD------------LTVTVEQIQ 828
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1655274895 2874 QLLEAEATKLRDLA----EEASKLRAIAEEAKHQRQL-AEEDAARQRAE 2917
Cdd:PRK10246 829 QELAQLAQQLRENTtrqgEIRQQLKQDADNRQQQQALmQQIAQATQQVE 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2760-3437 |
6.56e-05 |
|
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: 49.63 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2760 AKKRSKAEESALKQRDMAENELErqrrlaesTAQQKLAAEQELIRLRA-DFDNAEQQRSLLEDELYRLKNEVIAAQQERK 2838
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELK--------NKEKELKNLDKNLNKDEeKINNSNNKIKILEQQIKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2839 QLEDELSKVRSEMDILIQLKSRAEKEtMSNTEKSKQLLEAEATK----LRDLAEEASKLRAIAEEAKHQRQLAEEDAARQ 2914
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVE-LNKLEKQKKENKKNIDKflteIKKKEKELEKLNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2915 RAEAERILKEKLAAISDATRLKTEAEIaLKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSsdaeme 2994
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT------ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2995 rQKAIVDDTLKQRRVVEE-EIRILKLnfEKASSGKLDLELELNKLKNIAEETQQSKlrAEEEAEKLRRLVLEEEMRRKEA 3073
Cdd:TIGR04523 252 -QTQLNQLKDEQNKIKKQlSEKQKEL--EQNNKKIKELEKQLNQLKSEISDLNNQK--EQDWNKELKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3074 EDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvLAQQKEDSMM 3153
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3154 QNKLKEEYEKAKalardaEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDaefeaaklaqaeaa 3233
Cdd:TIGR04523 406 LNQQKDEQIKKL------QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-------------- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3234 alkQKQQADEEMAKHKKLaEQTLKQKfqvEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDdamrQKASVEEELFKVKI 3313
Cdd:TIGR04523 466 ---LETQLKVLSRSINKI-KQNLEQK---QKELKSKEKELKKLNEEKKELEEKVKDLTKKIS----SLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3314 QME-ELMKLKVRIEEENQRLmkkDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKE 3392
Cdd:TIGR04523 535 EKEsKISDLEDELNKDDFEL---KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1655274895 3393 KMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDE 3437
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2281-2534 |
6.81e-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: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2281 QIDLRQRELDQLgrqlgyyresydwlirwiadakqrQENIQAVpitdSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAK 2360
Cdd:COG4942 21 AAAEAEAELEQL------------------------QQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2361 AYIDIIKDYELQLVAYKAQVEPLTSPLKKTKlDSASDNIIQEYVTlrTRYSELMTLTSQyiKFITDTQRRLEDEEKAAEK 2440
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQK-EELAELLRALYRL--GRQPPLALLLSP--EDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2441 LKaEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNlSEQQI 2520
Cdd:COG4942 148 RR-EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEEL 225
|
250
....*....|....
gi 1655274895 2521 KDKSQQVDEALKSR 2534
Cdd:COG4942 226 EALIARLEAEAAAA 239
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
1113-1224 |
6.84e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 45.72 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1113 DRVQKKTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTLlseRDVARSvrlPREKGRMrfhkLQNVQIA 1190
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDINGC---PKNRSQM----IENIDAC 77
|
90 100 110
....*....|....*....|....*....|....
gi 1655274895 1191 LDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21285 78 LSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2612-2856 |
7.25e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2612 RKAANEKQKALEDLENLRMQAEEAERQvKQAEVEKERQIQVAHVAAQQSAAAELRSKQmsfAENVSKLEESLKQehgtvl 2691
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQKQAEEAKA------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2692 qlQQDAERLRKQQEDAEnareeaerelekwRQKANEALRlrlQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESAL 2771
Cdd:TIGR02794 127 --KQAAEAKAKAEAEAE-------------RKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2772 KQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM 2851
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAII 268
|
....*
gi 1655274895 2852 DILIQ 2856
Cdd:TIGR02794 269 QQAIQ 273
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2532-3093 |
8.04e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2532 KSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKlAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAE 2611
Cdd:PRK01156 149 AQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS-SNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2612 RKAANEKQKALEDLENLRMQAEEAER------------QVKQAEVEKERQIQVAHVAAQQSAAAELRS------------ 2667
Cdd:PRK01156 228 NNAMDDYNNLKSALNELSSLEDMKNRyeseiktaesdlSMELEKNNYYKELEERHMKIINDPVYKNRNyindyfkykndi 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2668 ---KQM---------SFAENVSKLEEsLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELekwrqKANEALRLRLQA 2735
Cdd:PRK01156 308 enkKQIlsnidaeinKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL-----KSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2736 EEEAHKKSLAQEEAEKQKEEADREAKKRSKAE--------ESAL-----KQRDMAENELERQRRLAESTAQQKLA----- 2797
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEinvklqdiSSKVsslnqRIRALRENLDELSRNMEMLNGQSVCPvcgtt 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2798 -AEQELIRLRADFDNaeqQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSE-------------------MDILIQL 2857
Cdd:PRK01156 462 lGEEKSNHIINHYNE---KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEeinksineynkiesaradlEDIKIKI 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2858 KSRAEKETMSNTEKSkqllEAEATKLRDL-AEEASKLRAIAeeakhQRQLAEEDAARQRAEaerilkEKLAAISDATRLK 2936
Cdd:PRK01156 539 NELKDKHDKYEEIKN----RYKSLKLEDLdSKRTSWLNALA-----VISLIDIETNRSRSN------EIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2937 TEAEIALKEKEAENERLRRQAEDEA--YQRKILEDQANQHKLE-IEEKIVLLKKSSDAEMERQKaivddtlkqrrvveee 3013
Cdd:PRK01156 604 QEIEIGFPDDKSYIDKSIREIENEAnnLNNKYNEIQENKILIEkLRGKIDNYKKQIAEIDSIIP---------------- 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3014 irilklNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMR---RKEAEDKVKKIAAAEEEAARQ 3090
Cdd:PRK01156 668 ------DLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRindINETLESMKKIKKAIGDLKRL 741
|
...
gi 1655274895 3091 RKA 3093
Cdd:PRK01156 742 REA 744
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2524-2865 |
8.49e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.19 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2524 SQQVDEALKSRL-RIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEE 2602
Cdd:COG5185 206 SIKESETGNLGSeSTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENAN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2603 ELKHKSEAERKAANEKQKALEDLENLrmqaEEAERQVKQAEVEKERQIQVAHV-AAQQSAAAELRSKQMSFAENVSKLEE 2681
Cdd:COG5185 286 NLIKQFENTKEKIAEYTKSIDIKKAT----ESLEEQLAAAEAEQELEESKRETeTGIQNLTAEIEQGQESLTENLEAIKE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2682 SLKQEHGTVlQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALrlrlqaeeEAHKKSLAQEEAEKQKEEADREAK 2761
Cdd:COG5185 362 EIENIVGEV-ELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEIL--------ATLEDTLKAADRQIEELQRQIEQA 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2762 KRSKAEESalKQRDMAENELERQRRLAESTAQQKLAAEQELI--RLRADFDNAEQQRSLLEDELYRLKNEViaaQQERKQ 2839
Cdd:COG5185 433 TSSNEEVS--KLLNELISELNKVMREADEESQSRLEEAYDEInrSVRSKKEDLNEELTQIESRVSTLKATL---EKLRAK 507
|
330 340
....*....|....*....|....*.
gi 1655274895 2840 LEDELSKVRSEMDILIQLKSRAEKET 2865
Cdd:COG5185 508 LERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2428-2653 |
9.51e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.22 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2428 QRRLEDEEKAAEKLK----AEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQ 2503
Cdd:pfam09787 17 ARILQSKEKLIASLKegsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2504 NIQLELHELKNLSEQQIkdksqqvdeALKSRLRIEEEIHLIRIQLEttvkQKSNAEDelkQLRDRADAAEKLRKLAQeEA 2583
Cdd:pfam09787 86 EEAESSREQLQELEEQL---------ATERSARREAEAELERLQEE----LRYLEEE---LRRSKATLQSRIKDREA-EI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 2584 EKLRKQVSEETQKKrLAEEELKHKSEAERKAANEKQKALEDLE----NLRMQAEEAERQVKQAEVEKERQIQVA 2653
Cdd:pfam09787 149 EKLRNQLTSKSQSS-SSQSELENRLHQLTETLIQKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3156-3363 |
9.61e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.85 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3156 KLKEEYEKAKALARDAEAAKERAEREAALLRQQ-AEEAERQKVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaa 3234
Cdd:pfam05262 185 ALREDNEKGVNFRRDMTDLKERESQEDAKRAQQlKEELDKKQIDADKAQQKADFAQDNADKQRDEVR------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3235 lkQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKqksllDDELQRLKDEVDDAMRQKASVEEelfkvkiQ 3314
Cdd:pfam05262 252 --QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKN-----DEEALKAKDHKAFDLKQESKASE-------K 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655274895 3315 MEElmklkvRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSI 3363
Cdd:pfam05262 318 EAE------DKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSN 360
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2527-2643 |
1.05e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2527 VDEALkSRLRIEeeihliriqLETTVKQKSNAEDELKQLRDRADAAEKLRKLA-QEEAEKLRKQvsEETQKKRLaeEELK 2605
Cdd:COG0542 395 IDEAA-ARVRME---------IDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDE--LAELEEEL--EALK 460
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 2606 HKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAE 2643
Cdd:COG0542 461 ARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELE 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3093-3308 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3093 AAQEELDRLQKKADEVRKQKEEADKEAEKQivAAQQAALKCNMAEQQVQSVLAQQKedsmmQNKLKEEYEKAKalARDAE 3172
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAAL--KKEEKALLKQLAALERRIAALARR-----IRALEQELAALE--AELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3173 AAKERAEREAALLRQQAEEAERQKVAAEQEAANQAK---AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQAdEEMAKHK 3249
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3250 KLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEEL 3308
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4461-4494 |
1.08e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....
gi 1655274895 4461 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPE 4494
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2758-2963 |
1.08e-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: 49.06 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQRDMAEN-----ELERQRRLA---------ESTAQQKLAAeqelirlradfdNAEQQRSLLEDEL 2823
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAaisgsqsqlESTDQNALET------------NGQAQRDAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2824 YRLKNEVIAAQQERKQLEDE-------------------LSKVRSEMDiliqlksRAEKETMSNTEKSKQLLEAEATKLR 2884
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVK 1688
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 2885 DlaeEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 2963
Cdd:NF012221 1689 D---AVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQ 1764
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2459-2614 |
1.14e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2459 QKQLAEAHAKA---IAKAEKEAQELKlrmqeevskretaavdaEKQKQNIQLELHELKNLSEQQIKDKSQQVDEaLKSRL 2535
Cdd:PRK12704 30 EAKIKEAEEEAkriLEEAKKEAEAIK-----------------KEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2536 RIEEEIhlIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQV------SEETQKKRL---AEEELKH 2606
Cdd:PRK12704 92 LQKEEN--LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisglTAEEAKEILlekVEEEARH 169
|
170 180
....*....|....*....|.
gi 1655274895 2607 -------------KSEAERKA 2614
Cdd:PRK12704 170 eaavlikeieeeaKEEADKKA 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2768-3078 |
1.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2768 ESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKV 2847
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2848 RSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLA 2927
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2928 AISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQR 3007
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3008 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVK 3078
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3384-3683 |
1.22e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3384 TLAEKMLKEKMQAIQEASRLKAEA---EMLQRQKDLAQEQAQKLLEDKQLMQQRldEETEEYQRSLEAERKRQLEIIAEA 3460
Cdd:TIGR00618 119 RILAAKKSETEEVIHDLLKLDYKTftrVVLLPQGEFAQFLKAKSKEKKELLMNL--FPLDQYTQLALMEFAKKKSLHGKA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3461 EKLKLQVSQLSEAQAKAEeeakkfkkqaDTIAARLhETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARL 3540
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMP----------DTYHERK-QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3541 KKEAEEHQNKSKEMADaQQKQIEREMTVLQqtFLTEKEMLLKKEKLIEDEKKKLESQFEEEIK----KAKALKDEQDRQR 3616
Cdd:TIGR00618 266 RARIEELRAQEAVLEE-TQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKllmkRAAHVKQQSSIEE 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 3617 QQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQ 3683
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2428-2664 |
1.26e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.79 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2428 QRRLEDEEKAaeklKAEEQKKMAEMQAELDKQkqlAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQL 2507
Cdd:PRK05035 459 QARLEREKAA----REARHKKAAEARAAKDKD---AVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQAR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2508 ELHELKNLSEqQIKDKSQQVDEALKsrlrieeeihliRIQLETTVKQKSNAEDELKQLRDRADAAEklrKLAQEEAEKLR 2587
Cdd:PRK05035 532 ARQAEKQAAA-AADPKKAAVAAAIA------------RAKAKKAAQQAANAEAEEEVDPKKAAVAA---AIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 2588 KQVSEETQKKRLAEEELKhksEAERKAANEKQKALEdLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE 2664
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPK---KAAVAAAIARAKAKK-AEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAE 668
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
3250-3597 |
1.26e-04 |
|
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: 47.64 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3250 KLAEQTLKQKFQVEQELTKVKL---QLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIE 3326
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAAlckKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3327 EENQRLMkkdkdntqkflvEEAENMKKlAEDAARLSIEAQEAARLRQIaEDDLNQQRTLAEKMLKEKMQAiqeASRLKAE 3406
Cdd:pfam09728 81 KQNKKLK------------EESKKLAK-EEEEKRKELSEKFQSTLKDI-QDKMEEKSEKNNKLREENEEL---REKLKSL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3407 AEmlqrQKDLAQEQAQKLLEDKQLMQQRLdeETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSeaqakaeeeakkfkk 3486
Cdd:pfam09728 144 IE----QYELRELHFEKLLKTKELEVQLA--EAKLQQATEEEEKKAQEKEVAKARELKAQVQTLS--------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3487 qadtiaarlhETEIATKEQMTE-VKKM-EFEK-LNTS--------KEADDLRKAITELEKEKARLKKEAEEHQNKSKEMA 3555
Cdd:pfam09728 203 ----------ETEKELREQLNLyVEKFeEFQDtLNKSnevfttfkKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMA 272
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1655274895 3556 DAQQKQIEremtvlqqtfltEKEMLLKKEKLIEDEKKKLESQ 3597
Cdd:pfam09728 273 EERQKLKE------------ELEKLQKKLEKLENLCRALQAE 302
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
1109-1225 |
1.27e-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: 44.75 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1109 EDERdrvqkKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdVARSVRLPREKGRM 1179
Cdd:cd21294 5 EDER-----REFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTI-----DERVLNKPPRKNKP 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1655274895 1180 --RFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21294 75 lnNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3238-3502 |
1.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3238 KQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAmrqkasvEEELFKVKIQMEE 3317
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-------EAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3318 LMklkvrieeenqRLMKKDKDNTQKF-----------LVEEAENMKKLAEDAARLsIEAQEAARlrqiaeDDLNQQRTLA 3386
Cdd:COG3883 91 RA-----------RALYRSGGSVSYLdvllgsesfsdFLDRLSALSKIADADADL-LEELKADK------AELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 EKMLKEKMQAIQEASRLKAEaemLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ 3466
Cdd:COG3883 153 EAKLAELEALKAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655274895 3467 VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIAT 3502
Cdd:COG3883 230 AAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3275-3681 |
1.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3275 ETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELmklkvrieEENQRLMKKDKDNTQKFLVEEAENMKKL 3354
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3355 A---EDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDlaqeqaqklledkqlm 3431
Cdd:PRK02224 254 EtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE---------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3432 qqRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLseaqakaEEEAKKFKKQADTIAARLHETEIATKEQMTEVkk 3511
Cdd:PRK02224 318 --ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEI-- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3512 mefeklntskeaDDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREmTVLQQTFLTEKEMLLKKEKLIEDEK 3591
Cdd:PRK02224 387 ------------EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-AELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3592 KKLESQFEEEIKKAKALkDEQDRQRQQMEEEKLKLKATMDaALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK 3671
Cdd:PRK02224 454 CPECGQPVEGSPHVETI-EEDRERVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
410
....*....|
gi 1655274895 3672 LREKLQQMEE 3681
Cdd:PRK02224 532 IEEKRERAEE 541
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
3505-3684 |
1.35e-04 |
|
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: 48.36 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3505 QMTEvkKMEFEKLNTSKEADDLRkaiTELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKE 3584
Cdd:pfam15964 342 QMTE--EANFEKTKALIQCEQLK---SELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3585 KLIED---EKKKLESQFEEEIKKAKAlkdeqdrqrQQMEEEKL--KLKATMDAALNKQKEAEKDILN-KQKEMQELERKR 3658
Cdd:pfam15964 417 AQVEKvtrEKNSLVSQLEEAQKQLAS---------QEMDVTKVcgEMRYQLNQTKMKKDEAEKEHREyRTKTGRQLEIKD 487
|
170 180
....*....|....*....|....*.
gi 1655274895 3659 LEQERVladeNQKLREKLQQMEEAQK 3684
Cdd:pfam15964 488 QEIEKL----GLELSESKQRLEQAQQ 509
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2768-2958 |
1.46e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2768 ESALKQRDMAENELERQR-RLAESTAQ-QKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELS 2845
Cdd:COG3206 171 EEARKALEFLEEQLPELRkELEEAEAAlEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2846 KVRSEMDILIQlksraeKETMSNTEKSKQLLEAE-ATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAE---RI 2921
Cdd:COG3206 251 SGPDALPELLQ------SPVIQQLRAQLAELEAElAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaelEA 324
|
170 180 190
....*....|....*....|....*....|....*...
gi 1655274895 2922 LKEKLAAISDA-TRLKTEAEiALKEKEAENERLRRQAE 2958
Cdd:COG3206 325 LQAREASLQAQlAQLEARLA-ELPELEAELRRLEREVE 361
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3249-3681 |
1.48e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.42 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3249 KKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQrlkdEVDDAMRQKASVEEELF--------KVKIQMEELMK 3320
Cdd:COG5185 32 SKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLN----YQNDVKKSESSVKARKFlkekkldtKILQEYVNSLI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3321 LKVRIEEENQRLM---KKDKDNTQKFLVEEAENMK--KLAEDAARLSIEAQEAARLRQ-IAEDDLNQQRTLAEKMLKEKM 3394
Cdd:COG5185 108 KLPNYEWSADILIsllYLYKSEIVALKDELIKVEKldEIADIEASYGEVETGIIKDIFgKLTQELNQNLKKLEIFGLTLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3395 QAIQEASRLKAEAEMLQRQKDLAQEQaQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQ 3474
Cdd:COG5185 188 LLKGISELKKAEPSGTVNSIKESETG-NLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3475 AKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAitELEKEKARLKKEAEEHQNKSKEM 3554
Cdd:COG5185 267 LEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAA--EAEQELEESKRETETGIQNLTAE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3555 ADAQQKQIEREMTVLQQTF--LTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKD--------------EQDRQRQQ 3618
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIenIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGyaqeilatledtlkAADRQIEE 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 3619 MEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQE-----RVLADENQKLREKLQQMEE 3681
Cdd:COG5185 425 LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAydeinRSVRSKKEDLNEELTQIES 492
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5342-5378 |
1.60e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.60e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1655274895 5342 DPSEETVPIAGILDTETLEKVSVTEAMHRNLVDNITG 5378
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2784-2966 |
1.67e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2784 QRRLAESTAQQKLAAeqelirlradfdnAEQQRslledelyrlKNEVIAAQQERKQledELSKVRSEMDILIQLKSRAEK 2863
Cdd:COG2268 191 RRKIAEIIRDARIAE-------------AEAER----------ETEIAIAQANREA---EEAELEQEREIETARIAEAEA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2864 ETmsntEKSKQLLEAEATKLRDLAEEASKLRAI---------AEEAKHQRQ--LAEEDAARQRAEAERILKEKLAAisDA 2932
Cdd:COG2268 245 EL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEIAEREREieLQEKEAEREEAELEADVRKPAEA--EK 318
|
170 180 190
....*....|....*....|....*....|....
gi 1655274895 2933 TRLKTEAeialkEKEAENERLRRQAEDEAYQRKI 2966
Cdd:COG2268 319 QAAEAEA-----EAEAEAIRAKGLAEAEGKRALA 347
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3422-3695 |
1.70e-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: 48.15 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3422 QKLLEDKQLMQQRLDEEteEYQRSLEAERKRQLeiIAEAEKLKLQVSQLSEAQAKaeeeakkfkkqaDTIAARLHETEIA 3501
Cdd:pfam05622 3 SEAQEEKDELAQRCHEL--DQQVSLLQEEKNSL--QQENKKLQERLDQLESGDDS------------GTPGGKKYLLLQK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3502 TKEQMTEvkkmEFEKLNTSKeaDDLRKAITELEKEKARLKKEAEEHQNKSKEMAdaqqkQIEREMTVLQQTflteKEMLL 3581
Cdd:pfam05622 67 QLEQLQE----ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEEAQ-----ALKDEMDILRES----SDKVK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3582 KKEKLIEDEKKKLES-----------------------QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALN--- 3635
Cdd:pfam05622 132 KLEATVETYKKKLEDlgdlrrqvklleernaeymqrtlQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKlef 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3636 --KQKEAEKDILNKQKEmqelerkRLEQER-VLADENQKLR-EKLQQMEEAQKSTLITEKHVTV 3695
Cdd:pfam05622 212 eyKKLEEKLEALQKEKE-------RLIIERdTLRETNEELRcAQLQQAELSQADALLSPSSDPG 268
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2828-3079 |
1.72e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2828 NEVIAA-QQERKQLEDELSKVRSemdiliqLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQ--R 2904
Cdd:PRK00409 519 NELIASlEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiiK 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2905 QLAEEDAARQRAEAERILKEKLAAISDATRLKteaEIALKEKEAENERLrrQAEDEAYQRKIledqaNQhkleieeKIVL 2984
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKK---EKKKKKQKEKQEEL--KVGDEVKYLSL-----GQ-------KGEV 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2985 LKKSSDAEmerqkaivddtlkqrrvVEEEIRILKLNfekassgkldleLELNKLKNIAEETQQSKLRAEEEAEKLRRLVL 3064
Cdd:PRK00409 655 LSIPDDKE-----------------AIVQAGIMKMK------------VPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSL 705
|
250
....*....|....*...
gi 1655274895 3065 EEE---MRRKEAEDKVKK 3079
Cdd:PRK00409 706 ELDlrgMRYEEALERLDK 723
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1609-1703 |
1.73e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.86 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1609 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQL---SPISRGKYREYLGRLD 1685
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1655274895 1686 LQYAKLLNSSKSRLRNLD 1703
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2812-2982 |
1.92e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2812 AEQQRSLLEdeLYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKEtMSNTEKSKQLLEAEATKLRDLAEEAS 2891
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2892 KLRAIAEEAKHQRQLAEE--DAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILED 2969
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|...
gi 1655274895 2970 QANQHKLEIEEKI 2982
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5455-5492 |
2.03e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 2.03e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1655274895 5455 QRFLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTA 5492
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2446-2997 |
2.20e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2446 QKKMAEMQAELDKQKQLAEAHAKAI-------------AKAEKEAQELKLRMQE-EVSKRETAAVDAEKQKQNIQL--EL 2509
Cdd:pfam10174 136 RKTLEEMELRIETQKQTLGARDESIkkllemlqskglpKKSGEEDWERTRRIAEaEMQLGHLEVLLDQKEKENIHLreEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2510 HELKNLSEQQIKDKS-QQVDEALKSRL-RIEEEIHLIRIQLETTvkqKSNA-------EDELKQL---RDRAD-AAEKLR 2576
Cdd:pfam10174 216 HRRNQLQPDPAKTKAlQTVIEMKDTKIsSLERNIRDLEDEVQML---KTNGllhtedrEEEIKQMevyKSHSKfMKNKID 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2577 KLAQEEAEK-------------LRKQVSEETQKKRLAEEELKHKSE---------------AERKAA--NEKQKALEDLE 2626
Cdd:pfam10174 293 QLKQELSKKesellalqtkletLTNQNSDCKQHIEVLKESLTAKEQraailqtevdalrlrLEEKESflNKKTKQLQDLT 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2627 NLRMQAEEAERQVKQAEVEKERQIQVAHvAAQQSAAAELRSKQMSFAEN-----------------VSKLEESLKQEHGT 2689
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKINVLQ-KKIENLQEQLRDKDKQLAGLkervkslqtdssntdtaLTTLEEALSEKERI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2690 VlqlqqdaERLRKQQEDAENAREEAERELEKWRQKANEalRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRS--KAE 2767
Cdd:pfam10174 452 I-------ERLKEQREREDRERLEELESLKKENKDLKE--KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSklKSL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2768 ESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRadfdnaeqqrsLLEDELYRLKNEVIAAQQERKQLEDELSKV 2847
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIR-----------LLEQEVARYKEESGKAQAEVERLLGILREV 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2848 RSE-------MDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAER 2920
Cdd:pfam10174 592 ENEkndkdkkIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2921 ilkeklaaisDATRLK-TEAEIALKEKEAENERL----RRQAED------EAYQRKILEDQANQHKLEI--------EEK 2981
Cdd:pfam10174 672 ----------DATKARlSSTQQSLAEKDGHLTNLraerRKQLEEilemkqEALLAAISEKDANIALLELssskkkktQEE 741
|
650
....*....|....*.
gi 1655274895 2982 IVLLKKSSDAEMERQK 2997
Cdd:pfam10174 742 VMALKREKDRLVHQLK 757
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2835-3196 |
2.29e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.22 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2835 QERKQLEDELSKVRSEMDILIQLKS-RAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAAR 2913
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEEReRALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2914 QRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKssdaem 2993
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2994 erqkaivddtlkqrrvveeeirilklnfekassgkldlELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEA 3073
Cdd:pfam13868 183 --------------------------------------EREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3074 EDKVKKIaaaeeeaaRQRKAAQEELdRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvLAQQKEDSMM 3153
Cdd:pfam13868 225 EEAEKKA--------RQRQELQQAR-EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR-RMKRLEHRRE 294
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1655274895 3154 QNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQK 3196
Cdd:pfam13868 295 LEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
3041-3367 |
2.40e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3041 IAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKV---KKIAAAEEEAARQRKAAQEE----LDRLQKKADEVRKQKE 3113
Cdd:pfam02029 1 IEDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEpneHNSYEEDSELKPSGQGGLDEeeafLDRTAKREERRQKRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3114 EADKEAEKQIVAAQQAAL-----KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYE-KAKALARDAEAAKERAEREaallrQ 3187
Cdd:pfam02029 81 EALERQKEFDPTIADEKEsvaerKENNEEEENSSWEKEEKRDSRLGRYKEEETEiREKEYQENKWSTEVRQAEE-----E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3188 QAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQK---QQADEEMAKHKKLAEQTLKQKFQVEQ 3264
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEvksQNGEEEVTKLKVTTKRRQGGLSQSQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3265 ELTKVKLQLeETDKQKSLLDDELQRLKDEVDDAMRQK-ASVEEELFKVKIQMEElmKLKVRIEEENQRlmkkdKDNTQKF 3343
Cdd:pfam02029 236 REEEAEVFL-EAEQKLEELRRRRQEKESEEFEKLRQKqQEAELELEELKKKREE--RRKLLEEEEQRR-----KQEEAER 307
|
330 340
....*....|....*....|....
gi 1655274895 3344 LVEEAENMKKLAEDAARLSIEAQE 3367
Cdd:pfam02029 308 KLREEEEKRRMKEEIERRRAEAAE 331
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2988-3195 |
2.43e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2988 SSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLvLEEE 3067
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-LGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3068 MRRK--------------EAED---------KVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIV 3124
Cdd:COG3883 92 ARALyrsggsvsyldvllGSESfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3125 AAQQAalkcnMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQ 3195
Cdd:COG3883 172 ELEAQ-----QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2503-2658 |
2.43e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2503 QNIQLELHELknlsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLA--- 2579
Cdd:COG1579 13 QELDSELDRL----EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2580 ------QEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLR--MQAEEAERQVKQAEVEKERQIQ 2651
Cdd:COG1579 89 keyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKaeLDEELAELEAELEELEAEREEL 168
|
....*..
gi 1655274895 2652 VAHVAAQ 2658
Cdd:COG1579 169 AAKIPPE 175
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2562-2742 |
2.53e-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: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2562 LKQLRDRADA--AEKLRKLAQ--EEAEKLRKQVSEETQKKrlaeeelkhKSEAERKAANEKQKALEDLENLRMQAEEAER 2637
Cdd:COG2268 176 ITDLEDENNYldALGRRKIAEiiRDARIAEAEAERETEIA---------IAQANREAEEAELEQEREIETARIAEAEAEL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2638 QVKQAEVEKERQIQvahvAAQQSAAAELRSKQMSfaENVSKLEESLKQEHGTVLQlQQDAERLRKQQEDAENAREEAERE 2717
Cdd:COG2268 247 AKKKAEERREAETA----RAEAEAAYEIAEANAE--REVQRQLEIAEREREIELQ-EKEAEREEAELEADVRKPAEAEKQ 319
|
170 180
....*....|....*....|....*.
gi 1655274895 2718 LEKWRQKAN-EALRLRLQAEEEAHKK 2742
Cdd:COG2268 320 AAEAEAEAEaEAIRAKGLAEAEGKRA 345
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
3031-3439 |
2.83e-04 |
|
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: 46.95 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3031 LELELNKLKNiAEETQQSKLRAEEEAEKLRRLvlEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 3110
Cdd:pfam15558 10 AALMLARHKE-EQRMRELQQQAALAWEELRRR--DQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3111 QKEEADKEAEKQIVAAQQAALKCNMAEQQVQsvlAQQKEDSMMQN-KLKEEYEKAKAlardaeaakeraEREAALLRQQA 3189
Cdd:pfam15558 87 KQVIEKESRWREQAEDQENQRQEKLERARQE---AEQRKQCQEQRlKEKEEELQALR------------EQNSLQLQERL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3190 EEAERQKVAAEQEAANQAKAQDDAERLRKDAefeaaklaqaEAAALKQKQQADEEMAKhkklaeQTLKQKFQVEQELTkv 3269
Cdd:pfam15558 152 EEACHKRQLKEREEQKKVQENNLSELLNHQA----------RKVLVDCQAKAEELLRR------LSLEQSLQRSQENY-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3270 klqleetdkqksllddelQRLKDEVDDAMRQKASVEEELFKvkiqmeelmKLKVRIEEENQRLMKKdkdntQKFLVEEAE 3349
Cdd:pfam15558 214 ------------------EQLVEERHRELREKAQKEEEQFQ---------RAKWRAEEKEEERQEH-----KEALAELAD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3350 NMKKLAEDAARLSIEaQEAARLRQIAEDDLNQQRTLAEKMLKE---KMQAIQEASRLKAE-AEMLQRQKDLAQEQAQKLL 3425
Cdd:pfam15558 262 RKIQQARQVAHKTVQ-DKAQRARELNLEREKNHHILKLKVEKEekcHREGIKEAIKKKEQrSEQISREKEATLEEARKTA 340
|
410
....*....|....
gi 1655274895 3426 EDKQLMQQRLDEET 3439
Cdd:pfam15558 341 RASFHMREKVREET 354
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2757-3459 |
2.98e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2757 DREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRL--------RADFDNAEQQRSLLEDELYRLkn 2828
Cdd:pfam10174 44 ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLlqqdfttsPVDGEDKFSTPELTEENFRRL-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2829 eviaaQQERKQLEDELSKVRSEMDILiQLKSRAEKETMSNTEKS-KQLLEAEATKlrdlaeeasKLRAIAEEAKHQRQLA 2907
Cdd:pfam10174 122 -----QSEHERQAKELFLLRKTLEEM-ELRIETQKQTLGARDESiKKLLEMLQSK---------GLPKKSGEEDWERTRR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2908 EEDAARQRAEAERILKEKlaaisdatrlKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLE-----IEEKI 2982
Cdd:pfam10174 187 IAEAEMQLGHLEVLLDQK----------EKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLErnirdLEDEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2983 VLLKKSSDAEMERQKaivdDTLKQRRVV-------EEEIRILKLNFEKASSGKLDLELELNKLKNiaeetQQSKLRAEEE 3055
Cdd:pfam10174 257 QMLKTNGLLHTEDRE----EEIKQMEVYkshskfmKNKIDQLKQELSKKESELLALQTKLETLTN-----QNSDCKQHIE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3056 aeklrrlVLEEEMRRKEaedkvkkiaaaeeeaarQRKAA-QEELDRLQKKADE-----VRKQKEEADKEAEKQIVAAQQA 3129
Cdd:pfam10174 328 -------VLKESLTAKE-----------------QRAAIlQTEVDALRLRLEEkesflNKKTKQLQDLTEEKSTLAGEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3130 ALKcNMAEQQVQSVLAQQKEDSMMQNKLKEE-------YEKAKALARDA----------EAAKERAEREAALLRQQAEEA 3192
Cdd:pfam10174 384 DLK-DMLDVKERKINVLQKKIENLQEQLRDKdkqlaglKERVKSLQTDSsntdtalttlEEALSEKERIIERLKEQRERE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3193 ERQKVAAEQEAANQAK-AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLaEQTLKQKFQ----VEQELT 3267
Cdd:pfam10174 463 DRERLEELESLKKENKdLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-EIAVEQKKEecskLENQLK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3268 KVKlQLEETDKQKSLLDDELQRLKDEV----DDAMRQKASVEEELFKVK-IQMEELMKLKvRIEEENQRLMKKDKDNTQK 3342
Cdd:pfam10174 542 KAH-NAEEAVRTNPEINDRIRLLEQEVarykEESGKAQAEVERLLGILReVENEKNDKDK-KIAELESLTLRQMKEQNKK 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3343 flveeAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMlkekmqaiqeasrlkaeaEMLQRQKDLAQEQAQ 3422
Cdd:pfam10174 620 -----VANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM------------------GALEKTRQELDATKA 676
|
730 740 750
....*....|....*....|....*....|....*..
gi 1655274895 3423 KLLEdkqlMQQRLdEETEEYQRSLEAERKRQLEIIAE 3459
Cdd:pfam10174 677 RLSS----TQQSL-AEKDGHLTNLRAERRKQLEEILE 708
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
3372-3687 |
2.99e-04 |
|
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: 47.48 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3372 RQIAEDDLNQQRTLAEKM-LKEKMQAIQEasrLKAEAEMLQRQkdLAQEQaQKLLEDKQLMQQRLDEEtEEYQRSLEAER 3450
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNaLQEQLQAETE---LCAEAEEMRAR--LAARK-QELEEILHELESRLEEE-EERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3451 KRQLEIIAEAEklklqvSQLSEAQakaeeeakkfkkqadtiAARLH-ETEIATKEqmTEVKKMEFEKLNTSKEADDLRKA 3529
Cdd:pfam01576 99 KKMQQHIQDLE------EQLDEEE-----------------AARQKlQLEKVTTE--AKIKKLEEDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3530 ITELEKEKARLKKEAEEHQNKSKEMADAQQKQiEREMTVLQQTFLTEKEMLLKKEKLiedeKKKLE---SQFEEEIKKAK 3606
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKH-EAMISDLEERLKKEEKGRQELEKA----KRKLEgesTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3607 ALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKrLEQERVLADENQKLREKLQQMEEAQKST 3686
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQED-LESERAARNKAEKQRRDLGEELEALKTE 307
|
.
gi 1655274895 3687 L 3687
Cdd:pfam01576 308 L 308
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2764-3129 |
3.02e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 47.32 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2764 SKAEESALKQRDMAENELER-----QRRLAESTAQQKLAAEQELIRLRAD-FDNAEQQRSLLEDEL-YRLKNEVIAAQQE 2836
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEyLYELNVLKEKSEAELtSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2837 RKQLEDELSKVRSEMDILI---QLKSRAEKET-----MSNTEKSKQLLEAEAtklrDLAEEASKLRAIAEEAKHQRQLAE 2908
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVeeaEKKAKDQKEEdrrnyPTNTYKTLELEIAES----DVEVKKAELELVKEEAKEPRDEEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2909 EDAARQRAEAERILKEKLAAI-SDATRLKTEAE--IALKEKEAENERLRRQAEDEA---YQRKILEDQANQHKLEIEEKi 2982
Cdd:NF033838 206 IKQAKAKVESKKAEATRLEKIkTDREKAEEEAKrrADAKLKEAVEKNVATSEQDKPkrrAKRGVLGEPATPDKKENDAK- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2983 vllkkSSDAEMERQKAIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLE---LELNKLKNIAEETQQSKLRAEEEAEKL 3059
Cdd:NF033838 285 -----SSDSSVGEETLPSPSLKPEKKVAEAEKKVEE--AKKKAKDQKEEDrrnYPTNTYKTLELEIAESDVKVKEAELEL 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3060 rrlvLEEEMRRKEAEDKVKKiaaaEEEAARQRKAAQEELDRLQ---KKADEVRKQK-EEADKEAEKQIVAAQQA 3129
Cdd:NF033838 358 ----VKEEAKEPRNEEKIKQ----AKAKVESKKAEATRLEKIKtdrKKAEEEAKRKaAEEDKVKEKPAEQPQPA 423
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2518-2684 |
3.14e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2518 QQIKDKSQQvdEALKSRLRIEEeihliriQLETTVKQKSNAEDE-LKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQK 2596
Cdd:PRK09510 67 QQQQQKSAK--RAEEQRKKKEQ-------QQAEELQQKQAAEQErLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2597 KRLAEEELKHKSEAERKAANE-KQKALEDlenlrMQAEEAERQVKQAEVEKERQiqvAHVAAQQSAAAELRSKQMSFAEN 2675
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAAaAKKAAAE-----AKKKAEAEAAKKAAAEAKKK---AEAEAAAKAAAEAKKKAEAEAKK 209
|
....*....
gi 1655274895 2676 VSKLEESLK 2684
Cdd:PRK09510 210 KAAAEAKKK 218
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
3261-3350 |
3.17e-04 |
|
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: 45.38 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3261 QVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKiqmeELMKLKVRIEEENQRLMKKDKDNT 3340
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIK----QISANAIELDEENRELREELAELK 145
|
90
....*....|
gi 1655274895 3341 QKFLVEEAEN 3350
Cdd:TIGR04211 146 QENEALEAEN 155
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2826-3127 |
3.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2826 LKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETmsntEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQ 2905
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2906 LAEEDAARQRAEAERILKEKLAAISDATRLK---TEAEIALKEKEAENERLRRQAEDEayQRKILEDQANQHKLEIEEKI 2982
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEaqiAELQSEIAEREEELKELEEQLESL--QEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2983 VLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRL 3062
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3063 VLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQ 3127
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2329-2850 |
3.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2329 KTLKEQLakekKLLEEIeknkdkVDECQKYAKAYIDIikdyeLQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRT 2408
Cdd:COG4913 245 EDAREQI----ELLEPI------RELAERYAAARERL-----AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2409 RYSELMTLTSQYIKFITDTQRRLE----DEEKAAEKLKAEEQKKMAEMQAELDKQKQLAE-------AHAKAIAKAEKEA 2477
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2478 QELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELknlsEQQIkdksqqvdEALKSR-LRIEEEIHLIRIQLETTVKqks 2556
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELREL----EAEI--------ASLERRkSNIPARLLALRDALAEALG--- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2557 NAEDELK------QLRDRA----DAAEK-LRKLA----------------------------QEEAEKLRKQVSEETQKK 2597
Cdd:COG4913 455 LDEAELPfvgeliEVRPEEerwrGAIERvLGGFAltllvppehyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2598 RLAE-----------------------------EELKH-----------KSEAERKAANEKQKALED----------LEN 2627
Cdd:COG4913 535 SLAGkldfkphpfrawleaelgrrfdyvcvdspEELRRhpraitragqvKGNGTRHEKDDRRRIRSRyvlgfdnrakLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2628 LRMQAEEAERQVKQAEvEKERQIQVAHVAAQQSAAAELRSKQMSFAEnvskleESLKQEHGTVLQLQQDAERLRkqqeda 2707
Cdd:COG4913 615 LEAELAELEEELAEAE-ERLEALEAELDALQERREALQRLAEYSWDE------IDVASAEREIAELEAELERLD------ 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2708 enareeaerelekwrqKANEALRlRLQAEEEAHKKSLaqeeaekqkEEADREAKKRSKAEESALKQRDMAENELER-QRR 2786
Cdd:COG4913 682 ----------------ASSDDLA-ALEEQLEELEAEL---------EELEEELDELKGEIGRLEKELEQAEEELDElQDR 735
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 2787 LAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEdelyRLKNEVIAAQQERKQLEDELSKVRSE 2850
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2619-3130 |
3.30e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.55 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2619 QKALEDLENLRMQAEEAERQVKQAEVEK-----ERQIQVAHVAAQQSAAAELRSKQMSFAENVSK----LEESLKQEHGT 2689
Cdd:COG3899 729 ERALELLPPDPEEEYRLALLLELAEALYlagrfEEAEALLERALAARALAALAALRHGNPPASARayanLGLLLLGDYEE 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2690 VLQLQQDAERL--RKQQEDAENAREEAERELEKWRQKANEALRLRLQAEE--EAHKKSLAQEEAEKQKEEADREAKKRSK 2765
Cdd:COG3899 809 AYEFGELALALaeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEagLETGDAALALLALAAAAAAAAAAAALAA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2766 AEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELS 2845
Cdd:COG3899 889 AAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAA 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2846 KVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEK 2925
Cdd:COG3899 969 AAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAA 1048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2926 LAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLK 3005
Cdd:COG3899 1049 LAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAA 1128
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3006 QRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEdkvkkiaaaEE 3085
Cdd:COG3899 1129 ARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLA---------AL 1199
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1655274895 3086 EAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAA 3130
Cdd:COG3899 1200 LALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
1236-1349 |
3.33e-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: 43.64 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1236 DIQVNGQSEDMSAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVA 1314
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274895 1315 EKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3444-3688 |
3.54e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.53 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3444 RSLEAERKRQLEIIAEAEK-LKLQVSQLSEAQAKAEEEAKKFKKQAD-TIAARLHETEIAtkeqmtEVKKMEFEKLNTSK 3521
Cdd:pfam12128 268 KSDETLIASRQEERQETSAeLNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEAL------EDQHGAFLDADIET 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3522 EADDLRKA---ITELEKEKARLKKEAEEHQNKSKEMADAQQK---QIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE 3595
Cdd:pfam12128 342 AAADQEQLpswQSELENLEERLKALTGKHQDVTAKYNRRRSKikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3596 SQFEEEIKKAKA-LKDEQDRQRQQMEEEKLKLKAT----------------MDAALNKQKEAEKDILNKQKEMQELERKR 3658
Cdd:pfam12128 422 SELREQLEAGKLeFNEEEYRLKSRLGELKLRLNQAtatpelllqlenfderIERAREEQEAANAEVERLQSELRQARKRR 501
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655274895 3659 LEQERVLADENQKLRE------KLQQMEEAQKSTLI 3688
Cdd:pfam12128 502 DQASEALRQASRRLEErqsaldELELQLFPQAGTLL 537
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
3489-3632 |
3.65e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.38 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3489 DTIAARLHeTEIATKEQmtevkkmefeklntskEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTV 3568
Cdd:COG0542 396 DEAAARVR-MEIDSKPE----------------ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEA 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3569 LQQTFLTEKEMLlkkeklieDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA 3632
Cdd:COG0542 459 LKARWEAEKELI--------EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
3267-3641 |
3.73e-04 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 46.88 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3267 TKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQ-KASVEEELFKVKIQMEE----LMKLKVRI----EEENQRLmkKDK 3337
Cdd:PTZ00332 174 TQIQNALASTDDQIKTQLAQLEKTNEIQNVAMHDgEMQVAEEQMWTKVQLQErlieLVADKFRLigkcEEENKSF--SKI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3338 DNTQKFLVEEAENMKklaeDAARlsieaqeaaRLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLA 3417
Cdd:PTZ00332 252 HEVQKQANQETSQMK----DAKR---------RLKQRCETDLKHIHDAIQKADLEDAEAMKRYATNKEKSERFIRENEDR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3418 QEQAQKLLEDKQLMQQRLDEETEEyqrsleaERKRQLEIIAEAEKLKLQVSQLseaqakaeeeakkfkkqadtiaarlhe 3497
Cdd:PTZ00332 319 QEEAWNKIQDLERQLQRLGTERFE-------EVKRRIEENDREEKRRVEYQQF--------------------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3498 TEIATKEQmtevKKMEFEKLNTSKeADDLRKAITELEKEKARLKKEaeEHQNKSKEMADAQQKQIEREMTVLQQTFLTEK 3577
Cdd:PTZ00332 365 LEVAGQHK----KLLELTVYNCDL-ALRCTGLVEELVSEGCAAVKA--RHDKTNQDLAALRLQVHKEHLEYFRMLYLTLG 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3578 EMLLKKEKLIEDEKKKLESQ----------FEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAE 3641
Cdd:PTZ00332 438 SLIYKKEKRLEEIDRNIRTThiqlefcvetFDPNAKKHADMKKELYKLRQGVEEELAMLKEKQAQALEMFKESE 511
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
3089-3370 |
3.82e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3089 RQRKAAQEELDRLQKKADEV---------RKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNklke 3159
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAkarfearqaRLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV---- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3160 eyEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAerlRKDAEFEAAKLAQAEAAALKQKQ 3239
Cdd:PRK05035 508 --IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKA---KKAAQQAANAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3240 QADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETD----KQKSLLDDELQRLKDEVDDamrQKASVEEELFKVKIqm 3315
Cdd:PRK05035 583 AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiaraKAKKAEQQANAEPEEPVDP---RKAAVAAAIARAKA-- 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3316 eelmklkvrieeenqrlmKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAAR 3370
Cdd:PRK05035 658 ------------------RKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3005-3342 |
4.39e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3005 KQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAE 3084
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3085 EEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLA--QQKEDSMMQNKLKEEYE 3162
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3163 KAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQAD 3242
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3243 EEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLK 3322
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1655274895 3323 VRIEEENQRLMKKDKDNTQK 3342
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
1111-1231 |
4.58e-04 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 43.05 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1111 ERDRVQKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVlsgdtllserdvarsVRLPREKGRM----------R 1180
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNP--YVNHLYSDLCDALVIFQLYEM---------------TRVPVDWGHVnkppypalggN 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 1181 FHKLQNVQIALDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21329 65 MKKIENCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2567-2910 |
4.59e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2567 DRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENL--RMQAEEAERQVKQAEv 2644
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFldRTAKREERRQKRLQE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2645 EKERQIQVAHVAAQQSAAAELRSKQMSFAENVS-------KLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERE 2717
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEENSSwekeekrDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2718 LEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKA----EESALKQRDMAENELERQRRLAESTAQ 2793
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQngeeEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2794 QKLAAEQELIRLRADFDNAEQQrslledELYRLKNEviaaQQERKQLEDELSKVRSEmdiliQLKSRAEKETMSNTEKSK 2873
Cdd:pfam02029 242 VFLEAEQKLEELRRRRQEKESE------EFEKLRQK----QQEAELELEELKKKREE-----RRKLLEEEEQRRKQEEAE 306
|
330 340 350
....*....|....*....|....*....|....*..
gi 1655274895 2874 QLLEAEATKlRDLAEEASKLRAiaeEAKHQRQLAEED 2910
Cdd:pfam02029 307 RKLREEEEK-RRMKEEIERRRA---EAAEKRQKLPED 339
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4498-4529 |
4.77e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.77e-04
10 20 30
....*....|....*....|....*....|..
gi 1655274895 4498 KLLSAEKAVTGYKDPFTGKTISLFEAMQKDLI 4529
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2426-2648 |
5.08e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2426 DTQRRLEDEEKAAEKLKAEEQKKMAEMQaELDKQKQLAEAHAKAIAKAEKEAQElklrmqEEVSKRETAAVDAEKQKQNI 2505
Cdd:pfam02029 140 YQENKWSTEVRQAEEEGEEEEDKSEEAE-EVPTENFAKEEVKDEKIKKEKKVKY------ESKVFLDQKRGHPEVKSQNG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2506 QLELHELKNLSEQQIKDKSQQVDEALKSRLRIEeeihliriqlettvkqksnAEDELKQLRDRADAAEklrklaQEEAEK 2585
Cdd:pfam02029 213 EEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLE-------------------AEQKLEELRRRRQEKE------SEEFEK 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 2586 LRkqvseetQKKRLAE---EELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKER 2648
Cdd:pfam02029 268 LR-------QKQQEAElelEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
3440-3626 |
5.26e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 46.09 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3440 EEYQRSLEAERKRQLEIIAEaEKLKLQVSQLseaqakaeeeaKKFKKQADTIAARlhETEIATKEQM---TEVKKMEFEK 3516
Cdd:COG4487 25 KQRRAEFEKELAERLADAAK-REAALELAEA-----------KAKAQLQEQVAEK--DAEIAELRARleaEERKKALAVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3517 LNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQK---QIEREmtvLQQTFLTEKEMLLKKEKLIEDEKKK 3593
Cdd:COG4487 91 EEKEKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREaelTVEKE---RDEELDELKEKLKKEEEEKQLAEKS 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1655274895 3594 L-ESQFEEEIKKAK----ALKDEQDRQRQQMEEEKLKL 3626
Cdd:COG4487 168 LkVAEYEKQLKDMQeqieELKRKKEQGSTQLQGEVLEL 205
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3517-3686 |
5.42e-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: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3517 LNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEkemLLKKEKLIEDEKKKLES 3596
Cdd:COG3206 208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3597 QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQ---------ELERKRLEQERVLAD 3667
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpelEAELRRLEREVEVAR 364
|
170 180
....*....|....*....|
gi 1655274895 3668 EN-QKLREKLQQMEEAQKST 3686
Cdd:COG3206 365 ELyESLLQRLEEARLAEALT 384
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2832-3005 |
5.58e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2832 AAQQERKQLEDElskVRSEMDILIqLKSRAEKEtmsntEKSKQLLEAEAtklRDLAEEASKlRAIAEeakhqrqlaeeda 2911
Cdd:PTZ00491 667 AARHQAELLEQE---ARGRLERQK-MHDKAKAE-----EQRTKLLELQA---ESAAVESSG-QSRAE------------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2912 ARQRAEAERIlkeKLAAISDATRLKTEAEIALKEKEAENERLRRQAEdeayqrkiLEDQANQHKLEIEEKivllKKSSDA 2991
Cdd:PTZ00491 721 ALAEAEARLI---EAEAEVEQAELRAKALRIEAEAELEKLRKRQELE--------LEYEQAQNELEIAKA----KELADI 785
|
170
....*....|....*...
gi 1655274895 2992 EMERQKAIVD----DTLK 3005
Cdd:PTZ00491 786 EATKFERIVEalgrETLI 803
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3005-3195 |
5.71e-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: 46.48 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3005 KQRRVVEEEIRILKLNFEKASSGKLDLELELNKlknIAEETQQSKLRAEEEaeklrRLVLEEEMRRKEAEDKVKKiaaae 3084
Cdd:pfam15709 352 RKRREQEEQRRLQQEQLERAEKMREELELEQQR---RFEEIRLRKQRLEEE-----RQRQEEEERKQRLQLQAAQ----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3085 EEAARQRKAAQEELDRLQKKadevrKQKEEADK-EAEKQivaaQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEK 3163
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRK-----KQQEEAERaEAEKQ----RQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|...
gi 1655274895 3164 AKALARDAEAAKERAEREA-ALLRQQAEEAERQ 3195
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLAlEEAMKQAQEQARQ 522
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3803-3836 |
5.92e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.92e-04
10 20 30
....*....|....*....|....*....|....
gi 1655274895 3803 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPE 3836
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
3570-3682 |
6.25e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.70 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3570 QQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKaKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNK-- 3647
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQR-KARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVLQew 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655274895 3648 -QKEMQELERKRLEQERVLADENQKLREKLQQMEEA 3682
Cdd:pfam13904 148 eRKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2941-3214 |
6.70e-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: 46.37 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2941 IALKEKEAENERLRRQAEDEAYQRKILEDQ----ANQHKLEiEEKIVLLK--KSSDAEMER--QKAIVDDTLKQRRVVEE 3012
Cdd:NF012221 1535 VATSESSQQADAVSKHAKQDDAAQNALADKeraeADRQRLE-QEKQQQLAaiSGSQSQLEStdQNALETNGQAQRDAILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3013 EIRILKLNFEKASSGkldleleLNKLKNIAEETQQSKLRAEEE-AEKLRRLVleeemrrKEAEDKVKKIAAAEEEAARQR 3091
Cdd:NF012221 1614 ESRAVTKELTTLAQG-------LDALDSQATYAGESGDQWRNPfAGGLLDRV-------QEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3092 KAaqeelDRLQKKADEVRK------QKEEADKEAEKQIVAAQqaalkcNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAK 3165
Cdd:NF012221 1680 HV-----DNQQKVKDAVAKseagvaQGEQNQANAEQDIDDAK------ADAEKRKDDALAKQNEAQQAESDANAAANDAQ 1748
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3166 ALA-RDAEAAK---ERAEREAALLRQQA-EEAERQKVAAEQEAANQAKAQDDAE 3214
Cdd:NF012221 1749 SRGeQDASAAEnkaNQAQADAKGAKQDEsDKPNRQGAAGSGLSGKAYSVEGVAE 1802
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3497-3655 |
6.84e-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: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3497 ETEIATKEQMTEVKKMEFEKlNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQqkQIEREMTVLQQTFLTE 3576
Cdd:COG2268 211 ETEIAIAQANREAEEAELEQ-EREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIA--EANAEREVQRQLEIAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3577 KEmllKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA-ALNKQKEAEKDILNKQKEMQELE 3655
Cdd:COG2268 288 RE---REIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAeGKRALAEAWNKLGDAAILLMLIE 364
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2770-3076 |
7.22e-04 |
|
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: 46.05 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2770 ALKQRDMAENELERQRRLAE---STAQQKLAAEQELIR--LRADFDNAEQQRSLLEDELYRLKNEVIAAQQER----KQL 2840
Cdd:pfam15964 354 ALIQCEQLKSELERQKERLEkelASQQEKRAQEKEALRkeMKKEREELGATMLALSQNVAQLEAQVEKVTREKnslvSQL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2841 EDELSKVRS-EMD---ILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLA---EEASKLRAIAEEAKHQRQLAEEDAAR 2913
Cdd:pfam15964 434 EEAQKQLASqEMDvtkVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAAR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2914 QRAEAERIlkeklaaisdaTRLKTEAEIALKEKEAENERLRRQAEDEAyqrKILEDQANQHKLEIEEKIVLLKKSSDAEM 2993
Cdd:pfam15964 514 AREECLKL-----------TELLGESEHQLHLTRLEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTV 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2994 ERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkldlelelNKLKNIAEETQQSKLRAEEEAEKLRRlvleeemRRKEA 3073
Cdd:pfam15964 580 NEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT----------QKSRSEVEQLSQEKEYLQDRLEKLQK-------RNEEL 642
|
...
gi 1655274895 3074 EDK 3076
Cdd:pfam15964 643 EEQ 645
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
338-613 |
8.11e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.06 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 338 IKATAESDGVQSHVGITTAAVQSTTvlTAPITKKTvnkdviEEKAKEAIAHEVKSTELKSTVETPAKMKPQAVATVASVQ 417
Cdd:pfam05109 405 ITRTATNATTTTHKVIFSKAPESTT--TSPTLNTT------GFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSP 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 418 ESYDTNDTSTPVITKPVKEEKAKKKKATEESVKLAEVKIPGQEKATKTDKVSVPTKAKPGSTTGKPVVSDNVETPKvvqe 497
Cdd:pfam05109 477 TPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPT---- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 498 PSDATPTSVNISEKPKSEV--LSKAAESSILEVTTSVRTGLTSSRTNAevvQVATDKTTIKEKRTTQDVMTlthvekdge 575
Cdd:pfam05109 553 PNATSPTPAVTTPTPNATIptLGKTSPTSAVTTPTPNATSPTVGETSP---QANTTNHTLGGTSSTPVVTS--------- 620
|
250 260 270
....*....|....*....|....*....|....*...
gi 1655274895 576 iapeDPKDPTPAPPSVQEDATTYHKSQNDVGIEAVKET 613
Cdd:pfam05109 621 ----PPKNATSAVTTGQHNITSSSTSSMSLRPSSISET 654
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3024-3241 |
8.21e-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: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3024 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLrrlvlEEEMRRKEAEdkvkkiaaaeeeaarqRKAAQEELDRLQK 3103
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-----NEEYNELQAE----------------LEALQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3104 KADEVRKQKEEADKEAEKQIVAAQQAALKCNMAE---------------QQVQSVLAQQKEDSMMQNKLKEEYEKAKAla 3168
Cdd:COG3883 73 EIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKA-- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 3169 rDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQA 3241
Cdd:COG3883 151 -ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
3038-3192 |
8.30e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.31 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3038 LKNIAEETQQSKLRAEEEAEKLRRlvlEEEMRRKEAEDKVKkiaaaeeeaarqrkaaqeelDRLQKKADEVRKQKEEADK 3117
Cdd:pfam13904 61 LAAKQRQRQKELQAQKEEREKEEQ---EAELRKRLAKEKYQ--------------------EWLQRKARQQTKKREESHK 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3118 EaekqiVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARdaeaAKERAEREAALLRQQAEEA 3192
Cdd:pfam13904 118 Q-----KAAESASKSLAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQR----EQLKKEEEEQERKQLAEKA 183
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
3387-3674 |
8.56e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 EKMLKEKMQAIQEaSRLKAEAEMLQRQKDLAQEQAqkllEDKQLMQQRLDEETEEYQRSLEAERKRQLEI----IAEAEK 3462
Cdd:pfam02029 61 EEAFLDRTAKREE-RRQKRLQEALERQKEFDPTIA----DEKESVAERKENNEEEENSSWEKEEKRDSRLgrykEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3463 LKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVK-KMEFEKLNTSKEADDLRKAITELEKEKARLK 3541
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKiKKEKKVKYESKVFLDQKRGHPEVKSQNGEEE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3542 KEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKL-ESQFEEEIKKAKaLKDEQDRQRQQME 3620
Cdd:pfam02029 216 VTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrQKQQEAELELEE-LKKKREERRKLLE 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 3621 EEKLKLKAtmDAALNKQKEAEKdilnKQKEMQELERKRLEQervlADENQKLRE 3674
Cdd:pfam02029 295 EEEQRRKQ--EEAERKLREEEE----KRRMKEEIERRRAEA----AEKRQKLPE 338
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3503-3613 |
8.57e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3503 KEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEkemllK 3582
Cdd:PRK00409 530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS-----V 604
|
90 100 110
....*....|....*....|....*....|.
gi 1655274895 3583 KEKLIEDEKKKLESQFEEEIKKAKALKDEQD 3613
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2408-2645 |
8.62e-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: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2408 TRYSELMtltSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELKLRMQEE 2487
Cdd:cd16269 44 AHYEEQM---EQRVQLPTETLQELLDLHAACEKEALEVFMKRSFKDEDQKFQKKLME-------QLEEKKEEFCKQNEEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2488 VSKRETAAVDA------EKQKQNI-------QLELHELKNLSE--QQIKDKSQQVDEALKSRLR----IEEEIHLiriql 2548
Cdd:cd16269 114 SSKRCQALLQElsapleEKISQGSysvpggyQLYLEDREKLVEkyRQVPRKGVKAEEVLQEFLQskeaEAEAILQ----- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2549 etTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVseETQKKRLAE--EELKHKSEAERK-AANEKQKALEDL 2625
Cdd:cd16269 189 --ADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL--EDQERSYEEhlRQLKEKMEEEREnLLKEQERALESK 264
|
250 260
....*....|....*....|..
gi 1655274895 2626 --ENLRMQAEEAERQVKQAEVE 2645
Cdd:cd16269 265 lkEQEALLEEGFKEQAELLQEE 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2911-3146 |
8.93e-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: 45.53 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2911 AARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANqhklEIEEKIVLLKKSSD 2990
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2991 AEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQqsklraeEEAEKLRRlvleeemRR 3070
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRA-------DL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 3071 KEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKadevRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQ 3146
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
3491-3697 |
9.08e-04 |
|
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: 45.62 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3491 IAARLHETEIATKEQMTEVKKMEFEklNTSKEADDLRKAITEL----EKEKaRLKKEAEEHQNKSKEM---ADAQQKQIE 3563
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENLELD--EAEEALEEIEERIDQLydllEKEV-DAKKYVEKNLPEIEDYlehAEEQNKELK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3564 REMTVLQQTF-LTEKEmlLKKEKLIEDEKKKLESQFEEEIKKAK-------ALKDEQDRQRQQM---EEEKLKLKATMDA 3632
Cdd:pfam06160 312 EELERVQQSYtLNENE--LERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILEQLeeiEEEQEEFKESLQS 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3633 ALNKQKEAEKDILNKQKEMQELERkRLEQER-------------VLADENQKLREKLQQ----MEEAQKSTLITEKHVTV 3695
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKR-LVEKSNlpglpesyldyffDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDT 468
|
..
gi 1655274895 3696 VE 3697
Cdd:pfam06160 469 LY 470
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
1117-1194 |
1.01e-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: 41.88 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 1117 KKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTlLSERDVARSVRLPRekgrmrfHKLQNVQIALDFL 1194
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEK-LEVPEVAQSEEGQK-------QKLAVVLACVNFL 72
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2444-2827 |
1.01e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2444 EEQKKMAEMQAELDKQKqlaeAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELH--ELKNLSEQQIK 2521
Cdd:pfam13868 12 NSKLLAAKCNKERDAQI----AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYrqELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2522 DKSQQVDEALKSRLRIEEEIHLIriqlettvkqksnaedelkQLRDRADAAEKLRKlaQEEAEKLRKQVSEETQKKRLAE 2601
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERI-------------------QEEDQAEAEEKLEK--QRQLREEIDEFNEEQAEWKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2602 EElkhKSEAERKAANEKQKAledlenlrMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSkqmsfaenvsklee 2681
Cdd:pfam13868 147 KE---EEREEDERILEYLKE--------KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA-------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2682 slkqehgtvlqlQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLaqeeaeKQKEEADREAK 2761
Cdd:pfam13868 202 ------------ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRL------AEEAEREEEEF 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 2762 KRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLK 2827
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5350-5381 |
1.12e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.62 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|..
gi 1655274895 5350 IAGILDTETLEKVSVTEAMHRNLVDNITGQRL 5381
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2310-2536 |
1.14e-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: 45.14 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2310 IADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKK 2389
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2390 TK------LDSASDNIIQEYVTLR---------TRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQA 2454
Cdd:COG4942 102 QKeelaelLRALYRLGRQPPLALLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2455 ELDKQKQlaeahakAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSR 2534
Cdd:COG4942 182 ELEEERA-------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
..
gi 1655274895 2535 LR 2536
Cdd:COG4942 255 LP 256
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2798-3195 |
1.17e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2798 AEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDElsKVRSEMDILIQLKsraEKETMSNTEKSKQLLE 2877
Cdd:COG5185 168 LTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETG--NLGSESTLLEKAK---EIINIEEALKGFQDPE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2878 AEATKLRDLAEEASKLRAIAEEAKhqrqlaeEDAARQRAEAERilkeklaaisdatRLKTEAEIALKEKEAENERLRRQA 2957
Cdd:COG5185 243 SELEDLAQTSDKLEKLVEQNTDLR-------LEKLGENAESSK-------------RLNENANNLIKQFENTKEKIAEYT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2958 EDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIR----------ILKLNFEKASSG 3027
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienivgevELSKSSEELDSF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3028 KLDLElelNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADE 3107
Cdd:COG5185 383 KDTIE---STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3108 VRKQKEEadkeaEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQ 3187
Cdd:COG5185 460 ESQSRLE-----EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG 534
|
....*...
gi 1655274895 3188 QAEEAERQ 3195
Cdd:COG5185 535 YAHILALE 542
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3842-3872 |
1.19e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|.
gi 1655274895 3842 LSAEKAVVGYKDPYSGGKISVFEAMKKGLMD 3872
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3240-3469 |
1.19e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3240 QADEEMAKHKKLAEQTL---KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQ---KASVEEELFKVKI 3313
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlsTLSLRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3314 QMEELMKLKVRIEEENQRLMkkdkdnTQKFLVEEA-----ENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEK 3388
Cdd:PRK11281 133 TLDQLQNAQNDLAEYNSQLV------SLQTQPERAqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3389 MLKEKMQAIQEASRLKaeaEMLQRQKDLAQEQAQKLLEDKQLMQ-----QRLD--EET-EEYQRSLEAERKRQLEIIAEA 3460
Cdd:PRK11281 207 QNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTlsEKTvQEAQSQDEAARIQANPLVAQE 283
|
....*....
gi 1655274895 3461 EKLKLQVSQ 3469
Cdd:PRK11281 284 LEINLQLSQ 292
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3089-3195 |
1.25e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3089 RQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvlAQQKEDSMMQNKLKEEYEKA-KAL 3167
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADT--SSPKEDKQVAENQKREIEKAqIEI 290
|
90 100
....*....|....*....|....*...
gi 1655274895 3168 ARDAEAAKERAEREAALLRQQAEEAERQ 3195
Cdd:pfam05262 291 KKNDEEALKAKDHKAFDLKQESKASEKE 318
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2431-2703 |
1.27e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.23 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2431 LEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDA---EKQKQNIQ 2506
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAmglQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2507 LELheLKNLSEQQ-----IKDKSQQVDE-------------ALKSRLRIEEEIHLIRIQLETTVKQ---KSNAEDELKQL 2565
Cdd:PLN03229 493 EEF--SKANSQDQlmhpvLMEKIEKLKDefnkrlsrapnylSLKYKLDMLNEFSRAKALSEKKSKAeklKAEINKKFKEV 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2566 RDRADAAEKLRKLAQEEAEKlrKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVK----Q 2641
Cdd:PLN03229 571 MDRPEIKEKMEALKAEVASS--GASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPppnlQ 648
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 2642 AEVEK---------ERQIQVAHVAA-----QQSAAAELRSKQMSFAENVSKLEESLKQEHGTVL---QLQQDAERLRKQ 2703
Cdd:PLN03229 649 EKIESlneeinkkiERVIRSSDLKSkiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALnssELKEKFEELEAE 727
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4131-4163 |
1.35e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|...
gi 1655274895 4131 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPE 4163
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3394-3597 |
1.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3394 MQAIQE--ASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQR---SLEAERKRQLEIIAEAEKLKLQVS 3468
Cdd:COG4717 40 LAFIRAmlLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqeELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3469 QLSEAQAKAEEEAKKFKKQA--DTIAARLHETEiatkEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEE 3546
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAelAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 3547 HQNKSKEMADAQQKQIEREMTVLQQT--FLTEKEMLLKKEKLIEDEKKKLESQ 3597
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEEleELEEELEQLENELEAAALEERLKEA 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2640-2867 |
1.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2640 KQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELE 2719
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2720 KWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAE 2799
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2800 QELIRLRADFDNAEQQRsllEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMS 2867
Cdd:COG4942 181 AELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2653-2900 |
1.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2653 AHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERelekwRQKANEALRLR 2732
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-----ELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2733 LQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMaeNELERQRRLAESTAQqklAAEQELIRLRADFDNA 2812
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAP---ARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2813 EQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRsemDILIQLKSRAEKEtmsntEKSKQLLEAEATKLRDLAEEASK 2892
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQ---KLLARLEKELAEL-----AAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1655274895 2893 LRAIAEEA 2900
Cdd:COG4942 235 EAAAAAER 242
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2416-2975 |
1.46e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2416 LTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKM------AEMQAELDKQKQLAEAHAKAIAKAEKEAQEL-------KL 2482
Cdd:PRK10246 213 LTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLnwltrlDELQQEASRRQQALQQALAAEEKAQPQLAALslaqparQL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2483 RMQEEVSKRETAAVDAekqkqniqlelhelknlSEQQIKDKSQQVDEALKSRLRIEeeihliriqlETTVKQKSNAEDEL 2562
Cdd:PRK10246 293 RPHWERIQEQSAALAH-----------------TRQQIEEVNTRLQSTMALRARIR----------HHAAKQSAELQAQQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2563 KQLRDRADAAEKLRKLAQEEA---EKLRKQVSEETQKKRLAEEELkhkseaerkAANEKQKALEDLeNLRMQAEEaerqv 2639
Cdd:PRK10246 346 QSLNTWLAEHDRFRQWNNELAgwrAQFSQQTSDREQLRQWQQQLT---------HAEQKLNALPAI-TLTLTADE----- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2640 kqaevekerqiqVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenareeAERELE 2719
Cdd:PRK10246 411 ------------VAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAA----------LNEMRQ 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2720 KWRQKANEALRLRLQAEEEAHKKSLAQEEAEKqkeeadrEAKKR----SKAEESALKQRDMAENELERQRRLAESTAQQK 2795
Cdd:PRK10246 469 RYKEKTQQLADVKTICEQEARIKDLEAQRAQL-------QAGQPcplcGSTSHPAVEAYQALEPGVNQSRLDALEKEVKK 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2796 LAAEQELIRLRADFDNAEQQR------SLLEDE--LYRLKNEVIA-----------------AQQERKQLEDELSKvRSE 2850
Cdd:PRK10246 542 LGEEGAALRGQLDALTKQLQRdeseaqSLRQEEqaLTQQWQAVCAslnitlqpqddiqpwldAQEEHERQLRLLSQ-RHE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2851 MDILIQLKSRAEKETMSNTEKSKQLLEAE----ATKLRDLAEEASKLRAIAEEAKH-QRQLAEEDAARQRAEAERILKEK 2925
Cdd:PRK10246 621 LQGQIAAHNQQIIQYQQQIEQRQQQLLTAlagyALTLPQEDEEASWLATRQQEAQSwQQRQNELTALQNRIQQLTPLLET 700
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2926 LAAiSDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHK 2975
Cdd:PRK10246 701 LPQ-SDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQK 749
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2208-2347 |
1.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2208 DVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKAsavsdkmsrvhserDAELDQHRQHLSSLQDRWKAVFTQIDLRQR 2287
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEEL--------------EAELEELEEELDELKGEIGRLEKELEQAEE 727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2288 ELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEK 2347
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2421-2509 |
1.52e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2421 IKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKR-ETAAVDA 2498
Cdd:COG0711 26 LKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEaRAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIiAQAEAEI 105
|
90
....*....|.
gi 1655274895 2499 EKQKQNIQLEL 2509
Cdd:COG0711 106 EQERAKALAEL 116
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3499-3690 |
1.59e-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: 45.06 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3499 EIATKEQMTEVKKMEFEKLNTSKE-ADDLRKAITELEKEKARLKKEaeehQNKSKEMADAQQKQIEREMTVL---QQTFL 3574
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEEnIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELlkeKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3575 TEKEMLLKKEKLIEDEKKKLESQFEEEIK----KAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE 3650
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655274895 3651 MQELERKRLEQE---RVLADENQKLREKLQQmEEAQKSTLITE 3690
Cdd:TIGR02169 317 LEDAEERLAKLEaeiDKLLAEIEELEREIEE-ERKRRDKLTEE 358
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2587-2794 |
1.60e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2587 RKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEaERQVKQAEVEKERQIQVAHVAAQQSAAAELR 2666
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEE-QRRLQQEQLERAEKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2667 SKQMSFAENVSKLEESLKQEHgtvLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEE----EAHKK 2742
Cdd:pfam15709 391 LRKQRLEEERQRQEEEERKQR---LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEmqlaEEQKR 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 2743 SLAQEEAEK---QKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQ 2794
Cdd:pfam15709 468 LMEMAEEERleyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2539-2649 |
1.61e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2539 EEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQ----------------KKRLAEE 2602
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQeaknlpkpadtsspkeDKQVAEN 278
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655274895 2603 ElkhKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQ 2649
Cdd:pfam05262 279 Q---KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK 322
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1118-1249 |
1.69e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.93 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1118 KTFTKWVNKHLIKSQrhVTDLYEDLRDGhnlISLLEVLSGDTLLSERDVARSVRLPREKGRM-RFHKLQNVQIALDFLRH 1196
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRFKAFENENYAVDLGIT 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 1197 RQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQVSSS--ISDIQVNGQSEDMSAK 1249
Cdd:COG5069 457 EGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKDGcgLSDSDLCAWLGSLGLK 517
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2634-2987 |
1.76e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2634 EAERQVKQAEVEKERQIQVAHVAAQQSAAA--ELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQ---QEDAE 2708
Cdd:pfam13868 10 ELNSKLLAAKCNKERDAQIAEKKRIKAEEKeeERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQieeREQKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2709 NAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLA 2788
Cdd:pfam13868 90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2789 ESTAQQ---KLAAEQELIRLRADFDNAEQQRslleDELYRLKNEVIAAQQERKQLEDElskvrsemdiliqlKSRAEKET 2865
Cdd:pfam13868 170 EREAEReeiEEEKEREIARLRAQQEKAQDEK----AERDELRAKLYQEEQERKERQKE--------------REEAEKKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2866 MSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKhqRQLAEEDAARQRAEAERILKeklaaisdatRLKTEAEIALKE 2945
Cdd:pfam13868 232 RQRQELQQAREEQIELKERRLAEEAEREEEEFERML--RKQAEDEEIEQEEAEKRRMK----------RLEHRRELEKQI 299
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1655274895 2946 KEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKK 2987
Cdd:pfam13868 300 EEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2255-2577 |
1.81e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2255 SERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQ 2334
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE----KLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2335 LAKEKKLLEEIEKNKDKVDECQKyakayidiikdyELQLVAYKAQVEPLtsPLKKTKldsasdniiqeyvtlrtryselm 2414
Cdd:COG1340 94 LDELRKELAELNKAGGSIDKLRK------------EIERLEWRQQTEVL--SPEEEK----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2415 tltsQYIKFITDTQRRLEDEEKAAEKlkaeeQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETA 2494
Cdd:COG1340 137 ----ELVEKIKELEKELEKAKKALEK-----NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADEL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2495 AVDAEkqkqniqlELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDElkqlRDRADAAEK 2574
Cdd:COG1340 208 RKEAD--------ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE----EKAEEIFEK 275
|
...
gi 1655274895 2575 LRK 2577
Cdd:COG1340 276 LKK 278
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2490-2696 |
1.82e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2490 KRETAAVDAEKQKQNIQLELH-----ELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQ 2564
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYnknieEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2565 LRD-RADAAEKLRKLAQEEA----------------------EKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKA 2621
Cdd:PHA02562 260 LNTaAAKIKSKIEQFQKVIKmyekggvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2622 LE---DLENLRMQAEEAERQVKQAEVEKERqIQVAHVaaqqSAAAELRSKQMSFAENVSKLEESLKQ--EHGTVLQLQQD 2696
Cdd:PHA02562 340 LElknKISTNKQSLITLVDKAKKVKAAIEE-LQAEFV----DNAEELAKLQDELDKIVKTKSELVKEkyHRGIVTDLLKD 414
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3238-3685 |
1.82e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3238 KQQADEEMAKHKkLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEE 3317
Cdd:PRK01156 203 KKQIADDEKSHS-ITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEER 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3318 LMKL------KVRIEEENQRLMKKDKDNTQKFLV-------EEAENMKKLAEDAARLSIEAQEAARLrqiaeDDLNQQRT 3384
Cdd:PRK01156 282 HMKIindpvyKNRNYINDYFKYKNDIENKKQILSnidaeinKYHAIIKKLSVLQKDYNDYIKKKSRY-----DDLNNQIL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3385 LAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLE--------------AER 3450
Cdd:PRK01156 357 ELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQdisskvsslnqrirALR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3451 KRQLEIIAEAEKLKLQ----VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEqmTEVKKMEFEKLNTSKEADDL 3526
Cdd:PRK01156 437 ENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKD--IDEKIVDLKKRKEYLESEEI 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3527 RKAITELEKEKArLKKEAEEHQNKSKEMADAQQK--QIEREMTVLQQTFLTEKEM----LLKKEKLIEDEkkKLESQFEE 3600
Cdd:PRK01156 515 NKSINEYNKIES-ARADLEDIKIKINELKDKHDKyeEIKNRYKSLKLEDLDSKRTswlnALAVISLIDIE--TNRSRSNE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3601 eikKAKALKDEQDRQrQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADenqkLREKLQQME 3680
Cdd:PRK01156 592 ---IKKQLNDLESRL-QEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN----YKKQIAEID 663
|
....*
gi 1655274895 3681 EAQKS 3685
Cdd:PRK01156 664 SIIPD 668
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2359-2591 |
1.94e-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: 44.37 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2359 AKAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKldSASDNIIQEYVTLRTRYSELMTL---TSQYIKFITDTQRRLEDEE 2435
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALK--KEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2436 KAAEKLKAEEQKKMAEMQAELdkQKQLAEAHAKAIAKAEKEAQELK-LRMQEEVSKRETAAVDAEKQKQNiqlELHELKN 2514
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLA---ELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2515 LSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLR---DRADAAekLRKLAQEEAEKLRKQVS 2591
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaEELEAL--IARLEAEAAAAAERTPA 245
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2559-2698 |
1.94e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2559 EDELKQLRDRADAAEKLRKlaqeEAEKLRKQVSEetQKKRLAEEELKHKSEAERKA----ANEKQKALEDLENLRMQAEE 2634
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEELEE--KKEKLQEEEDKLLEEAEKEAqqaiKEAKKEADEIIKELRQLQKG 599
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2635 AERQVKQAEVEKERQiqvaHVAAQQSAAAELRSKQMSFAENVSKLEE----SLKQEhGTVLQLQQDAE 2698
Cdd:PRK00409 600 GYASVKAHELIEARK----RLNKANEKKEKKKKKQKEKQEELKVGDEvkylSLGQK-GEVLSIPDDKE 662
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
2506-2703 |
2.02e-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: 44.65 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2506 QLELHELKNLSEQQIKdKSQQVDEAlksrlrIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADA-AEKLRKlAQEEAE 2584
Cdd:pfam10168 535 QLLSRATQVFREEYLK-KHDLAREE------IQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKlAEKYEE-IKDKQE 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2585 KLRKQVSEETQkkrLAEEELKHKSEAERKAANEkqkaledLENLRMQAEEAERQVKQAEVEKERQIQvaHVAAQQSAAae 2664
Cdd:pfam10168 607 KLMRRCKKVLQ---RLNSQLPVLSDAEREMKKE-------LETINEQLKHLANAIKQAKKKMNYQRY--QIAKSQSIR-- 672
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655274895 2665 lRSKQMSFAENVSK-LEESLKQEHGTVLQLQQDAERLRKQ 2703
Cdd:pfam10168 673 -KKSSLSLSEKQRKtIKEILKQLGSEIDELIKQVKDINKH 711
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3877-3913 |
2.03e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 2.03e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1655274895 3877 IRVLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEM 3913
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2310-2526 |
2.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2310 IADAKQRQENIQAvpitdskTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEpltsplkk 2389
Cdd:COG3883 25 LSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2390 tkldsasDNIIQEYVTLRTRYSELMTLTSQ----------YIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQ 2459
Cdd:COG3883 90 -------ERARALYRSGGSVSYLDVLLGSEsfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 2460 KQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQ 2526
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2471-2742 |
2.08e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2471 AKAEKEAQELKlRMQEEVSKRETAAvdAEKQKQNIQLeLHELKNlSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLET 2550
Cdd:PRK11637 40 AHASDNRDQLK-SIQQDIAAKEKSV--RQQQQQRASL-LAQLKK-QEEAISQASRKLRETQNTLNQLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2551 TVKQKSNAEDEL-KQLrdraDAAEKlrklaQEEAEKLRKQVS-EETQKKRLAEEELKHKSEAERKAANEKQKALEDLenl 2628
Cdd:PRK11637 115 LEQQQAAQERLLaAQL----DAAFR-----QGEHTGLQLILSgEESQRGERILAYFGYLNQARQETIAELKQTREEL--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2629 rmQAEEAERQVKQAEvekerqiQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedae 2708
Cdd:PRK11637 183 --AAQKAELEEKQSQ-------QKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDS----- 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655274895 2709 narEEAERELEKWR--QKANEALRLRlQAEEEAHKK 2742
Cdd:PRK11637 249 ---IARAEREAKARaeREAREAARVR-DKQKQAKRK 280
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
3136-3683 |
2.10e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3136 AEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANqakaQDDAER 3215
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL----REQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3216 LRkdaefeaaklaqaeaaalkQKQQADEEMAKHKKLAEQTLKQKFQV----EQELTKVKLQLEETDKQKSLLDDELQRLK 3291
Cdd:pfam05557 78 NR-------------------LKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3292 dEVDDAMRQKASVEEELFK-VKIQMEELMKLKVRIEEENQRLMKKDKDNtqkflvEEAENMKklaedaarlsieaqeaAR 3370
Cdd:pfam05557 139 -ERLDLLKAKASEAEQLRQnLEKQQSSLAEAEQRIKELEFEIQSQEQDS------EIVKNSK----------------SE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3371 LRQIAEDDLNQQRTLAE-KMLKEkmqAIQEASRLKAEAEMLQR---QKDLAQEQAQKLLEDKQLMQQRLDEETEEYQ--- 3443
Cdd:pfam05557 196 LARIPELEKELERLREHnKHLNE---NIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSWVKLAQdtg 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3444 ---RSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTS 3520
Cdd:pfam05557 273 lnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3521 KEADDLRKAITELEKE---------KARLKKEAE----EHQNKSKEMaDAQQKQIEREMTVLQQTFLT-EKEMLLKKEKL 3586
Cdd:pfam05557 353 KERDGYRAILESYDKEltmsnyspqLLERIEEAEdmtqKMQAHNEEM-EAQLSVAEEELGGYKQQAQTlERELQALRQQE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3587 IEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAeKDILNKQKEMQELERKRLEQERVLA 3666
Cdd:pfam05557 432 SLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKT-KVLHLSMNPAAEAYQQRKNQLEKLQ 510
|
570
....*....|....*..
gi 1655274895 3667 DENQKLREKLQQMEEAQ 3683
Cdd:pfam05557 511 AEIERLKRLLKKLEDDL 527
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
3575-3685 |
2.13e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3575 TEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKdeqdrqrqQMEEEKLKLKAT-MDAALNKQKEAEKDILNKQKEMQE 3653
Cdd:smart00787 158 EDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK--------QLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLEE 229
|
90 100 110
....*....|....*....|....*....|..
gi 1655274895 3654 LERKRLEQERVLADENQKLREKLQQMEEAQKS 3685
Cdd:smart00787 230 LEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2775-3114 |
2.15e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2775 DMAENELERQRRlaestaqqklaAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDIL 2854
Cdd:pfam02029 3 DEEEAARERRRR-----------AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2855 IQLKSRAEKETMsntEKSKQLLEAEATKLRDLAEEASKL-RAIAEEAKHQRQLAEEDAARQRAEAERILKEklaaisDAT 2933
Cdd:pfam02029 72 EERRQKRLQEAL---ERQKEFDPTIADEKESVAERKENNeEEENSSWEKEEKRDSRLGRYKEEETEIREKE------YQE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2934 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQH-----KLEIEEKIVLLKKSSDAEMERQKAiVDDTLKQRR 3008
Cdd:pfam02029 143 NKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKikkekKVKYESKVFLDQKRGHPEVKSQNG-EEEVTKLKV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3009 VVEEEIRILKLNFEKASSGKLDLELElNKLKNIAEETQQSklrAEEEAEKLRR------LVLEEEMRRKEAEDKVKKiaa 3082
Cdd:pfam02029 222 TTKRRQGGLSQSQEREEEAEVFLEAE-QKLEELRRRRQEK---ESEEFEKLRQkqqeaeLELEELKKKREERRKLLE--- 294
|
330 340 350
....*....|....*....|....*....|..
gi 1655274895 3083 aeeEAARQRKaaQEELDRLQKKADEVRKQKEE 3114
Cdd:pfam02029 295 ---EEEQRRK--QEEAERKLREEEEKRRMKEE 321
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3039-3182 |
2.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3039 KNIAEETQQSKLRAEEEAEKLRRLVLEE-EMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADK 3117
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3118 EAE--KQIVAAQQAALkcnmaeqQVQSVLAQQKEDSMMQNKLKEEYEKAKA-LARDAEA-AKERAEREA 3182
Cdd:PRK12704 129 KEEelEELIEEQLQEL-------ERISGLTAEEAKEILLEKVEEEARHEAAvLIKEIEEeAKEEADKKA 190
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
3092-3194 |
2.28e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3092 KAAQEELDRLQKKADEVRKQK-EEADKEAEKQIV----AAQQAALKCNMAEQQ-----VQSVLA--QQKEDSMMQNKLKE 3159
Cdd:PRK11637 166 QARQETIAELKQTREELAAQKaELEEKQSQQKTLlyeqQAQQQKLEQARNERKktltgLESSLQkdQQQLSELRANESRL 245
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274895 3160 EYEKAKAlARDAEAAKERAEREAALLRQQAEEAER 3194
Cdd:PRK11637 246 RDSIARA-EREAKARAEREAREAARVRDKQKQAKR 279
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
3043-3347 |
2.39e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.33 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3043 EETQQSKLRAEEEAEKLRRL--VLEEEMRRKEAedKVKKIAAAEEEAARQRKAAQEELdrlQKKADEVRKQKEEADKEAE 3120
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLkqQLEAEFNQKRA--KFKELYLAKEEDLKRQNAVLQEA---QVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3121 kQIVAAqqAALKCNMAEQQVQSVLAQ-QKEDSMMQNKLKE---EYEKAKALARDAEAA-----KERAEREAALLRQQAEE 3191
Cdd:pfam03528 79 -NIKAV--ATVSENTKQEAIDEVKSQwQEEVASLQAIMKEtvrEYEVQFHRRLEQERAqwnqyRESAEREIADLRRRLSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3192 AERQKvaaeQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADE-EMAKHKKL-----AEQTLKQKFQ---- 3261
Cdd:pfam03528 156 GQEEE----NLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKElEASKMKELnhyleAEKSCRTDLEmyva 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3262 ---------------VEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDA----MRQKASVEEELFKVKIQMEELMKLK 3322
Cdd:pfam03528 232 vlntqksvlqedaekLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESqrllMRDMQRMESVLTSEQLRQVEEIKKK 311
|
330 340
....*....|....*....|....*
gi 1655274895 3323 VRIEEENQRlMKKDKDNTQKFLVEE 3347
Cdd:pfam03528 312 DQEEHKRAR-THKEKETLKSDREHT 335
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3252-3438 |
2.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3252 AEQTLkQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQM-------------EEL 3318
Cdd:COG3206 194 AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpellqspviqqlrAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3319 MKLKVRIEEENQRLMKKDKDntqkflVEEAENmkKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQ 3398
Cdd:COG3206 273 AELEAELAELSARYTPNHPD------VIALRA--QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655274895 3399 EASRLKAEAEMLQRQKDLAQEQAQKLLedKQLMQQRLDEE 3438
Cdd:COG3206 345 ELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEA 382
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
3558-3689 |
2.47e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 41.39 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3558 QQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDekkKLESQFEEEIKK-AKALKDEQDRqRQQMEEEKLKLKAT-MDAALN 3635
Cdd:pfam12474 8 QKDRFEQERQQLKKRYEKELEQLERQQKQQIE---KLEQRQTQELRRlPKRIRAEQKK-RLKMFRESLKQEKKeLKQEVE 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3636 KQ-KEAEKDILNKQKEMQELErKRLEQERVLADENQKLREKLQQMEEAQKSTLIT 3689
Cdd:pfam12474 84 KLpKFQRKEAKRQRKEELELE-QKHEELEFLQAQSEALERELQQLQNEKRKELAE 137
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3256-3684 |
2.49e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3256 LKQKFQVEQ-ELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmk 3334
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3335 kdkdntqKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQK 3414
Cdd:PRK01156 266 -------SMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3415 DlAQEQAQKLLEDkqLMQQRLDEETEE-----YQRSLEAERKRQLEIIAEAEKLKLQVSQLseaqakaeeeAKKFKKQAD 3489
Cdd:PRK01156 339 N-DYIKKKSRYDD--LNNQILELEGYEmdynsYLKSIESLKKKIEEYSKNIERMSAFISEI----------LKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3490 TIAARLHETEIATKEQMTEV------------KKMEFEK-------------LNTSKEADDLRKAITELEKEKARLKKEA 3544
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVsslnqriralreNLDELSRnmemlngqsvcpvCGTTLGEEKSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3545 EEHQNKSKEMADAQQKQIER---------EMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQ 3615
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRkeyleseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3616 RQqmeEEKLKLKATMDA----ALNKQKEAEKDILNK-QKEMQELER-------------KRLEQE-RVLADENQKLREKL 3676
Cdd:PRK01156 566 KR---TSWLNALAVISLidieTNRSRSNEIKKQLNDlESRLQEIEIgfpddksyidksiREIENEaNNLNNKYNEIQENK 642
|
....*...
gi 1655274895 3677 QQMEEAQK 3684
Cdd:PRK01156 643 ILIEKLRG 650
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
3589-3678 |
2.61e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.41 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3589 DEKKKLESQFEeeiKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQervLADE 3668
Cdd:pfam03938 15 PEGKAAQAQLE---KKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE---LQKK 88
|
90
....*....|
gi 1655274895 3669 NQKLREKLQQ 3678
Cdd:pfam03938 89 QQELLQPIQD 98
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2967-3126 |
2.66e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2967 LEDQANQHKLEIEEKIVLLKKSSDaEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlelelnKLKNIAEETQ 3046
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3047 QSKLRAEEEAEKLRRLVLEEEM-----RRKEAEDKVKKIAAAEEEAARQRKAAQEELD----RLQKKADEVRKQKEEADK 3117
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEIlelmeRIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAA 170
|
....*....
gi 1655274895 3118 EAEKQIVAA 3126
Cdd:COG1579 171 KIPPELLAL 179
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3387-3678 |
2.68e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3387 EKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ 3466
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3467 VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEE 3546
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3547 HQNkSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEdEKKKLESQFEEEIKKAKALKDE-----QDRQRQQMEE 3621
Cdd:pfam07888 197 LRN-SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE-ELRSLQERLNASERKVEGLGEElssmaAQRDRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3622 EKLKLKAT------MDAAL--------------NKQKEAEKD---ILNKQKEMQELErKRLEQERVladENQKLREKLQQ 3678
Cdd:pfam07888 275 HQARLQAAqltlqlADASLalregrarwaqereTLQQSAEADkdrIEKLSAELQRLE-ERLQEERM---EREKLEVELGR 350
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
3244-3941 |
2.70e-03 |
|
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: 44.66 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3244 EMAKHKKLAEQTLKQKfQVEQELTKVKLQLEETDKQKSLLDdELQRLKDEVDDAMRQKASVEEelfkVK-IQM---EELM 3319
Cdd:TIGR01612 1151 QINDLEDVADKAISND-DPEEIEKKIENIVTKIDKKKNIYD-EIKKLLNEIAEIEKDKTSLEE----VKgINLsygKNLG 1224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3320 KLKV-RIEEEnqrlmKKDKDNTQKflveeaeNMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQ 3398
Cdd:TIGR01612 1225 KLFLeKIDEE-----KKKSEHMIK-------AMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHII 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3399 EASRLKAEAEMlqRQKDLaqeqaqKLLEDKQlMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLK-----LQVSQLSEA 3473
Cdd:TIGR01612 1293 SKKHDENISDI--REKSL------KIIEDFS-EESDINDIKKELQKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKI 1363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3474 QAKAEEEAKKFKKQADTIAARLHETE--IATKEQMTEVK--KMEFEKLNTSKEADDLRKAITEL-------EKEKARLKK 3542
Cdd:TIGR01612 1364 IDEVKEYTKEIEENNKNIKDELDKSEklIKKIKDDINLEecKSKIESTLDDKDIDECIKKIKELknhilseESNIDTYFK 1443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3543 EAEEHQN------KSKEMADAQQKQIeremtvlqqtfltekeMLLKKEKLIEDEKKKLeSQFEEEIKKAKALKDEQDRQR 3616
Cdd:TIGR01612 1444 NADENNEnvlllfKNIEMADNKSQHI----------------LKIKKDNATNDHDFNI-NELKEHIDKSKGCKDEADKNA 1506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3617 QQMEEEKLKLKatmdaalnKQKEAEKDILNKQKEMQ---ELERKRLEQERVLaDENQKLREK--LQQMEEAQKSTLITEK 3691
Cdd:TIGR01612 1507 KAIEKNKELFE--------QYKKDVTELLNKYSALAiknKFAKTKKDSEIII-KEIKDAHKKfiLEAEKSEQKIKEIKKE 1577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3692 HVTVVETVLNGQNAGDVLDGVEKRPDPMafdgirdkvpASRLLDIGVLPKKEFDLLKngkttakelgETENLRKilkgkn 3771
Cdd:TIGR01612 1578 KFRIEDDAAKNDKSNKAAIDIQLSLENF----------ENKFLKISDIKKKINDCLK----------ETESIEK------ 1631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3772 siagiltpsnQKMTIYQASKEKKITP-GTAMILLEAqaatgyMLDPINNHKLSVNEAVKEgliGPELHNKMLSAEKAVVG 3850
Cdd:TIGR01612 1632 ----------KISSFSIDSQDTELKEnGDNLNSLQE------FLESLKDQKKNIEDKKKE---LDELDSEIEKIEIDVDQ 1692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3851 YKDPYsggKISVFEAMKKGLMDHDHAIRVLEAQLATG--GIIDPLNSHRV----PNEiayKQGQYDAEMNKIME---NPS 3921
Cdd:TIGR01612 1693 HKKNY---EIGIIEKIKEIAIANKEEIESIKELIEPTieNLISSFNTNDLegidPNE---KLEEYNTEIGDIYEefiELY 1766
|
730 740
....*....|....*....|
gi 1655274895 3922 DDTKGYFDPSTQEPLTYSEL 3941
Cdd:TIGR01612 1767 NIIAGCLETVSKEPITYDEI 1786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1453-1721 |
2.94e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1453 VEKEWGRLHVAILERERLLRIEFERLERLQRIVNKVQMESGSCDEQLGNLE-TLLQTDIRLLNAGKPAQHTAEIERELDK 1531
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1532 ADNTIRLLFNDVQILKDGRHPQAEQMYRRVFRIHERLVNLRSDYNLRLKSTTS-AIQATRLSPQESSMKARpelddvtlr 1610
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDR--------- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1611 yVQDLLEWVQENQRRIDEAEwgsdLPSVESQLGSH-RGLHQTVEDFRSKIERAKADENQLSPISRgKYREYLGRLDlQYA 1689
Cdd:TIGR02168 416 -RERLQQEIEELLKKLEEAE----LKELQAELEELeEELEELQEELERLEEALEELREELEEAEQ-ALDAAERELA-QLQ 488
|
250 260 270
....*....|....*....|....*....|..
gi 1655274895 1690 KLLNSSKSRLRNLDSLHAFVSAATKELMWLND 1721
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3599-3713 |
3.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3599 EEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKrleqervLADENQKLREKLQQ 3678
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-------IAEAEAEIEERREE 87
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274895 3679 MEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVE 3713
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGSESFSDFLDRLS 122
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2446-2703 |
3.28e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.94 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2446 QKKMAEMQ---AELDKQKQLAEAHakaIAKAEKEAQELKLRMQEEVsKRETAAVDAEK--------QKQNIQLELHELKN 2514
Cdd:pfam03528 7 QQRVAELEkenAEFYRLKQQLEAE---FNQKRAKFKELYLAKEEDL-KRQNAVLQEAQveldalqnQLALARAEMENIKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2515 LSEQQIKDKSQQVDEaLKSRLRiEEEIHLIRIQLETTVKQKSNAEDELKQlrDRADAAEkLRKLAQEEAEKLRKQVSEET 2594
Cdd:pfam03528 83 VATVSENTKQEAIDE-VKSQWQ-EEVASLQAIMKETVREYEVQFHRRLEQ--ERAQWNQ-YRESAEREIADLRRRLSEGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2595 QKKRLaEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQvAHVAAQQSAAAELrskQMSFAe 2674
Cdd:pfam03528 158 EEENL-EDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELN-HYLEAEKSCRTDL---EMYVA- 231
|
250 260
....*....|....*....|....*....
gi 1655274895 2675 nVSKLEESLkqehgtvlqLQQDAERLRKQ 2703
Cdd:pfam03528 232 -VLNTQKSV---------LQEDAEKLRKE 250
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3239-3371 |
3.51e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3239 QQADEEMAKHKKLAEQTLKQKF-----QVEQELT--KVKLQ-LEETDKQK-SLLDDELQRLKDEVDDAMRQKASVEEELF 3309
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIhklrnEFEKELRerRNELQkLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3310 KVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAEnmKKLAEDAARLSIEAQEAARL 3371
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVE--EEARHEAAVLIKEIEEEAKE 184
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2556-2968 |
3.53e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.52 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2556 SNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAAN---EKQKALEDLENLRMQA 2632
Cdd:pfam19220 13 GEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGltrRLSAAEGELEELVARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2633 EEAERQVKQAEVEKERQiqvahvaaqqsaAAELRSKQmSFAENvskLEESLKQEHGTVLQLQQDaerlrkqqedaenare 2712
Cdd:pfam19220 93 AKLEAALREAEAAKEEL------------RIELRDKT-AQAEA---LERQLAAETEQNRALEEE---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2713 eaerelekwrqkaNEALRLRLQAEEEAhkkslaqeeaekqkeeadreaKKRSKAEESALKQR-DMAENELERQRRLAEST 2791
Cdd:pfam19220 141 -------------NKALREEAQAAEKA---------------------LQRAEGELATARERlALLEQENRRLQALSEEQ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2792 AQQKLAAEQeliRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILiqlksRAEKETMSN-TE 2870
Cdd:pfam19220 187 AAELAELTR---RLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASL-----RMKLEALTArAA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2871 KSKQLLEAEATKLRDLAE----------EASKLRAIAE------EAKHQRQLAE-EDAARQRAEAE-------RILKEKL 2926
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEairaaerrlkEASIERDTLErrlaglEADLERRTQQfQEMQRARAELEeraemltKALAAKD 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 2927 AAISDAT--------RLKTEAEIALKEK---EAENERLRRQAEDEAYQRKILE 2968
Cdd:pfam19220 339 AALERAEeriaslsdRIAELTKRFEVERaalEQANRRLKEELQRERAERALAQ 391
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2944-3188 |
3.56e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2944 KEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVllkkssdAEMERQKAivddtLKQRRVVEEEIRilklNFEK 3023
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRA-------AEQARQKE-----LEQRAAAEKAAK----QAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3024 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLV--LEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEEldRL 3101
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkqAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEA--EA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3102 QKKADEVRKQKEEADKEAEKQIVA-AQQAALKCNMAEqqvqsvlAQQKEDSMMQNK---LKEEYEKAKALARDAEAAKER 3177
Cdd:TIGR02794 188 KAKAEEAKAKAEAAKAKAAAEAAAkAEAEAAAAAAAE-------AERKADEAELGDifgLASGSNAEKQGGARGAAAGSE 260
|
250
....*....|.
gi 1655274895 3178 AEREAALLRQQ 3188
Cdd:TIGR02794 261 VDKYAAIIQQA 271
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
3034-3444 |
3.59e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3034 ELNKLKNIAEETQQSKLRAEEEA--EKLRRLVLEEEMRRKEAEDKVKKiaaaeeeaARQRKAAQEELDRlqkkadevRKQ 3111
Cdd:NF033838 103 ELNVLKEKSEAELTSKTKKELDAafEQFKKDTLEPGKKVAEATKKVEE--------AEKKAKDQKEEDR--------RNY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3112 KEEADKEAEKQIVaaqQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKerAEREAAllrqqAEE 3191
Cdd:NF033838 167 PTNTYKTLELEIA---ESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIK--TDREKA-----EEE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3192 AERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEmakhkkLAEQTLKQ-KFQVEQELTKVK 3270
Cdd:NF033838 237 AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSS------VGEETLPSpSLKPEKKVAEAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3271 LQLEETDKqksllddelqRLKDEVDDAMRQKASVEEELFKVkiqmeELMKLKVRIEEENQRLMKKDKdntqkflvEEAEN 3350
Cdd:NF033838 311 KKVEEAKK----------KAKDQKEEDRRNYPTNTYKTLEL-----EIAESDVKVKEAELELVKEEA--------KEPRN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3351 MKKLAEDAARLSIEAQEAARLRQI------AEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKl 3424
Cdd:NF033838 368 EEKIKQAKAKVESKKAEATRLEKIktdrkkAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEK- 446
|
410 420
....*....|....*....|
gi 1655274895 3425 LEDKQLMQQRLDEETEEYQR 3444
Cdd:NF033838 447 PADQQAEEDYARRSEEEYNR 466
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3581-3684 |
3.59e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3581 LKKEKLIEDEKKKLESQFEEeikkAKALKDEQDRQRQQMEEeklkLKATMDAALNKQKEAEKDILNKQKEMQELERKRLE 3660
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQ----TLALLDKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100
....*....|....*....|....
gi 1655274895 3661 QeRVLADENQKLREKLQQMEEAQK 3684
Cdd:PRK11281 120 T-LSLRQLESRLAQTLDQLQNAQN 142
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2236-2459 |
3.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2236 LEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLR--QRELDQLGRQLGYYRESYDWLIRWIADA 2313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2314 KQRQENIQAVpitdSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDY-ELQLVAYKAQVepltspLKKTKL 2392
Cdd:COG4913 695 EELEAELEEL----EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAA------LGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2393 DSASDNIIQEYVTLRTR----YSELMTLTSQYIK--------------FITDTQRRLED---------EEKAAEKLKAEE 2445
Cdd:COG4913 765 RELRENLEERIDALRARlnraEEELERAMRAFNRewpaetadldadleSLPEYLALLDRleedglpeyEERFKELLNENS 844
|
250
....*....|....
gi 1655274895 2446 QKKMAEMQAELDKQ 2459
Cdd:COG4913 845 IEFVADLLSKLRRA 858
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
3037-3244 |
3.66e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3037 KLKNIAEETQQS---KLRAE--------EEAEKLRRLVLEEEMRRKEAEDKV---------KKIAAAEEEAARQRK---- 3092
Cdd:PRK05035 437 EIRAIEQEKKKAeeaKARFEarqarlerEKAAREARHKKAAEARAAKDKDAVaaalarvkaKKAAATQPIVIKAGArpdn 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3093 ---AAQEELDRLQKKADEVRKQKEEADkEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSmmqNKLKEEYEKAKALAR 3169
Cdd:PRK05035 517 savIAAREARKAQARARQAEKQAAAAA-DPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDP---KKAAVAAAIARAKAK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3170 --------------DAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaal 3235
Cdd:PRK05035 593 kaaqqaasaepeeqVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKAR-------------- 658
|
....*....
gi 1655274895 3236 KQKQQADEE 3244
Cdd:PRK05035 659 KAAQQQANA 667
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3056-3390 |
3.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3056 AEKLRRLVLEEEMRRKEAED---KVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALK 3132
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQlreELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3133 CNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQ-- 3210
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEll 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3211 -DDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQR 3289
Cdd:COG4372 190 kEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3290 LKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAA 3369
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330 340
....*....|....*....|.
gi 1655274895 3370 RLRQIAEDDLNQQRTLAEKML 3390
Cdd:COG4372 350 LLDNDVLELLSKGAEAGVADG 370
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1705-1798 |
3.71e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.99 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1705 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 1784
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
|
90
....*....|....
gi 1655274895 1785 AALQTQWSWILQLC 1798
Cdd:pfam00435 83 EELNERWEQLLELA 96
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2434-2664 |
3.94e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.67 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2434 EEKAAEKLKAEEQKKMAE-------MQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQeevskRETAAVDAEKQKQNIQ 2506
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQdlqqalsLLDKIDASKQRAAAYQKALDDAPAELRELRQELA-----ALQAKAEAAPKEILAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2507 LELHELknlsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAeKLRKLAQEEAEKL 2586
Cdd:pfam12795 78 LSLEEL----EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGP-APPGEPLSEAQRW 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2587 RKQVSEETQKKRLAEEELKHKSEAERKAANEKQKaleDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE 2664
Cdd:pfam12795 153 ALQAELAALKAQIDMLEQELLSNNNRQDLLKARR---DLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3164-3389 |
4.02e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3164 AKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADE 3243
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3244 EMAKHKK-LAEQTLKQKFQVEQELTKVKLQ---LEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM 3319
Cdd:COG4942 98 ELEAQKEeLAELLRALYRLGRQPPLALLLSpedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3320 KLKVRIEEENQRLmKKDKDNTQKFLveeAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKM 3389
Cdd:COG4942 178 ALLAELEEERAAL-EALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2461-2651 |
4.13e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2461 QLAEAHAKAIAKAEKEAQELKLRMQEEVSkretaavdaekqkqNIQLELHELKNlSEQQIKDKSQQVDEALKsrlRIEEE 2540
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELE--------------ELQEQLEDLES-SIQELEKEIKKLESSIK---QVEEE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2541 IHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLrKQVSEETQKKRLAE-EELKHKSEAERKAANEKQ 2619
Cdd:pfam05667 372 LEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiEEYRALKEAKSNKEDESQ 450
|
170 180 190
....*....|....*....|....*....|..
gi 1655274895 2620 KALEDLENLRMQAEEAERQVKQAEvEKERQIQ 2651
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKE-ELYKQLV 481
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2305-2480 |
4.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2305 WLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPlt 2384
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2385 splKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDeekaAEKLKAEEQKKM----AEMQAELDKQK 2460
Cdd:PRK12704 101 ---KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER----ISGLTAEEAKEIllekVEEEARHEAAV 173
|
170 180
....*....|....*....|
gi 1655274895 2461 QLAEAHAKAIAKAEKEAQEL 2480
Cdd:PRK12704 174 LIKEIEEEAKEEADKKAKEI 193
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3351-3684 |
4.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3351 MKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKaeaemlQRQKDLAQEQAQKLLEDKQL 3430
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE------EELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3431 MQQRLDEETEEYQRSLEAERKrqlEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVK 3510
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELA---ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3511 KmEFEKLntSKEADDLRKAITELEKEKARLKKEAEEHQNKSkeMADAQQKQIEREMTVLQQ-----TFLTEKEMLLKKEK 3585
Cdd:COG4717 199 E-ELEEL--QQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIaaallALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3586 LIED--------------EKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKL-------KATMDAALNKQKEAEKDI 3644
Cdd:COG4717 274 TIAGvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELL 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1655274895 3645 LNKQKEMQELERKRLEQER------VLADENQKLREKLQQMEEAQK 3684
Cdd:COG4717 354 REAEELEEELQLEELEQEIaallaeAGVEDEEELRAALEQAEEYQE 399
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
3379-3551 |
4.27e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3379 LNQQRTLAEKMLKEKMQAIQEASRLKAEAEmLQRQKDLAQEQAQKLledkqlmqQRLDEETEEYQRSLE--AERKRQLEi 3456
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQR--------QEARREREELQREEErlVQKEEQLD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3457 iAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQmteVKKMEFEKLNtskeaddlrkaiTELEKE 3536
Cdd:PRK12705 95 -ARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQ---ARKLLLKLLD------------AELEEE 158
|
170
....*....|....*....
gi 1655274895 3537 KA----RLKKEAEEHQNKS 3551
Cdd:PRK12705 159 KAqrvkKIEEEADLEAERK 177
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3518-3684 |
4.30e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3518 NTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIE--REMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE 3595
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAqvKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3596 SQFEEEIKKAKALKDEQDrQRQQMEEEKLKLKATMDAALNKQ------KEAEKDILNKQKEMqeleRKRLEQERVLADEN 3669
Cdd:COG1340 85 EKLNELREELDELRKELA-ELNKAGGSIDKLRKEIERLEWRQqtevlsPEEEKELVEKIKEL----EKELEKAKKALEKN 159
|
170
....*....|....*
gi 1655274895 3670 QKLREKLQQMEEAQK 3684
Cdd:COG1340 160 EKLKELRAELKELRK 174
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2632-2821 |
4.34e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2632 AEEAERQVKQAEVEKERQIQVAHVAAQQsaAAELRSKQMSFAENVSKLE-ESLKQEHGTVLQLQQDAERLRKQQEDAENA 2710
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEELQQKQAAEQERLKQLEkERLAAQEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2711 REEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQ-----------KEEADREAKKRSKAE-ESALKQRDMAE 2778
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAaeakkkaeaeaAAKAAAEAKKKAEAEaKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655274895 2779 NELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLED 2821
Cdd:PRK09510 219 AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
3089-3195 |
4.37e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.70 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3089 RQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAAlkcNMAEQQVQsvlaQQKEDSMMQNKLKEEYEKAKALA 3168
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQ---QNYERELV----LHAEDIKALQALREELNELKAEI 73
|
90 100
....*....|....*....|....*..
gi 1655274895 3169 RDAEAAKERAEREAALLRQQAEEAERQ 3195
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQKKE 100
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
3280-3690 |
4.46e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3280 KSLLDDELQRLKDEVDdamRQKasveEELFKVKIQMEELmklKVRIEEENQRLMKKDkDNTQKFLveEAENMKKLA---- 3355
Cdd:pfam10174 111 PELTEENFRRLQSEHE---RQA----KELFLLRKTLEEM---ELRIETQKQTLGARD-ESIKKLL--EMLQSKGLPkksg 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3356 ----EDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKmLKEKMQAIQEASRLKAEAEMLQRQ--KDLAQEQAQKLLEDK- 3428
Cdd:pfam10174 178 eedwERTRRIAEAEMQLGHLEVLLDQKEKENIHLREE-LHRRNQLQPDPAKTKALQTVIEMKdtKISSLERNIRDLEDEv 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3429 QLMQQRLDEETEEYQrsleaERKRQLEIIAEAEK-LKLQVSQLSEAQAKAEEEAKKFKKQADTIaarlheteiatKEQMT 3507
Cdd:pfam10174 257 QMLKTNGLLHTEDRE-----EEIKQMEVYKSHSKfMKNKIDQLKQELSKKESELLALQTKLETL-----------TNQNS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3508 EVKKmEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEhqnkskEMADAQQKQIER---EMTVLQQTFLTEKEMLLKKE 3584
Cdd:pfam10174 321 DCKQ-HIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE------SFLNKKTKQLQDlteEKSTLAGEIRDLKDMLDVKE 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3585 KLIEDEKKKLESQFEEEIKKAKALKDEQDRQrQQMEEEKlklkATMDAALNKQKEA----EKDILNKQKEMQELERKRLE 3660
Cdd:pfam10174 394 RKINVLQKKIENLQEQLRDKDKQLAGLKERV-KSLQTDS----SNTDTALTTLEEAlsekERIIERLKEQREREDRERLE 468
|
410 420 430
....*....|....*....|....*....|..
gi 1655274895 3661 QERVLADENQKLREKL--QQMEEAQKSTLITE 3690
Cdd:pfam10174 469 ELESLKKENKDLKEKVsaLQPELTEKESSLID 500
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2421-2511 |
4.57e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2421 IKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK-RETAAVDA 2498
Cdd:cd06503 25 LKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEaRAEAQEIIEEARKEAEKIKEEILAEAKEEAERiLEQAKAEI 104
|
90
....*....|...
gi 1655274895 2499 EKQKQNIQLELHE 2511
Cdd:cd06503 105 EQEKEKALAELRK 117
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
3589-3678 |
4.58e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 41.36 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3589 DEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEkdILNKQKEMQELERKRLEQervLADE 3668
Cdd:COG2825 39 PEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQKKERE--LQKKQQELQRKQQEAQQD---LQKR 113
|
90
....*....|
gi 1655274895 3669 NQKLREKLQQ 3678
Cdd:COG2825 114 QQELLQPILE 123
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4537-4572 |
4.67e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 4.67e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1655274895 4537 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVA 4572
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2432-2701 |
4.70e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2432 EDEEKAAEKLKAEEqkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNiqlELHE 2511
Cdd:PRK07735 36 KLEEENREKEKALP--KNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAA---ALAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2512 LKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETT--VKQKSNAEDELKQLRDRADAAE-KLRKLAQEEAEKLRK 2588
Cdd:PRK07735 111 QKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTeeVTEEEEETDKEKAKAKAAAAAKaKAAALAKQKAAEAGE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2589 QVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDlenlrmqaeeaerqvkQAEVEKERQIQVAHVAAQQSAAAELRSK 2668
Cdd:PRK07735 191 GTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQG----------------NGDSGDEDAKAKAIAAAKAKAAAAARAK 254
|
250 260 270
....*....|....*....|....*....|....*
gi 1655274895 2669 QMSfaeNVSKLEESLKQEHGTVLQ--LQQDAERLR 2701
Cdd:PRK07735 255 TKG---AEGKKEEEPKQEEPSVNQpyLNKYVEVIK 286
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2428-2638 |
4.77e-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: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2428 QRRLEDEEKAAE-----KLKAEEQKKMAEMQAELDKQKQlaeahakaiakaeKEAQELKLRMQEEVSKRETAAvdAEKQK 2502
Cdd:pfam15709 345 MRRLEVERKRREqeeqrRLQQEQLERAEKMREELELEQQ-------------RRFEEIRLRKQRLEEERQRQE--EEERK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2503 QNIQlelhelknlsEQQIKDKSQQVDEALKSRLRieeEIHLIRIQLETtvkQKSNAEDE-LKQLRDR-ADAAEKLRKLAQ 2580
Cdd:pfam15709 410 QRLQ----------LQAAQERARQQQEEFRRKLQ---ELQRKKQQEEA---ERAEAEKQrQKELEMQlAEEQKRLMEMAE 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2581 EEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAAnekqkaledLENLRMQAEEAERQ 2638
Cdd:pfam15709 474 EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLA---------LEEAMKQAQEQARQ 522
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2856-2999 |
4.80e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2856 QLKSRAEKETmSNTEKSKQLLEAEATKLRDLAEEASKlRAIAEeakhqRQLAEEDAARQRAEAErilkekLAAISDATRL 2935
Cdd:COG2268 196 EIIRDARIAE-AEAERETEIAIAQANREAEEAELEQE-REIET-----ARIAEAEAELAKKKAE------ERREAETARA 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 2936 KTEAEIALKEKEAENErLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKssdAEMERQKAI 2999
Cdd:COG2268 263 EAEAAYEIAEANAERE-VQRQLEIAEREREIELQEKEAEREEAELEADVRKP---AEAEKQAAE 322
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
1111-1231 |
5.05e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 40.36 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 1111 ERDRVQKKTFTKWVNKHLIKSQrhVTDLYEDLRDGHNLISLLEVLSGDTllserDVARSVRLPREKGRMRFHKLQNVQIA 1190
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIKVPV-----DWNRVNKPPYPKLGENMKKLENCNYA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655274895 1191 LDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4754-4790 |
5.21e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 5.21e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655274895 4754 KQYLYGTGCVAGFT-TDSGSKMSIYQAMKRGFIQPDVA 4790
Cdd:smart00250 1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2120-2559 |
5.27e-03 |
|
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: 43.50 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2120 LEGLKKDLDKVSTKTQDILNSPQPSATAPVLRSELELTVQKMDHAYMLSSVYLEKL------------------------ 2175
Cdd:TIGR01612 1245 MEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENIsdirekslkiiedfseesdindik 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2176 KTVEMVIRNTQGAEGVLKQYENCLREVHTV------PNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDK 2249
Cdd:TIGR01612 1325 KELQKNLLDAQKHNSDINLYLNEIANIYNIlklnkiKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEEC 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2250 MSRVHSERDA-ELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQlgrqlgyYRESYDWLIRWIADAKQRQENIQAVPITDS 2328
Cdd:TIGR01612 1405 KSKIESTLDDkDIDECIKKIKELKNHILSEESNIDTYFKNADE-------NNENVLLLFKNIEMADNKSQHILKIKKDNA 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2329 KT--------LKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYidiIKDYELQLVAYKAQvePLTSPLKKTKLDsaSDNII 2400
Cdd:TIGR01612 1478 TNdhdfnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQY---KKDVTELLNKYSAL--AIKNKFAKTKKD--SEIII 1550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2401 QEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEK-----------LKAEEQK--KMAEMQAELDKQKQLAEAHA 2467
Cdd:TIGR01612 1551 KEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKsnkaaidiqlsLENFENKflKISDIKKKINDCLKETESIE 1630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2468 KAIAKAEKEAQELKLRMQEEVSKRETAAVDAEK-QKQNIQLELHELKNLsEQQIKDKSQQVDEALKSRlrieeEIHLIRI 2546
Cdd:TIGR01612 1631 KKISSFSIDSQDTELKENGDNLNSLQEFLESLKdQKKNIEDKKKELDEL-DSEIEKIEIDVDQHKKNY-----EIGIIEK 1704
|
490
....*....|...
gi 1655274895 2547 QLETTVKQKSNAE 2559
Cdd:TIGR01612 1705 IKEIAIANKEEIE 1717
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4422-4458 |
5.31e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.31e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1655274895 4422 KYLQGSESIAGIYLEPTKENISIYQAMKKKLLRHNTG 4458
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
3537-3660 |
5.48e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3537 KARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQfEEEIKKAKALKDEQDRQR 3616
Cdd:pfam05672 22 QAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE-EEAEEREQREQEEQERLQ 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655274895 3617 QQMEEEKLKLkatmdaalnkQKEAEKDILNKQKEMQELERKRLE 3660
Cdd:pfam05672 101 KQKEEAEAKA----------REEAERQRQEREKIMQQEEQERLE 134
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2994-3197 |
5.51e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2994 ERQKAIVDDTLKQRRVVEEEIRILKLNFEKA---------SSGKLDLELELN-KLKNIAE-ETQQSKLRAEEEAEKLRRL 3062
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAeaaleefrqKNGLVDLSEEAKlLLQQLSElESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3063 VLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKA-----------DEVRKQKEEADKEAEKQIVAAQQAAL 3131
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 3132 KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEkakALARDAEAAKERAEreaALL--RQQAEEAERQKV 3197
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR---RLEREVEVARELYE---SLLqrLEEARLAEALTV 385
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3034-3167 |
5.69e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3034 ELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEA-ARQRKAAQEELDRLQKKADEVRKQK 3112
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLlEEAEKEAQQAIKEAKKEADEIIKEL 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3113 EEADKEAEKQIVAAQQaalkcnmaeQQVQSVLAQQKEdsMMQNKLKEEYEKAKAL 3167
Cdd:PRK00409 594 RQLQKGGYASVKAHEL---------IEARKRLNKANE--KKEKKKKKQKEKQEEL 637
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2399-2641 |
5.76e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2399 IIQEYVTLRTRYSELmtltSQYIKFITDTQRRLEDEEKAAEKLK--AEEQKKMAEMQAEL-DKQKQLAEAHA--KAIAKA 2473
Cdd:COG4913 615 LEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIaELEAELERLDAssDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2474 EKEAQELKLRMQE---EVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRieeeiHLIRIQLET 2550
Cdd:COG4913 691 EEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA-----AALGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2551 TVKQksNAEDELKQLRDRADAAE-KLRKLAQE-----EAEKLRKQVS----EETQK--KRLAEEELKHKSEAERKAANEK 2618
Cdd:COG4913 766 ELRE--NLEERIDALRARLNRAEeELERAMRAfnrewPAETADLDADleslPEYLAllDRLEEDGLPEYEERFKELLNEN 843
|
250 260
....*....|....*....|...
gi 1655274895 2619 QKalEDLENLRMQAEEAERQVKQ 2641
Cdd:COG4913 844 SI--EFVADLLSKLRRAIREIKE 864
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2459-2672 |
6.05e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2459 QKQLAEAHAKaIAKAEKEAQELKLR-----MQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQ---QIKDKSQQVDEA 2530
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2531 LKSRlrieeeihliriQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKkrlAEEELKHKSEA 2610
Cdd:COG3206 260 LQSP------------VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR---ILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274895 2611 ERKAANEKQKALEDLEN--LRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSF 2672
Cdd:COG3206 325 LQAREASLQAQLAQLEArlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2758-3219 |
6.06e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2758 REAKKRSKAEESALKQRDMAEnelERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELyRLKNEVIAAQQER 2837
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAE---AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEA-EQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2838 KQLEDElskvrsemdiliqlKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKhqrqlAEEDAARQRAE 2917
Cdd:COG3064 78 KLAEAE--------------KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKR-----KAEEEAKRKAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2918 AERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQK 2997
Cdd:COG3064 139 EERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2998 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKV 3077
Cdd:COG3064 219 LAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3078 KKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKL 3157
Cdd:COG3064 299 DSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLG 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3158 KEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKD 3219
Cdd:COG3064 379 KLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKL 440
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2454-2587 |
6.08e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2454 AELDKQK---QLAEAHAK-AIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKsQQVDE 2529
Cdd:COG1566 74 ARLDPTDlqaALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ-QELDE 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274895 2530 ALKSRLRIEEEIHLIRIQLETTvKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLR 2587
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQA-QAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2433-2651 |
6.16e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2433 DEEKAAEKLKAEEQKKMAEMQAELDKQKqlaeahakaiakaekeaQELKLRMQEEVSKRetaavdAEKQKQNIQLELHEL 2512
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVERKRRE-----------------QEEQRRLQQEQLER------AEKMREELELEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2513 KnlseQQIKDKSQQVDEalkSRLRIEEEIHLIRIQLETTVKQKSNAEDELkqlrdRADAAEKLRKLAQEEAEKL----RK 2588
Cdd:pfam15709 386 F----EEIRLRKQRLEE---ERQRQEEEERKQRLQLQAAQERARQQQEEF-----RRKLQELQRKKQQEEAERAeaekQR 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 2589 QVSEETQ----KKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERqVKQAEVEKERQIQ 2651
Cdd:pfam15709 454 QKELEMQlaeeQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAAR-LALEEAMKQAQEQ 519
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
3532-3662 |
6.30e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 40.24 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3532 ELEKEKARLKKEAEEHQNK---SKEMaDAQQKQIEREMTVLQQTFLTEKEMLLKKEKLiedEKKKLESQFEEEIK-KAKA 3607
Cdd:pfam12474 2 QLQKEQQKDRFEQERQQLKkryEKEL-EQLERQQKQQIEKLEQRQTQELRRLPKRIRA---EQKKRLKMFRESLKqEKKE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274895 3608 LKDEQDRQRQQMEEEKLKLKatMDAALNKQKEAEKDILNKQKEMQELERKRLEQE 3662
Cdd:pfam12474 78 LKQEVEKLPKFQRKEAKRQR--KEELELEQKHEELEFLQAQSEALERELQQLQNE 130
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
3000-3128 |
6.48e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 41.69 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3000 VDDTLKQRRVVEEE-----IRILKLNFEKASSGKLDLELEL--NKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKE 3072
Cdd:cd07647 24 LEDFLKQRAKAEEDygkalLKLSKSAGPGDEIGTLKSSWDSlrKETENVANAHIQLAQSLREEAEKLEEFREKQKEERKK 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274895 3073 AEDKVKKIAaaeeeaaRQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 3128
Cdd:cd07647 104 TEDIMKRSQ-------KNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKSSSGAQP 152
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2985-3700 |
6.74e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2985 LKKssDAEMERQKAIVDDTLK-QRRVVEEEIRILKLNFEkASSGKLDLELELNKL--------KNIAEETQQSKLRAEEE 3055
Cdd:pfam10174 41 LKK--ERALRKEEAARISVLKeQYRVTQEENQHLQLTIQ-ALQDELRAQRDLNQLlqqdfttsPVDGEDKFSTPELTEEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3056 AEKLR----RLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKAdeVRKQKEEADKEAEKQIVAAQqaal 3131
Cdd:pfam10174 118 FRRLQseheRQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKG--LPKKSGEEDWERTRRIAEAE---- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3132 kcnMAEQQVQSVLAQQKEDSMmqnKLKEEyekakaLARDAEAAKERAEREAAllrQQAEEAERQKVAAEQEAANQAkaQD 3211
Cdd:pfam10174 192 ---MQLGHLEVLLDQKEKENI---HLREE------LHRRNQLQPDPAKTKAL---QTVIEMKDTKISSLERNIRDL--ED 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3212 DAERLRKDAEFEAAKLAQAEAAALKQKQQADeeMAKHKKlaeQTLKQKFQ-VEQELTKVKLQLEETDKQKSLLDDELQRL 3290
Cdd:pfam10174 255 EVQMLKTNGLLHTEDREEEIKQMEVYKSHSK--FMKNKI---DQLKQELSkKESELLALQTKLETLTNQNSDCKQHIEVL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3291 KDEVDdAMRQKASVEEElfkvkiqmeELMKLKVRIEEENQRLMKK-----DKDNTQKFLVEEAENMKKLaedaarLSIEA 3365
Cdd:pfam10174 330 KESLT-AKEQRAAILQT---------EVDALRLRLEEKESFLNKKtkqlqDLTEEKSTLAGEIRDLKDM------LDVKE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3366 QEAARLRQIAEDDLNQQRTLAEKM--LKEKMQAIQEASRlkaeaemlqrQKDLAQEQAQKLLEDKQLMQQRLDE--ETEE 3441
Cdd:pfam10174 394 RKINVLQKKIENLQEQLRDKDKQLagLKERVKSLQTDSS----------NTDTALTTLEEALSEKERIIERLKEqrERED 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3442 YQRSLEAERKRQleiiaEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIA-------ARLHETEIATKEQMTEVKKMEF 3514
Cdd:pfam10174 464 RERLEELESLKK-----ENKDLKEKVSALQPELTEKESSLIDLKEHASSLAssglkkdSKLKSLEIAVEQKKEECSKLEN 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3515 EKLNTSKEADDLRKA------ITELEKEKARLKKEAeehqNKSkemadaqQKQIEREMTVLQQTfltEKEMLLKKEKLIE 3588
Cdd:pfam10174 539 QLKKAHNAEEAVRTNpeindrIRLLEQEVARYKEES----GKA-------QAEVERLLGILREV---ENEKNDKDKKIAE 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3589 DEKKKLEsQFEEEIKKAKALKDEQdrqrQQMeeeklklkatmdaalnkqkeaekdilnKQKEMQELERKRLEQERVLADE 3668
Cdd:pfam10174 605 LESLTLR-QMKEQNKKVANIKHGQ----QEM---------------------------KKKGAQLLEEARRREDNLADNS 652
|
730 740 750
....*....|....*....|....*....|...
gi 1655274895 3669 NQKLREKLQQMEEAQKSTL-ITEKHVTVVETVL 3700
Cdd:pfam10174 653 QQLQLEELMGALEKTRQELdATKARLSSTQQSL 685
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
1896-1940 |
6.77e-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: 38.02 E-value: 6.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1655274895 1896 VQAVCDFKQVE---ITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPS 1940
Cdd:cd11768 2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
3365-3686 |
6.99e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3365 AQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAemLQRQKDlAQEQAQKLLEDKQLMQQRLDEETEEYQR 3444
Cdd:TIGR00606 236 SREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK--KQMEKD-NSELELKMEKVFQGTDEQLNDLYHNHQR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3445 SLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEK-LNTSKEA 3523
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3524 DDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsqfeeeik 3603
Cdd:TIGR00606 393 KNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ-------- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3604 kakalkdeqdrQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQElerKRLEQERvlADENQKLREKLQQMEEAQ 3683
Cdd:TIGR00606 465 -----------QLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV---KSLQNEK--ADLDRKLRKLDQEMEQLN 528
|
...
gi 1655274895 3684 KST 3686
Cdd:TIGR00606 529 HHT 531
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3054-3166 |
7.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3054 EEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQkkaDEVRKQKEEADKEAEKQIVAAQQAALK- 3132
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKKEADEi 589
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274895 3133 ----CNMAEQQVQSVLAQQKEDsmMQNKLKEEYEKAKA 3166
Cdd:PRK00409 590 ikelRQLQKGGYASVKAHELIE--ARKRLNKANEKKEK 625
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2410-2643 |
7.13e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.27 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2410 YSELMtltSQYIKFITDTQRRLEDEEKAAEKL----------KAEEQKKMAEMQAELDKQKQ--LAEAHAKAIAKAEKEA 2477
Cdd:pfam02841 52 YEQQM---AQKVKLPTETLQELLDLHRDCEKEaiavfmkrsfKDENQEFQKELVELLEAKKDdfLKQNEEASSKYCSALL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2478 QELKLRMQEEVsKRETAAVDAekqkqNIQLELHELKNLSEQ--QIKDKSQQVDEALKSRLRIEEEIHLIRIQLET--TVK 2553
Cdd:pfam02841 129 QDLSEPLEEKI-SQGTFSKPG-----GYKLFLEERDKLEAKynQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQalTAK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2554 QKSNAEDelkqlRDRADAAEKLRklaQEEAEKLRK-QVSEETQKKRLAE--EELKHKSEAER--------KAANEKQKAL 2622
Cdd:pfam02841 203 EKAIEAE-----RAKAEAAEAEQ---ELLREKQKEeEQMMEAQERSYQEhvKQLIEKMEAEReqllaeqeRMLEHKLQEQ 274
|
250 260
....*....|....*....|...
gi 1655274895 2623 EDL--ENLRMQAEEAERQVKQAE 2643
Cdd:pfam02841 275 EELlkEGFKTEAESLQKEIQDLK 297
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2194-2577 |
7.16e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2194 QYENCLREVHTVPNDVKEVETYRTN----------LKKMRAEAEAEQP-VFDSLEEELKKASAVSDKMSRVHSERDAELD 2262
Cdd:PRK01156 340 DYIKKKSRYDDLNNQILELEGYEMDynsylksiesLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIKKELNEINVKLQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2263 QHRQHLSSLQDRWKAVFTQIDLRQRELDQL---------GRQLGyYRESYDWLIRWIADAKQRQENIQAVPItDSKTLKE 2333
Cdd:PRK01156 420 DISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcGTTLG-EEKSNHIINHYNEKKSRLEEKIREIEI-EVKDIDE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2334 QLAKEKKLLEEIEKnkdkvDECQKYAKAYiDIIKDYELQLVAYKAQVEPLT-SPLKKTKLDSASDNIIQEyvTLRTRYSE 2412
Cdd:PRK01156 498 KIVDLKKRKEYLES-----EEINKSINEY-NKIESARADLEDIKIKINELKdKHDKYEEIKNRYKSLKLE--DLDSKRTS 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2413 LMTLTSQYIKFITDTQRRLEDEEKA----AEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQE-- 2486
Cdd:PRK01156 570 WLNALAVISLIDIETNRSRSNEIKKqlndLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKlr 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2487 ---EVSKRETAAVDAEKQKQNiqlELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIhliriqlETTVKQKSNAEDELK 2563
Cdd:PRK01156 650 gkiDNYKKQIAEIDSIIPDLK---EITSRINDIEDNLKKSRKALDDAKANRARLESTI-------EILRTRINELSDRIN 719
|
410
....*....|....
gi 1655274895 2564 QLRDRADAAEKLRK 2577
Cdd:PRK01156 720 DINETLESMKKIKK 733
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2428-2509 |
7.62e-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: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2428 QRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQL 2507
Cdd:COG2268 225 EAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEA 304
|
..
gi 1655274895 2508 EL 2509
Cdd:COG2268 305 EL 306
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
3037-3194 |
7.75e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.55 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3037 KLKNIAEETQQSKLRAEEEAEKLR-RLVLEEEMRRKEAEdkvkkiaaaeeeaaRQRKAAQEELdrLQKKADEVRKQKEEA 3115
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRgKAERDAEHIKKTAK--------------RESKALKKEL--LLEAKEEARKYREEI 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274895 3116 DKEAEKQIVAAQQaalkcnMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAER 3194
Cdd:PRK00106 89 EQEFKSERQELKQ------IESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2792-3009 |
7.91e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2792 AQQKLAAEQEliRLRADFDNAEQQRSLLEDELyRLKNeviAAQQERKQLEDE----LSKVRSEMDILIQLKSRAEKETMS 2867
Cdd:PRK05035 442 EQEKKKAEEA--KARFEARQARLEREKAAREA-RHKK---AAEARAAKDKDAvaaaLARVKAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2868 NTEkskqllEAEATKLRDLAEEASKLRAIAEEAKHQRQlAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKE 2947
Cdd:PRK05035 516 NSA------VIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIAR 588
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 2948 AENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDtlKQRRV 3009
Cdd:PRK05035 589 AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP--RKAAV 648
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2955-3218 |
7.98e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2955 RQAEDEAYQRKILEDQANQHKLEIEEKIvllkkssdAEMERQKAivddtlkqrrvvEEEIRILKLNFEKASSGKLDLELE 3034
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEARQ--------ARLEREKA------------AREARHKKAAEARAAKDKDAVAAA 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3035 LNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRK-AAQEELDRLQKKADEVRKQKE 3113
Cdd:PRK05035 492 LARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAvAAAIARAKAKKAAQQAANAEA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3114 EADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKE----------RAEREAA 3183
Cdd:PRK05035 572 EEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANaepeepvdprKAAVAAA 651
|
250 260 270
....*....|....*....|....*....|....*
gi 1655274895 3184 LLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRK 3218
Cdd:PRK05035 652 IARAKARKAAQQQANAEPEEAEDPKKAAVAAAIAR 686
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
3567-3685 |
8.49e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3567 TVLQQtFLTEKEMLlkkEKLIEDEKKKLESQfEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKdiln 3646
Cdd:pfam02841 176 EVLQE-FLQSKEAV---EEAILQTDQALTAK-EKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVK---- 246
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655274895 3647 KQKEMQELERKRL--EQERVLAdenQKLREKLQQMEEAQKS 3685
Cdd:pfam02841 247 QLIEKMEAEREQLlaEQERMLE---HKLQEQEELLKEGFKT 284
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3276-3672 |
8.51e-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: 42.37 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3276 TDKQKSLLDDELQRLKDEVddaMRQKASVEEELFKVKIQMEELMKLKVRIEEenqrLMKkdkdntqkfLVEEAENMKK-- 3353
Cdd:pfam05622 57 GGKKYLLLQKQLEQLQEEN---FRLETARDDYRIKCEELEKEVLELQHRNEE----LTS---------LAEEAQALKDem 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3354 --LAEDAARLSIEAQEAARLRQIAED--DLNQQ-RTLAEKMLKEKMQAIQEASRLKaEAEMLQRQKDLAQEQAQKLledk 3428
Cdd:pfam05622 121 diLRESSDKVKKLEATVETYKKKLEDlgDLRRQvKLLEERNAEYMQRTLQLEEELK-KANALRGQLETYKRQVQEL---- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3429 qlmQQRLDEETE-------EYQRS---LEAERKRQLEIIAEAEKLK-----LQVSQLSEAQAKAEEEAKKFKKQ-ADTIA 3492
Cdd:pfam05622 196 ---HGKLSEESKkadklefEYKKLeekLEALQKEKERLIIERDTLRetneeLRCAQLQQAELSQADALLSPSSDpGDNLA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3493 ARLHETEIATK-EQMTEVKKM--------EFEKLNT-SKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQ- 3561
Cdd:pfam05622 273 AEIMPAEIREKlIRLQHENKMlrlgqegsYRERLTElQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQg 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3562 --------IEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEI--------KKAKALKDEQDRQRQQMEEEKLK 3625
Cdd:pfam05622 353 skaedsslLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIdelqealrKKDEDMKAMEERYKKYVEKAKSV 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1655274895 3626 LKaTMDAALNKQKEAE-----KDILNKQKEMQELERKrLEQERVLADENQKL 3672
Cdd:pfam05622 433 IK-TLDPKQNPASPPEiqalkNQLLEKDKKIEHLERD-FEKSKLQREQEEKL 482
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2391-2541 |
8.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2391 KLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAE---EQKKMAEMQAELD---KQKQLaE 2464
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEieeVEARIKKYEEQLGnvrNNKEY-E 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2465 AHAKAIAKAEKEAQELK---LRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEI 2541
Cdd:COG1579 93 ALQKEIESLKRRISDLEdeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2875-3438 |
8.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2875 LLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEE--DAARQR---AEAERILKEKLAAISDATRLKTEAEIALKEKEAE 2949
Cdd:COG3899 676 LEARGPEPLEERLFELAHHLNRAGERDRAARLLLRaaRRALARgayAEALRYLERALELLPPDPEEEYRLALLLELAEAL 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2950 NERLRRQAEDEAYQRkILEDQANQHKLEIEekIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRIL-KLNFEKASSGK 3028
Cdd:COG3899 756 YLAGRFEEAEALLER-ALAARALAALAALR--HGNPPASARAYANLGLLLLGDYEEAYEFGELALALAeRLGDRRLEARA 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3029 LDLELELNKLKNIAEETQQSKLRAEEEAEKL--RRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKAD 3106
Cdd:COG3899 833 LFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAA 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3107 EVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLR 3186
Cdd:COG3899 913 LAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALE 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3187 QQAEEAERQKVAAEQEAANQAkAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQEL 3266
Cdd:COG3899 993 AAAAALLALLAAAAAAAAAAA-ALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAA 1071
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3267 TKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVE 3346
Cdd:COG3899 1072 AAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLL 1151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3347 EAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLE 3426
Cdd:COG3899 1152 LAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAAL 1231
|
570
....*....|..
gi 1655274895 3427 DKQLMQQRLDEE 3438
Cdd:COG3899 1232 ALAAALLALRLL 1243
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3548-3684 |
8.65e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3548 QNKSKEMADAQQ---KQIEREMTVLQQTFLTEKEML--LKKEKLIEDEKKKlesQFEEEIKKAK-ALKDEQDRQRQQMEE 3621
Cdd:PRK09510 68 QQQQKSAKRAEEqrkKKEQQQAEELQQKQAAEQERLkqLEKERLAAQEQKK---QAEEAAKQAAlKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274895 3622 EKLKLKATMDAALNKQKEAEKDilnKQKEMQELERKRLEQErvlADENQKLREKLQQMEEAQK 3684
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAE---AKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKK 201
|
|
| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
3587-3687 |
8.65e-03 |
|
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 38.72 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3587 IEDEKKKLESQFEEEIKKAKALKDEQdrqrQQMEEEKLKLKATMDAALNKQKEAEKDilnkqKEMQELERKRLeqeRVLA 3666
Cdd:pfam08647 1 LQTELVKLEQAFEELSEQLDKKVKDL----TILEEKKLRLEAEKAKADQKYFAAMRS-----KDALENENKKL---NTLL 68
|
90 100
....*....|....*....|.
gi 1655274895 3667 DENQKLREKLQQMEEAQKSTL 3687
Cdd:pfam08647 69 SKSSELIEQLKETEKEFVRKL 89
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2434-2587 |
8.76e-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: 41.90 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2434 EEKAAEKLK---AEEQKKMAEMQAELDKQKqlaeahakAIAKAEKEAQELKLRMQEEVskretaavdAEKqkqniqlelh 2510
Cdd:cd03406 169 EAMEAEKTKlliAEQHQKVVEKEAETERKR--------AVIEAEKDAEVAKIQMQQKI---------MEK---------- 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274895 2511 elknlseqqikdksqqvdEALKSRLRIEEEIHLIRiqlettvkqksnaedelkqLRDRADaAEKLRKLAQEEAEKLR 2587
Cdd:cd03406 222 ------------------EAEKKISEIEDEMHLAR-------------------EKARAD-AEYYRALREAEANKLK 260
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
3247-3568 |
8.77e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3247 KHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEvdDAMRQKASVE---EELFKVKIQMEElmklkV 3323
Cdd:pfam03528 1 QPDEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE--DLKRQNAVLQeaqVELDALQNQLAL-----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3324 RIEEENQRLMKKDKDNTQKFLV--------EEAENMKKLAEDAARlSIEAQEAARLRQiAEDDLNQQRTLAEKMLKEKMQ 3395
Cdd:pfam03528 74 RAEMENIKAVATVSENTKQEAIdevksqwqEEVASLQAIMKETVR-EYEVQFHRRLEQ-ERAQWNQYRESAEREIADLRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3396 AIQEASrlkaEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDE------ETEEYQRSLEAERKRQLEIIAEAEK-----LK 3464
Cdd:pfam03528 152 RLSEGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3465 LQVSQLSEAQAKAEEEAKKFKKQADTIaARLHETEIATKEQMTEVKKMEFEKLNTSKE--ADDLRKAITELEKEKAR--- 3539
Cdd:pfam03528 228 MYVAVLNTQKSVLQEDAEKLRKELHEV-CHLLEQERQQHNQLKHTWQKANDQFLESQRllMRDMQRMESVLTSEQLRqve 306
|
330 340 350
....*....|....*....|....*....|
gi 1655274895 3540 -LKKEAEEHQNKSKEMADAQQKQIEREMTV 3568
Cdd:pfam03528 307 eIKKKDQEEHKRARTHKEKETLKSDREHTV 336
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2883-2980 |
8.83e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2883 LRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERIlkEKLAAisdatrlktEAEIALKEKEAENERLRRQA----- 2957
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL--EGLAA---------ELEEKQQELEAQLEQLQEKAaetsq 212
|
90 100
....*....|....*....|...
gi 1655274895 2958 EDEAYQRKILEDQANQHKLEIEE 2980
Cdd:PRK11448 213 ERKQKRKEITDQAAKRLELSEEE 235
|
|
| 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 ... |
2916-3007 |
8.95e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.60 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2916 AEAERILKEKLAAISdatrlktEAEIALKEKEAENERLRRQAEDEAYQrkiledQANQHKLEIEEKIVLLKKSSDAEMER 2995
Cdd:pfam00430 40 AEAEERRKDAAAALA-------EAEQQLKEARAEAQEIIENAKKRAEK------LKEEIVAAAEAEAERIIEQAAAEIEQ 106
|
90
....*....|..
gi 1655274895 2996 QKAIVDDTLKQR 3007
Cdd:pfam00430 107 EKDRALAELRQQ 118
|
|
| PRK13455 |
PRK13455 |
F0F1 ATP synthase subunit B; Provisional |
2564-2685 |
9.06e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184062 [Multi-domain] Cd Length: 184 Bit Score: 40.94 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2564 QLRDRADAAEKLRklaqEEAEKL-----RKQVSEETQKKRLAEEElkhKSEAERkAANEKQKALEDLENLRMQAeeAERQ 2638
Cdd:PRK13455 62 GIRSELEEARALR----EEAQTLlasyeRKQREVQEQADRIVAAA---KDEAQA-AAEQAKADLEASIARRLAA--AEDQ 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655274895 2639 VKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQ 2685
Cdd:PRK13455 132 IASAEAAAVKAVRDRAVSVAVAAAADVIAKQMTAADANALIDEAIKE 178
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
2858-2960 |
9.25e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 42.61 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2858 KSRaeKETMSNT-EKSK------QLLEAEATKLR-----DLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAE--RILK 2923
Cdd:pfam04147 162 KSK--KEVMEEViAKSKlhkyerQKAKEEDEELReeldkELKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVR 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1655274895 2924 E----KLAAISDatRLKTEAEIALKEKE----AENERLRR-QAEDE 2960
Cdd:pfam04147 240 ElafdKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRmRGEED 283
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
3363-3704 |
9.39e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3363 IEAQEAARLRQIAEDDLNQQRTlaekmlkekmQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLE--DKQLMQQR--LDEE 3438
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3439 TEEYQRSLEAERKrqlEIIAEAEKLK-LQVSQLSEAQAKaeeeakkfkkqadtiaarlheTEIATKEQMTEVKKMEFEK- 3516
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKYSLQKKV---------------------SEMEQKLQLHLLAKEDHHKq 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3517 LNtskEADDLRKAITE---LEKEK-ARLKKEAEEHQNKSKEMADAQQKQiEREMTVLQqtflteKEMLLKKEKLIedeKK 3592
Cdd:pfam15818 136 LN---EIEKYYATITGqfgLVKENhGKLEQNVQEAIQLNKRLSALNKKQ-ESEICSLK------KELKKVTSDLI---KS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3593 KLESQF---EEEIKKA-KALKDEQDRQRQQMEeekLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADE 3668
Cdd:pfam15818 203 KVTCQYkmgEENINLTiKEQKFQELQERLNME---LELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAE 279
|
330 340 350
....*....|....*....|....*....|....*.
gi 1655274895 3669 NQKLREKLQQMEeaQKSTLITEKHVTVVETVLNGQN 3704
Cdd:pfam15818 280 LKALKENNQTLE--RDNELQREKVKENEEKFLNLQN 313
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
3089-3453 |
9.42e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3089 RQRKaaqeeldrlQKKADEVRKQKEEADKEAE-KQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL 3167
Cdd:pfam02029 9 RERR---------RRAREERRRQKEEEEPSGQvTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3168 ARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAK 3247
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3248 HKKLAEQTLKQK---FQVEQELTKVKLQLEETDKQKSLLDDELQRLkdevddamrqkasveeelfKVKIQMEELMKLKVR 3324
Cdd:pfam02029 160 EDKSEEAEEVPTenfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHP-------------------EVKSQNGEEEVTKLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3325 IEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLS-IEAQEAARLRQiaeddlNQQRTLAE-KMLKEKMQaiqeaSR 3402
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQeKESEEFEKLRQ------KQQEAELElEELKKKRE-----ER 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1655274895 3403 LKAEAEMLQRQKDLAQEQAQKLLEDKqlmqQRLDEETEeyQRSLEAERKRQ 3453
Cdd:pfam02029 290 RKLLEEEEQRRKQEEAERKLREEEEK----RRMKEEIE--RRRAEAAEKRQ 334
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3043-3221 |
9.50e-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: 42.25 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3043 EETQQSKLRAEEEAEKLRRLVLE------EEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEvRKQKEEAD 3116
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVErkrreqEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEE-RQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 3117 KEAEKQIVAAQQAAlkcnmaEQQVQSVlaQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEA---- 3192
Cdd:pfam15709 408 RKQRLQLQAAQERA------RQQQEEF--RRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEErley 479
|
170 180
....*....|....*....|....*....
gi 1655274895 3193 ERQKvaaeqeAANQAKAQDDAERLRKDAE 3221
Cdd:pfam15709 480 QRQK------QEAEEKARLEAEERRQKEE 502
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2819-3072 |
9.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2819 LEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILI----QLKSRAEK------ETMSNTEKSKQLLEAEATKLRDLAE 2888
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNaqvkELREEAQElrekrdELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2889 EASKLRAIAEEAKHQRQlaEEDAARQR--------------AEAERILKEKLAAIS---DATRLKTEAEIALKEKEAENE 2951
Cdd:COG1340 93 ELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIKELEkelEKAKKALEKNEKLKELRAELK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274895 2952 RLRRQAEDEAYQRKILEDQANQHKLEIEE---KIVLLKKSSD---AEMERQKAIVDDTLKQRRVVEEEIRilklnfekas 3025
Cdd:COG1340 171 ELRKEAEEIHKKIKELAEEAQELHEEMIElykEADELRKEADelhKEIVEAQEKADELHEEIIELQKELR---------- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1655274895 3026 sgklDLELELNKLKNIAEETqqsKLRAEEEAEKLRRLVLEEEMRRKE 3072
Cdd:COG1340 241 ----ELRKELKKLRKKQRAL---KREKEKEELEEKAEEIFEKLKKGE 280
|
|
| |
