|
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 ... |
41-150 |
1.35e-74 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 243.85 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 41 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQV 120
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKI 75
|
90 100 110
....*....|....*....|....*....|
gi 530389149 121 KLVNIRNDDIADGNPKLTLGLIWTIILHFQ 150
Cdd:cd21188 76 KLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
163-268 |
1.03e-71 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 235.69 E-value: 1.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 530389149 243 PEDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
38-161 |
2.43e-71 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 235.30 E-value: 2.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 38 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530389149 118 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 161
Cdd:cd21235 76 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
37-159 |
8.53e-70 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 231.03 E-value: 8.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 37 QDERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLR 116
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLK 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530389149 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 159
Cdd:cd21236 86 RRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
164-268 |
3.26e-66 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 219.96 E-value: 3.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 530389149 244 EDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
38-160 |
3.04e-61 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 206.42 E-value: 3.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 38 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530389149 118 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 160
Cdd:cd21237 76 RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
164-268 |
2.88e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.43 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 530389149 244 EDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
162-268 |
1.71e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 177.93 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 162 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 241
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 530389149 242 DPEDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
43-151 |
1.04e-48 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 169.87 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 43 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 122
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77
|
90 100
....*....|....*....|....*....
gi 530389149 123 VNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21186 78 VNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
37-147 |
3.74e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 162.92 E-value: 3.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 37 QDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYL 115
Cdd:cd21246 10 ADEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFL 84
|
90 100 110
....*....|....*....|....*....|..
gi 530389149 116 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21246 85 KEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
164-264 |
8.69e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 161.43 E-value: 8.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 530389149 244 EDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
36-264 |
1.34e-44 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 173.97 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 36 EQDERDRVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALD 113
Cdd:COG5069 2 EAKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 114 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSW 192
Cdd:COG5069 78 FIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSW 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 193 RDGRLFNAIIHRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 264
Cdd:COG5069 155 RDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
39-151 |
1.89e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.92 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 39 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 116
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*
gi 530389149 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21241 78 SKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
39-151 |
3.79e-44 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 156.96 E-value: 3.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 39 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 116
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 530389149 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
164-264 |
5.92e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 530389149 244 EDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
37-147 |
1.05e-42 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 153.22 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 37 QDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYL 115
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL 84
|
90 100 110
....*....|....*....|....*....|..
gi 530389149 116 rHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21193 85 -KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
163-268 |
3.89e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 148.24 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 530389149 243 PEDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
151-266 |
6.87e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 147.89 E-value: 6.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
39-151 |
2.36e-39 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 143.43 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 39 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNK 77
|
90 100 110
....*....|....*....|....*....|...
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21242 78 SIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
160-264 |
1.75e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.91 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 160 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 239
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 530389149 240 LLDPEDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
38-147 |
4.33e-38 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 140.93 E-value: 4.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 38 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 116
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
160-264 |
6.45e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.42 E-value: 6.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 160 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 239
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 530389149 240 LLDPEDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
37-147 |
1.01e-37 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 139.42 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 37 QDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYL 115
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFL 99
|
90 100 110
....*....|....*....|....*....|..
gi 530389149 116 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21317 100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
163-264 |
3.39e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 137.30 E-value: 3.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 530389149 243 PEDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
41-147 |
1.51e-36 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 135.21 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 41 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQ 119
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKG 77
|
90 100
....*....|....*....|....*...
gi 530389149 120 VKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21214 78 VKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
43-149 |
2.20e-36 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 134.84 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 43 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 120
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGV 78
|
90 100
....*....|....*....|....*....
gi 530389149 121 KLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21215 79 KLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
38-151 |
6.75e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 133.51 E-value: 6.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 38 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQK 76
|
90 100 110
....*....|....*....|....*....|....
gi 530389149 118 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21231 77 NNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1344-2056 |
8.41e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 151.45 E-value: 8.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1423
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1424 Q----EELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEATERQRGGAEGELQALRA--RAEEAEAQKRQA 1497
Cdd:PTZ00121 1192 ElrkaEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeEARMAHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1498 QEEAERLRRQVQ-DESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQ 1576
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK-KKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1577 rsAEAELQSKRASFAEKTAQLERSLQEEHvavaqlreeaerraqqqaeaerareeaerelerwQLKANEAlrlRLQAEEV 1656
Cdd:PTZ00121 1350 --AEAEAAADEAEAAEEKAEAAEKKKEEA----------------------------------KKKADAA---KKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1657 AQQKSLAQaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQ 1735
Cdd:PTZ00121 1391 KKADEAKK------------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1736 LLEEelarlQREAAAATQKRQEL-EAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEaEAGRFRELAEEAARLRAl 1814
Cdd:PTZ00121 1452 KAEE-----AKKAEEAKKKAEEAkKADEAKKKAE-------EAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK- 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1815 AEEAKRQRQLAEEDAARQRAEA----ERVLAEKLAAIGEATRL--KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1888
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAkkaeEKKKADELKKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1889 AAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRrqveEEILALKASFEKAAAGKAELELELGRIRS-----NAEDT 1963
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1964 LRSKEQA--ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQES 2037
Cdd:PTZ00121 1674 KKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDE 1753
|
730
....*....|....*....
gi 530389149 2038 ARQLQLAQEAAQKRLQAEE 2056
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEE 1772
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
167-268 |
1.14e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 132.55 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 167 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 530389149 246 VDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
148-264 |
4.72e-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: 131.71 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 148 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQA 227
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 228 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
163-261 |
1.57e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.69 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 530389149 243 PEDVDVPQPDEKSIITYVS 261
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
164-264 |
1.80e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 123.67 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 530389149 244 EDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
43-151 |
9.12e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 121.65 E-value: 9.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 43 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 122
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVEL 77
|
90 100
....*....|....*....|....*....
gi 530389149 123 VNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21232 78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
42-152 |
1.16e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 121.79 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 42 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ 119
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDE 88
|
90 100 110
....*....|....*....|....*....|....
gi 530389149 120 -VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21311 89 gIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
43-151 |
1.22e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 121.24 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 43 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 120
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGI 78
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 121 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21227 79 KLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
151-266 |
3.16e-31 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 120.33 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 151 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 231 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 266
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
167-268 |
5.04e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 119.29 E-value: 5.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 167 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 530389149 246 VDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
167-269 |
1.47e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.11 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 167 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 244
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 530389149 245 DVDVPQPDEKSIITYVSSLYDAMPR 269
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
163-261 |
1.85e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 530389149 243 PEDVDVPQPDEKSIITYVS 261
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
38-147 |
2.84e-30 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 118.99 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 38 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 116
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
39-153 |
3.38e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.30 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 39 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLR 116
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 153
Cdd:cd21191 78 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
169-264 |
3.99e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 116.68 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 169 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 247
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 530389149 248 VPQPDEKSIITYVSSLY 264
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1174-2058 |
2.22e-29 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 129.83 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1174 ERDVEVERWRERVAQLLERwqavlaqtdvRQRELEQLGRQLRYYRESADplgawlqDARRRQEQIQAMPLADSQAVREQL 1253
Cdd:COG1196 172 ERKEEAERKLERTEENLER----------LEDLLEELEKQLEKLERQAE-------KAERYQELKAELRELELALLLAKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1254 RQEQALLEEIErhgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpkvqsgseSVIQEYVDLRTHYSELTT 1333
Cdd:COG1196 235 KELRKELEELE---EELSRLEEELEELQEELEEAEKEIEELKSELE----------------ELREELEELQEELLELKE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1334 LtsqyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvrreeaa 1413
Cdd:COG1196 296 E----IEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL-------- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1414 vdaQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1493
Cdd:COG1196 364 ---EEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1494 KRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAeEAERRLRQAEVERARQV----- 1568
Cdd:COG1196 441 LEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQ-RASQGVRAVLEALESGLpgvyg 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1569 ------------QVALETAQRSAEAELQSKRASFAEKTAQLERSlQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL 1636
Cdd:COG1196 520 pvaelikvkekyETALEAALGNRLQAVVVENEEVAKKAIEFLKE-NKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1637 ERWQLKANEALRLRL----------QAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLA 1706
Cdd:COG1196 599 IDFDPKYEPAVRFVLgdtlvvddleQARRLARKLRIKYRIVTLDGDLVEPSGSITGGSRNK--RSSLAQKRELKELEEEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1707 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrst 1786
Cdd:COG1196 677 AELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEE---- 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1787 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA 1866
Cdd:COG1196 753 LEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEE 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1867 ENERLRRLAEDEAFQRRRLEE---QAAQHKADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEILALKASFEKAA 1943
Cdd:COG1196 833 LEEEIEELEEKLDELEEELEElekELEELKEELEELEAEKEELED-ELKELEEEKEELEEELRELESELAELKEEIEKLR 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1944 AGKAELELELGRIRSNAEDTLRSKEQAELEaarqrqlaaeeerrrrEAEERVQKSLAAEEEAARQRK----AALEEVERL 2019
Cdd:COG1196 912 ERLEELEAKLERLEVELPELEEELEEEYED----------------TLETELEREIERLEEEIEALGpvnlRAIEEYEEV 975
|
890 900 910
....*....|....*....|....*....|....*....
gi 530389149 2020 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKA 2058
Cdd:COG1196 976 EERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKET 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1682-2465 |
2.39e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 130.26 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1682 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1761
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEE--ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1762 LAKvRAEmevllasKARAEEESRSTSEKSKqrleaeagrfrelAEEAARlralAEEAKRQRQLAEEDAARQRAEAERvlA 1841
Cdd:PTZ00121 1174 DAK-KAE-------AARKAEEVRKAEELRK-------------AEDARK----AEAARKAEEERKAEEARKAEDAKK--A 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1842 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRleeqaAQHKADIEERLAQLRKASdselERQKGLVEDT 1921
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ-----AAIKAEEARKADELKKAE----EKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1922 LRQRRQVEEeilalkasfekaAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAA 2001
Cdd:PTZ00121 1298 AEEKKKADE------------AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2002 EEEAARQRKAALEEVERLKAKVEEARR---LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2078
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2079 SvlDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQsaeeqaqaraqaqaaaekLRKEAEQEAARRAQAE 2158
Cdd:PTZ00121 1446 A--DEAK--KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE------------------AKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2159 QAALRQKQAADAEMEKHKKFAEQTlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQrlKAEATEAARQRSQVEEELFSV 2238
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2239 RVQMEELSKL-KARIEAENRALILRDKDNTQRFLQEEAEKMKqvAEEAARlsvaAQEAARLRQLAEEDLAQQRALAEKML 2317
Cdd:PTZ00121 1580 LRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2318 KEKMQAVQEATRLKAEAEllqQQKELAQEqARRLQEDKEQMAQQLAEETQgfqrtlEAERQRQLEMSAEAERLKlrVAEM 2397
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAE---EDKKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK--AEEL 1721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 2398 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvTLVQTLEIQRQQSDHDAERLREAIAELEREKE 2465
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
149-266 |
5.58e-29 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 114.41 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 149 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAF 228
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 530389149 229 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
899-976 |
6.27e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 436447 Cd Length: 78 Bit Score: 112.30 E-value: 6.27e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 899 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 976
Cdd:pfam18373 1 VSWQYLLKDIERIRSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNACQQHYQTLLVS 78
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
42-149 |
1.36e-28 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 112.57 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1319-2032 |
1.58e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.09 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1319 QEYVDLRTHYSELT-TLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqAKAQAEREAKE 1397
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1398 LQQRMQEEVVRREeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1477
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1478 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1557
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1558 RQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL- 1636
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1637 ---------------ERWQLKANEALRLRLQA----------EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1691
Cdd:TIGR02168 518 lsgilgvlselisvdEGYEAAIEAALGGRLQAvvvenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1692 RELA------------------------------EQELEKQRQL-----------------------AEGTAQQRLAAEQ 1718
Cdd:TIGR02168 598 EGFLgvakdlvkfdpklrkalsyllggvlvvddlDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1719 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRL 1794
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1795 EAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAeialKEKEAENERLRRL 1874
Cdd:TIGR02168 758 ELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1875 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAGKAELELELG 1954
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1955 RIRSNAE--DTLRSKEQAELEAARQR------QLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK----AK 2022
Cdd:TIGR02168 912 ELRRELEelREKLAQLELRLEGLEVRidnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAA 991
|
810
....*....|
gi 530389149 2023 VEEARRLRER 2032
Cdd:TIGR02168 992 IEEYEELKER 1001
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
167-266 |
3.10e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.22 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 167 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 245
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 530389149 246 VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1727-2611 |
1.14e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.87 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1727 TEQGEQQRQLLEEELARLQREAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1804
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1805 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAIGEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 1882
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1883 RRLEEQaaqHKADIEERLAQLRKASDSelerqkglvedtlrqrRQVEEeilalkasfekaaAGKAELELELGRIRsNAED 1962
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1963 TLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2042
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2043 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTlqqeqsvldqlrgeaeaarraaeeaeearVQAEREAAQSRRQVEEAERL 2122
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKK-----------------------------ADAAKKKAEEAKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2123 KQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2202
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2203 TDHQknlldEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARiEAENRALILRDKDNtqrfLQEEAEKMKQVA 2282
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADE----AKKKAEEAKKKA 1499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2283 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeQM 2358
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NM 1578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2359 AQQLAEETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtlvqt 2438
Cdd:PTZ00121 1579 ALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK----- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2439 leiqrqqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLlqetqalqqsflsEKDSLLQRErfiEQEK 2518
Cdd:PTZ00121 1647 ---------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-------------KAAEALKKE---AEEA 1701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2519 AKLEQL---FQDEVAKAQqlreEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEE 2595
Cdd:PTZ00121 1702 KKAEELkkkEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
890
....*....|....*.
gi 530389149 2596 NQRLREQLQLLEEQHR 2611
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRR 1793
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
151-266 |
2.50e-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: 109.40 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1404-2121 |
1.10e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.40 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1404 EEVVrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL 1483
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1484 RARAEEaEAQKRQAQEEAERLRRqvqdeSQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQ-AEEAERRLRQAEV 1562
Cdd:PTZ00121 1108 TGKAEE-ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1563 ERARQVQVALETaqRSAEaelQSKRASFAEKtAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1642
Cdd:PTZ00121 1182 RKAEEVRKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1643 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELI 1721
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKKaDAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1722 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE-----A 1796
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkaA 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1797 EAGRFRELAEEAARLRALAEEAKRQRQLAEE-DAARQRAEAERVlAEKLAAIGEATRLKTEAEIALKEKEAENErLRRLA 1875
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADE-AKKKA 1492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1876 EDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGR 1955
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKK 1571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1956 IRSNAEDTLRSKEQA-ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE--EVERLKAKVEE----ARR 2028
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkKVEQLKKKEAEekkkAEE 1651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2029 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAERE 2108
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
730
....*....|...
gi 530389149 2109 AAQSRRQVEEAER 2121
Cdd:PTZ00121 1732 AEEAKKEAEEDKK 1744
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
151-266 |
1.39e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.50 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1690-2481 |
4.49e-26 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 119.05 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1690 RQRELAEQELEKQRQLaegtaqQRLAAEQELIRLRAETEQgeqqRQLLEEELARLQREAAAATQKRQELEAELAKVRAEM 1769
Cdd:COG1196 207 RQAEKAERYQELKAEL------RELELALLLAKLKELRKE----LEELEEELSRLEEELEELQEELEEAEKEIEELKSEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1770 EVLLASKARAEEESRSTSEKsKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGE 1849
Cdd:COG1196 277 EELREELEELQEELLELKEE-IEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1850 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGL----------VE 1919
Cdd:COG1196 356 LEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLkeelkeleaeLE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1920 DTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRskeqaELEAARQRQLAAEEERRRREAEERVQKSL 1999
Cdd:COG1196 436 ELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEK-----ELSSLEARLDRLEAEQRASQGVRAVLEAL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2000 AAEEEAArqrKAALEEVERLKAKVEEA--RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAvqqkeqelqqtlqqe 2077
Cdd:COG1196 511 ESGLPGV---YGPVAELIKVKEKYETAleAALGNRLQAVVVENEEVAKKAIEFLKENKAGRATFL--------------- 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2078 qsVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQV-------------EEAERLkqsAEEQAQARAQAQAAAEKLR 2144
Cdd:COG1196 573 --PLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVrfvlgdtlvvddlEQARRL---ARKLRIKYRIVTLDGDLVE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2145 KEAE----QEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQ----KAQVEQELTTLRLQLEETDHQKNLLDEELQR 2216
Cdd:COG1196 648 PSGSitggSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSlkneLRSLEDLLEELRRQLEELERQLEELKRELAA 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2217 LKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRfLQEEAEKMKQVAEEAARLSVAAQEAA 2296
Cdd:COG1196 728 LEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEE-IEELEEKRQALQEELEELEEELEEAE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2297 RLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQ---EDKEQMAQQLAEETQGFQRTL 2373
Cdd:COG1196 807 RRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKeelEELEAEKEELEDELKELEEEK 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2374 EAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSD------ 2447
Cdd:COG1196 887 EELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEAlgpvnl 966
|
810 820 830
....*....|....*....|....*....|....*..
gi 530389149 2448 ---HDAERLREAIAELEREKEKLQQEAKLLQLKSEEM 2481
Cdd:COG1196 967 raiEEYEEVEERYEELKSQREDLEEAKEKLLEVIEEL 1003
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
37-151 |
4.98e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 106.00 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 37 QDERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYL 115
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFL 90
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 116 RHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21247 91 KTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1106-1859 |
1.52e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1106 AEEVLRAHE-EQLKEAQAVPATLPELEATKASLKKlRAQ----AEAQQPTFDALR-DELRGAQEVGERLQQRHGERDVEV 1179
Cdd:PTZ00121 1136 AEDARKAEEaRKAEDAKRVEIARKAEDARKAEEAR-KAEdakkAEAARKAEEVRKaEELRKAEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1180 ERWR----ERVAQLLERWQAVLAQTD-VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVR--EQ 1252
Cdd:PTZ00121 1215 EEARkaedAKKAEAVKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDE 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1253 LR--QEQALLEEIERHGEKVEECQRFAKQYINAIKDYELqlVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTHYSE 1330
Cdd:PTZ00121 1295 AKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEA-----EAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1331 LTTLTSQYIKFISETLRRMEEEERLAEQ--QRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAKELQQRmQEEVVR 1408
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKK-AEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1409 REEAAVDAQQQKRSiqEELQQlrqsseaeiqaKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGElQALRARAE 1488
Cdd:PTZ00121 1446 ADEAKKKAEEAKKA--EEAKK-----------KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKK 1511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1489 EAEAQKRQAQEEAERLRRqvqdeSQRKRQAEvelasrvkaEAEAAREKQRAlqalEELRlQAEEAERRLRQAEVERARQV 1568
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKK-----AEEAKKAD---------EAKKAEEKKKA----DELK-KAEELKKAEEKKKAEEAKKA 1572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1569 QVALETAQRSAE--AELQSKRASFAEKTAQLERSLQEEHVAvaqlreeaerraqqqaeaerareeaerelerwqlKANEA 1646
Cdd:PTZ00121 1573 EEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAK----------------------------------KAEEA 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1647 lrlRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRElaeqELEKQRQLAEGTAQQRLAAEQELIRLRAE 1726
Cdd:PTZ00121 1619 ---KIKAEELKKAEEEKKKVEQLK------------KKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1727 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakVRAEMEVllaskARAEEESRSTSEKSKQRLEAEAGRFRELAE 1806
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE---KKKAEEL-----KKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1807 EAARLRALAEEAKRQRQLAEEdaarQRAEAERVLAEKLAAIGEATRLKTEAEI 1859
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
42-149 |
1.83e-25 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 103.72 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERE 77
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21228 78 SIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
169-264 |
2.70e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.00 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 169 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 247
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 530389149 248 VPQPDEKSIITYVSSLY 264
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
151-266 |
3.69e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 103.23 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
42-152 |
1.07e-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: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDRE 89
|
90 100 110
....*....|....*....|....*....|....
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21310 90 HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1686-2524 |
1.13e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.38 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1686 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1765
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1766 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1845
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1846 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrRLEEQAAQHKADIEERLAQLrkaSDSELERQKGLVEDTLRQR 1925
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1926 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdtlrsKEQAELEAARQRQLaaeeerrrreaeervqkSLAAEEEA 2005
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2006 ARQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQ 2065
Cdd:TIGR02168 487 LQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2066 KEQELQQTLQQEQSVLDQ-LRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEE-------AERLKQSAEEQAQARAQAQ 2137
Cdd:TIGR02168 567 QNELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2138 AAAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRL 2217
Cdd:TIGR02168 647 IVTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2218 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEnralilrdkdntqrfLQEEAEKMKQVAEEAARLSVAAQEAAR 2297
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2298 LRQLAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleae 2376
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2377 rqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA 2456
Cdd:TIGR02168 849 -----ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 2457 IAELEREKEKLQQEAKLLQlkseemQTVQQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2524
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
163-269 |
1.31e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 Cd Length: 109 Bit Score: 101.21 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 163 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 239
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 240 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 269
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1408-2253 |
1.93e-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: 113.61 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1408 RREEAavdaQQQKRSIQEELQQL---RQSSEAEIQAKARQAEAAERSRlRIEEEIRvvrlqleaterqrggaEGELQALR 1484
Cdd:TIGR02168 173 RRKET----ERKLERTRENLDRLediLNELERQLKSLERQAEKAERYK-ELKAELR----------------ELELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1485 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLR--QAEV 1562
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1563 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLErSLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLK 1642
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELE-----------------------ELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1643 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIR 1722
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1723 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGR 1800
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1801 FRELAEEAARLRALAEEAKRQR--QLAEEDAARQRAEAErvlAEKLAAIGEATRLkteAEIALKEKEAENERLRRLAEDE 1878
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGRlqAVVVENLNAAKKAIA---FLKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1879 AFQR--RRLEEQAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILALKASFEKAAAG----KAELELE 1952
Cdd:TIGR02168 599 GFLGvaKDLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1953 LGRI-RSNAEDTLRSK-EQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2030
Cdd:TIGR02168 670 SSILeRRREIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2031 ERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAA 2110
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2111 QSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVE 2190
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 2191 QELTTLRLQLEETDHQKNLLDEELQRLKAEA---TEAARQRSQVEEELFSVRVQMEELSKLKARIE 2253
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIdnlQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
167-267 |
1.96e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 100.62 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 167 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 246
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 530389149 247 DVPQPDEKSIITYVSSLYDAM 267
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1716-2523 |
2.95e-24 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 112.89 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1716 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRQELEAELAKVRAEMEVLLASKARAE-EESRSTSEKSKQRL 1794
Cdd:COG1196 177 AERKLERTEENLERLEDLLEELEKQLEKLERQAEKA-ERYQELKAELRELELALLLAKLKELRKElEELEEELSRLEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1795 EAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVlaeklaaigeatrlktEAEIALKEKEAENERLRRL 1874
Cdd:COG1196 256 EELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEEL----------------EGEISLLRERLEELENELE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1875 AEDEAfqRRRLEEQAAQHKADIEERLAQLRK--ASDSELERQKGLVEDTLRQRRQ-VEEEILALKASFEKAAAGKAELEL 1951
Cdd:COG1196 320 ELEER--LEELKEKIEALKEELEERETLLEEleQLLAELEEAKEELEEKLSALLEeLEELFEALREELAELEAELAEIRN 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1952 ELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2031
Cdd:COG1196 398 ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQ 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2032 RAEQESARqlqlaQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLR--------------GEAEAARRAAEE 2097
Cdd:COG1196 478 RLEKELSS-----LEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKvkekyetaleaalgNRLQAVVVENEE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2098 AEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKeaeqEAARRAQAEQAALRQK------QAADAE 2171
Cdd:COG1196 553 VAKKAIEFLKENKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDLID----FDPKYEPAVRFVLGDTlvvddlEQARRL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2172 MEKHKKF-------------------AEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVE 2232
Cdd:COG1196 629 ARKLRIKyrivtldgdlvepsgsitgGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELR 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2233 EELFSVRVQMEELSKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2310
Cdd:COG1196 709 RQLEELERQLEELKRELAALEEELEQLQsrLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKR 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2311 ALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEetqgFQRTLEAERQRQLEMSAE 2386
Cdd:COG1196 789 QALQEELEELEEELEEAERrldaLERELESLEQRRERLEQEIEELEEEIEELEEKLDE----LEEELEELEKELEELKEE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2387 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDhdaERLREAIAELERE--- 2463
Cdd:COG1196 865 LEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLE---VELPELEEELEEEyed 941
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530389149 2464 --KEKLQQEAKLLQLKSEEMQTVQQEQllqetqalqqsfLSEKDSLLQRERFIEQEKAKLEQ 2523
Cdd:COG1196 942 tlETELEREIERLEEEIEALGPVNLRA------------IEEYEEVEERYEELKSQREDLEE 991
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
46-148 |
3.07e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 99.70 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 46 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKL 122
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKV 76
|
90 100
....*....|....*....|....*.
gi 530389149 123 VNIRNDDIADGnPKLTLGLIWTIILH 148
Cdd:smart00033 77 VLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
165-264 |
4.67e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.56 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 165 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 244
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 530389149 245 D-VDVPQPDEKSIITYVSSLY 264
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
43-151 |
1.01e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 Cd Length: 109 Bit Score: 98.51 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 43 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-V 120
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgV 78
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 121 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:pfam00307 79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1068-1941 |
1.04e-23 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 111.34 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1068 LRSELELTLGKLEQVRslsaiylEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEaq 1147
Cdd:COG1196 170 YKERKEEAERKLERTE-------ENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKE-- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1148 qptFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAW 1227
Cdd:COG1196 241 ---LEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1228 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK 1307
Cdd:COG1196 318 LEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRN 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1308 pkvqsgsesviqeyvdlrthysELTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1387
Cdd:COG1196 398 ----------------------ELEELKRE-IESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQ 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1388 KAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIqEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE 1467
Cdd:COG1196 455 LEELRDRLKELERELAELQEELQRLEKELSSLEARL-DRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKEKYET 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1468 ATERQRGGAegeLQALRARAEEA--EAQKRQAQEEAER-----LRRQVQDESQRKRQAEVELASRVKAEaEAAREKQRAL 1540
Cdd:COG1196 534 ALEAALGNR---LQAVVVENEEVakKAIEFLKENKAGRatflpLDRIKPLRSLKSDAAPGFLGLASDLI-DFDPKYEPAV 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1541 QA----------LEELRLQAEEAERRLR-----QAEVERARQVQVAleTAQRSAEAELQSKRASFAEKTAQLERSLQEEH 1605
Cdd:COG1196 610 RFvlgdtlvvddLEQARRLARKLRIKYRivtldGDLVEPSGSITGG--SRNKRSSLAQKRELKELEEELAELEAQLEKLE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1606 VAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEvaQQKSLAQAEAEKQKEEAEREARRRGKAE 1685
Cdd:COG1196 688 EELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQS--RLEELEEELEELEEELEELQERLEELEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1686 EQAVRQRELA--EQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1763
Cdd:COG1196 766 ELESLEEALAklKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLD 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1764 KVRAEMEVlLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1843
Cdd:COG1196 846 ELEEELEE-LEKELEELKEELEELEAEKEELEDELKELEEEKEE---LEEELRELESELAELKEEIEKLRERLEELEAKL 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1844 laaigeaTRLKTEAEIALKEKEAENErlrrlAEDEAFQRRRLEEqaaqhkadIEERLAQLR---KASDSELERQKGLVED 1920
Cdd:COG1196 922 -------ERLEVELPELEEELEEEYE-----DTLETELEREIER--------LEEEIEALGpvnLRAIEEYEEVEERYEE 981
|
890 900
....*....|....*....|.
gi 530389149 1921 TLRQRRQVEEEILALKASFEK 1941
Cdd:COG1196 982 LKSQREDLEEAKEKLLEVIEE 1002
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1106-1906 |
2.69e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.76 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1106 AEEVLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1185
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1186 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1265
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1266 hgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQyikfISET 1345
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1346 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-------------------EAKE--LQQRMQE 1404
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegyeAAIEaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1405 EVVRREEAAVDAQQ---QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQ 1481
Cdd:TIGR02168 550 VVVENLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKLRKALSYLLG 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1482 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevelASRVKAEAEAAREKQRalQALEELRLQAEEAERRLR--Q 1559
Cdd:TIGR02168 624 GVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSSILERR--REIEELEEKIEELEEKIAelE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1560 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEehvaVAQLREEAERRAQQQAEAERAREEAERELERW 1639
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1640 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1719
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1720 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEA 1796
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEG 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1797 EAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIGEATRLkteaeiALKEKEAENERLRRLa 1875
Cdd:TIGR02168 934 LEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL- 1005
|
810 820 830
....*....|....*....|....*....|.
gi 530389149 1876 edeafqrrrleeqaAQHKADIEERLAQLRKA 1906
Cdd:TIGR02168 1006 --------------TAQKEDLTEAKETLEEA 1022
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
164-268 |
3.47e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.17 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 530389149 244 EDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
164-264 |
3.75e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 96.73 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 530389149 244 EDVDVPQ-PDEKSIITYVSSLY 264
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1335-2066 |
6.17e-23 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 108.65 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1335 TSQYIKFISETLRRMEE-EERLAEQQraEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAA 1413
Cdd:COG1196 167 VSKYKERKEEAERKLERtEENLERLE--DLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1414 VDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1493
Cdd:COG1196 245 EEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEER 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1494 KRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVA-- 1571
Cdd:COG1196 325 LEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELkr 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1572 -----------LETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQ 1640
Cdd:COG1196 405 eiesleerlerLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELS 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1641 LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrGKAEEQ----------------AVRQRELAEQELEKQRQ 1704
Cdd:COG1196 485 SLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAEL-IKVKEKyetaleaalgnrlqavVVENEEVAKKAIEFLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1705 LAEGTA------------QQRLAAEQELIRLRAETEQGEQQ-----RQLLEEELARLQREAAAATQKRQELEAELakVRA 1767
Cdd:COG1196 564 NKAGRAtflpldrikplrSLKSDAAPGFLGLASDLIDFDPKyepavRFVLGDTLVVDDLEQARRLARKLRIKYRI--VTL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1768 EMEVLLASKaraeeeSRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRqlaeEDAARQRAEAERVLAEKLAAI 1847
Cdd:COG1196 642 DGDLVEPSG------SITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEEL----KSLKNELRSLEDLLEELRRQL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1848 GEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKgLVEDTLRQRRQ 1927
Cdd:COG1196 712 EELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKE-EIEELEEKRQA 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1928 VEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAArqrqlaaEEERRRREAEERVQKSLAAEEEAAR 2007
Cdd:COG1196 791 LQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIE-------ELEEKLDELEEELEELEKELEELKE 863
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 2008 QRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQK 2066
Cdd:COG1196 864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLE 922
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1686-2471 |
1.30e-22 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 107.49 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1686 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1765
Cdd:COG1196 270 EELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1766 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1845
Cdd:COG1196 350 EQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1846 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEE-QAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQ 1924
Cdd:COG1196 430 LEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAElQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1925 RRQVEEEILALKASFEKAaagKAELELELGRIRSNA-----EDTLRSKEQAeLEAARQRQLAAEEERRrreaeervqksL 1999
Cdd:COG1196 510 LESGLPGVYGPVAELIKV---KEKYETALEAALGNRlqavvVENEEVAKKA-IEFLKENKAGRATFLP-----------L 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2000 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAAQKRLQAE-EKAHAFAVQQK 2066
Cdd:COG1196 575 DRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRfvlgdtlvvddlEQARRLARKLRIKYRIVTLDgDLVEPSGSITG 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2067 EQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKE 2146
Cdd:COG1196 655 GSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQ 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2147 AEQEAARRAQAEQAALRQKQAADAEMEKHKkfaeqtlRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAAR 2226
Cdd:COG1196 735 LQSRLEELEEELEELEEELEELQERLEELE-------EELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAER 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2227 QRSQVEEELFSVRVQMEELSKLKARIEAENRALILRdkdntqrfLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2306
Cdd:COG1196 808 RLDALERELESLEQRRERLEQEIEELEEEIEELEEK--------LDELEEELEELEKELEELKEELEELEAEKEELEDEL 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2307 AQQRalaekmlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEmsAE 2386
Cdd:COG1196 880 KELE-------EEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELE--RE 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2387 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEigeklhrtelatqekvtlvqtLEIQRQQSDHDAERLREAIAELEREKEK 2466
Cdd:COG1196 951 IERLEEEIEALGPVNLRAIEEYEEVEERYEE---------------------LKSQREDLEEAKEKLLEVIEELDKEKRE 1009
|
....*
gi 530389149 2467 LQQEA 2471
Cdd:COG1196 1010 RFKET 1014
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
164-262 |
3.99e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 93.84 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 530389149 243 PEDVDVPQPDEKSIITYVSS 262
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
798-864 |
6.00e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.94 E-value: 6.00e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 798 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 864
Cdd:pfam17902 1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1361-1950 |
3.47e-21 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 102.53 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1361 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQA 1440
Cdd:COG0419 153 PKERKEILDELFGLEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1441 KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAegeLQALRARAEEAEAQKRQAQEEAERLRRQVQD--ESQRKRQA 1518
Cdd:COG0419 233 EIEALEERLAELEEEKERLEELKARLLEIESLELEA---LKIREEELRELERLLEELEEKIERLEELEREieELEEELEG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1519 EVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQvALETAQRSAEAELQSKRASFAEKTAQLE 1598
Cdd:COG0419 310 LRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLE-ERLKELEERLEELEKELEKALERLKQLE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1599 RSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER-------WQLKANEALRLRLQAEEVAQQKSLAQAEAEKQK 1671
Cdd:COG0419 389 EAIQELKEELAELSAALEEIQEELEELEKELEELERELEEleeeikkLEEQINQLESKELMIAELAGAGEKCPVCGQELP 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1672 EEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR-----------LRAETEQGEQQRQLLEEE 1740
Cdd:COG0419 469 EEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIElleleealkeeLEEKLEKLENLLEELEEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1741 LARLQREAAAatQKRQELEAELAKVRAEMEvllasKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEakr 1820
Cdd:COG0419 549 KEKLQLQQLK--EELRQLEDRLQELKELLE-----ELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQS--- 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1821 qrqLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERL--RRLAEDEAFQRRRLEEQAAQHKADIEE 1898
Cdd:COG0419 619 ---LELSEAENELEEAEEELESELEKLNLQAELEELLQAALEELEEKVEELeaEIRRELQRIENEEQLEEKLEELEQLEE 695
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 530389149 1899 RLAQLRkASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELE 1950
Cdd:COG0419 696 ELEQLR-EELEELLKKLGEIEQLIEELESRKAELEELKKELEKLEKALELLE 746
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1106-1906 |
2.75e-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: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1106 AEEVLRAHE--EQLKEAQAVPATLpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDveverwr 1183
Cdd:TIGR02168 209 AEKAERYKElkAELRELELALLVL-RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1184 ERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQALLEEi 1263
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE-LAELEEKLEELKEELESLEA- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1264 erhgeKVEECQrfakqyiNAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDlrthySELTTLTSQYIKFIS 1343
Cdd:TIGR02168 359 -----ELEELE-------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevVRREEAAvdAQQQKRSI 1423
Cdd:TIGR02168 422 EIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQ--LQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1424 QEELQQLRQSSEAEIQAKArqaeaaerSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALRARAEEAEAQKRQAQE 1499
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLK--------NQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1500 EAERLRR-------------QVQDESQRKRQAEVE--LASRVKAEAEAarekQRALQALEELRLQAEEAERRLRQAEVER 1564
Cdd:TIGR02168 567 QNELGRVtflpldsikgteiQGNDREILKNIEGFLgvAKDLVKFDPKL----RKALSYLLGGVLVVDDLDNALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1565 ARQVQVALET-----------AQRSAEAELQSKRASFAE---KTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERARE 1630
Cdd:TIGR02168 643 PGYRIVTLDGdlvrpggvitgGSAKTNSSILERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1631 EAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTA 1710
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1711 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKS 1790
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1791 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAE--- 1867
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidn 940
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 530389149 1868 -NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1906
Cdd:TIGR02168 941 lQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
974-1796 |
2.86e-20 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 99.79 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 974 LQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPAR---ECAQRIAEQQKAQAEVEGLGKGVARLSA 1050
Cdd:COG1196 202 LEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEELEEELSRleeELEELQEELEEAEKEIEELKSELEELRE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1051 EAEKVlalpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAH-EEQLKEAQAVPATLPE 1129
Cdd:COG1196 282 ELEEL------QEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEElEERETLLEELEQLLAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1130 LEATKASL-KKLRAQAEAQQPTFDALRDELR-------GAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTD 1201
Cdd:COG1196 356 LEEAKEELeEKLSALLEELEELFEALREELAeleaelaEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1202 VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYI 1281
Cdd:COG1196 436 ELQTELEELNEELEELEEQLEELRDRLKELERELAELQEE-LQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1282 NAIKDYELQLVTYKAQLEPVASPAKKPKVQSgseSVIQEYVDLRTHYSELTTLTSQYIKFI-SETLRRMEEEERLAEQQR 1360
Cdd:COG1196 515 PGVYGPVAELIKVKEKYETALEAALGNRLQA---VVVENEEVAKKAIEFLKENKAGRATFLpLDRIKPLRSLKSDAAPGF 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1361 AEERERLAEVEAALEKQRQLAEAH---AQAKAQAEREAKELQQRM------QEEV---------VRREEAAVDAQQQKRS 1422
Cdd:COG1196 592 LGLASDLIDFDPKYEPAVRFVLGDtlvVDDLEQARRLARKLRIKYrivtldGDLVepsgsitggSRNKRSSLAQKRELKE 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1423 IQEELQQLRQ---SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1499
Cdd:COG1196 672 LEEELAELEAqleKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEE 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1500 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSA 1579
Cdd:COG1196 752 ELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIE 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1580 EAELQSKRAsfAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAreeaerelerwqLKANEALRLRLQAEEVAQQ 1659
Cdd:COG1196 832 ELEEEIEEL--EEKLDELEEELEELEKELEELKEELEELEAEKEELEDE------------LKELEEEKEELEEELRELE 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1660 KSLAqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQGEQQRQL--L 1737
Cdd:COG1196 898 SELA-------------------ELKEEIEKLRERLEELEAKLERLEV----ELPELEEELEEEYEDTLETELEREIerL 954
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1738 EEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA 1796
Cdd:COG1196 955 EEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKE 1013
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
168-265 |
3.59e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.56 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 168 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 246
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 530389149 247 DVPQPDEKSIITYVSSLYD 265
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
42-152 |
4.10e-20 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 89.37 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRE 90
|
90 100 110
....*....|....*....|....*....|....
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21309 91 SIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
1336-2066 |
4.13e-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: 99.28 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1336 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVD 1415
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1416 AQQQKRSIQEELQQLRQSSEAEIQA-----KARQAEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAE 1488
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESskqeiEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1489 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQALEELRLQAEEAE-RRLRQAEVERA 1565
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKkKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1566 RQVQVALETAQR-SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1644
Cdd:pfam02463 391 KLKEEELELKSEeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1645 EALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELI 1721
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1722 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG-R 1800
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIlK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1801 FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAF 1880
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1881 QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA 1960
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1961 EDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2040
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740
....*....|....*....|....*....
gi 530389149 2041 LQLAQE---AAQKRLQAEEKAHAFAVQQK 2066
Cdd:pfam02463 871 ELLLKEeelEEQKLKDELESKEEKEKEEK 899
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
42-152 |
4.46e-20 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 88.99 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRE 93
|
90 100 110
....*....|....*....|....*....|....
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21308 94 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
164-264 |
4.99e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 88.17 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 530389149 244 EDVDV--PQPDEKSIITYVSSLY 264
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1404-2342 |
1.81e-19 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 97.48 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1404 EEVVRREEAAVDAQQQKRSIQEELqqlrqssEAEIQAKARQAEAAERsRLRIEEEIRVVRLQLEATERqrggaegelqal 1483
Cdd:COG1196 175 EEAERKLERTEENLERLEDLLEEL-------EKQLEKLERQAEKAER-YQELKAELRELELALLLAKL------------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1484 raraEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVE 1563
Cdd:COG1196 235 ----KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1564 RARQVQVALETAQRsaEAELQSKRASFAEKTAQLERSLQEehvavaqlreeaerraqqqaeaerareeaerelerwqlKA 1643
Cdd:COG1196 311 LEELENELEELEER--LEELKEKIEALKEELEERETLLEE--------------------------------------LE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1723
Cdd:COG1196 351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKEL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1724 RAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlaskaraeeesrstsEKSKQRLEAEAGRFRE 1803
Cdd:COG1196 431 EAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRL---------------EKELSSLEARLDRLEA 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1804 LAEEAARLRALAEEAKRQR-----QLAEEDAARQRAEA--ERVLAEKL-AAIGEATRLKTEAEIALKEKEAENERLRRL- 1874
Cdd:COG1196 496 EQRASQGVRAVLEALESGLpgvygPVAELIKVKEKYETalEAALGNRLqAVVVENEEVAKKAIEFLKENKAGRATFLPLd 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1875 -AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELeRQKGLVEDtlrqrRQVEEEILALKASFEKAAAGKAELeLEL 1953
Cdd:COG1196 576 rIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVL-GDTLVVDD-----LEQARRLARKLRIKYRIVTLDGDL-VEP 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1954 GRIRSNAEDTLRSKEQAELEAARQRQlaaeeerrrreaeeRVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE-- 2031
Cdd:COG1196 649 SGSITGGSRNKRSSLAQKRELKELEE--------------ELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEel 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2032 RAEQESARQLQLAQEAAQKRLQAEEKahafAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQ 2111
Cdd:COG1196 715 ERQLEELKRELAALEEELEQLQSRLE----ELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQA 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2112 SRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2191
Cdd:COG1196 791 LQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEA 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2192 ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELsklkariEAENRALILRDKDNTQRFL 2271
Cdd:COG1196 871 EKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERL-------EVELPELEEELEEEYEDTL 943
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530389149 2272 QEEAEKMKQVAEEaarlsvaaqEAARLRQ---LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKE 2342
Cdd:COG1196 944 ETELEREIERLEE---------EIEALGPvnlRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKR 1008
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
164-263 |
3.10e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 85.61 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 530389149 244 ED-VDVPQPDEKSIITYVSSL 263
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
160-265 |
3.28e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 85.77 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 160 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 239
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 530389149 240 LLDPEDV-DVPQPDEKSIITYVSSLYD 265
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
167-263 |
4.47e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.06 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 167 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 242
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 530389149 243 PEDVDVPQPDEKSIITYVSSL 263
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1416-2062 |
4.97e-19 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 95.60 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1416 AQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQK 1494
Cdd:COG0419 152 KPKERKEILDELFGLEKYEKLSELLKEVIKEAKAKIE-ELEGQLSELLEDIEDlLEALEEELKELKKLEEIQEEQEEEEL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1495 RQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQvaLET 1574
Cdd:COG0419 231 EQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEE--ELE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1575 AQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1654
Cdd:COG0419 309 GLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1655 EVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1734
Cdd:COG0419 389 EAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQELP 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1735 QLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL 1814
Cdd:COG0419 469 EEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1815 AEEAKRQRQLAEEDAARQRAEaervlaeklaaigeatrlkteaeiALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKA 1894
Cdd:COG0419 549 KEKLQLQQLKEELRQLEDRLQ------------------------ELKELLEELRLLRTRKEELEELRERLKE-LKKKLK 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1895 DIEERLAQLRKasdselERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdTLRSKEQAELEA 1974
Cdd:COG0419 604 ELEERLSQLEE------LLQSLELSEAENELEEAEEELESELEKLNLQAELEELLQAALEELEEKVE-ELEAEIRRELQR 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1975 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESaRQLQLAQEAAQKRLQA 2054
Cdd:COG0419 677 IENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLE-KALELLEELREKLGKA 755
|
....*...
gi 530389149 2055 EEKAHAFA 2062
Cdd:COG0419 756 GLRADILR 763
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1310-1958 |
8.01e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1310 VQSGSESVIQEYVDLRTHySELTTLTSQyIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQ 1379
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLH-ERLNGLESE-LAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1380 laeahaqAKAQAEREAKELQQRMQEEVVRREEaavdaqqqkrsIQEELQQLRQSSE---AEIQAKARQAEAAERSRLRIE 1456
Cdd:PRK02224 266 -------TIAETEREREELAEEVRDLRERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1457 EEIRVVRLQLEATERQRGGAEGELQALRARAEEaeaqkrqAQEEAERLRRQVQdesqrkrqaevelasrvkaEAEAAREK 1536
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEE-------LREEAAELESELE-------------------EAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1537 QRAlqALEELRLQAEEAERRLRQAEVERArqvqvalETAQRSaeAELQSKRASFAEKTAQLERSLQEEHVAVAQlreeae 1616
Cdd:PRK02224 382 RRE--EIEELEEEIEELRERFGDAPVDLG-------NAEDFL--EELREERDELREREAELEATLRTARERVEE------ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1617 rraqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAE 1696
Cdd:PRK02224 445 ---------------------------AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1697 qELEKQRqLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1776
Cdd:PRK02224 483 -ELEDLE-EEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1777 ARAEEEsrstSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAIGEatrLKTE 1856
Cdd:PRK02224 561 AEAEEE----AEEAREEVAELNSKLAELKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1857 AEIALKEKeaeNERLRRLAEDeaFQRRRLEE------QAAQHKADIEERLAQLRKASDsELERQKGLVE------DTLRQ 1924
Cdd:PRK02224 625 RRERLAEK---RERKRELEAE--FDEARIEEaredkeRAEEYLEQVEEKLDELREERD-DLQAEIGAVEneleelEELRE 698
|
650 660 670
....*....|....*....|....*....|....*
gi 530389149 1925 RR-QVEEEILALKASFEKAaagkAELELELGRIRS 1958
Cdd:PRK02224 699 RReALENRVEALEALYDEA----EELESMYGDLRA 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1794-2627 |
1.18e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 94.74 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1794 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLAEKLAAIGEATRlKTEAE 1858
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1859 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILAL 1935
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1936 KASFEKAAAGKAELELELgrirsnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2015
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2016 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEqelqqtlqqeqsvLDQLRGEAEAARR 2093
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-------------LKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2094 AAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQAraqaqaaaeklrkeaeqeaarraqaeqaaLRQKQAADAEME 2173
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-----------------------------LQARLDSLERLQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2174 KHKKFAEQTLRQKAQVEQELTTLR---LQLEETDHQ-----KNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL 2245
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSGLSGILgvlSELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2246 SKLKARIEAENRALILRDKDNTQRFLqeeaekmKQVAEEAARLSVAAQeaARLRQLA-EEDLAQQRALAEKMLKEKMQAV 2324
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNIEGFLGVA-------KDLVKFDPKLRKALS--YLLGGVLvVDDLDNALELAKKLRPGYRIVT 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2325 QEATRL--------------------KAEAELLQQQKELAQEQARRLQ---EDKEQMAQQLAEETQGFQRTLEAERQRQL 2381
Cdd:TIGR02168 650 LDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQIS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2382 EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELE 2461
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2462 REKEKLQQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQR 2541
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEE 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2542 QQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEqhrAALAHSEEVT 2621
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIE 964
|
....*.
gi 530389149 2622 ASQVAA 2627
Cdd:TIGR02168 965 DDEEEA 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1893-2694 |
3.40e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1893 KADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAEL 1972
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA--KKTETGKAEEARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1973 EAARQrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQEAAQKRl 2052
Cdd:PTZ00121 1137 EDARK------------------------AEEARKAEDAKRVEIAR---KAEDARKAEEARKAEDAKKAEAARKAEEVR- 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2053 QAEEKAHAFAVQQKEQELQQTLQQEqsvLDQLRgeaeaarraaEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQA 2132
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERK---AEEAR----------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2133 RAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ--KQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEETDHQKnll 2210
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKA--- 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2211 dEELQRlKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAenralilrDKDNTQRfLQEEAEKMKQVAEEAARLSV 2290
Cdd:PTZ00121 1332 -DAAKK-KAEEAKKAAEAAKAEAE-----AAADEAEAAEEKAEA--------AEKKKEE-AKKKADAAKKKAEEKKKADE 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2291 AAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAEllqqQKELAQEQARRLQEDKEqmaqqlAEETQgfQ 2370
Cdd:PTZ00121 1396 AKKKAEEDKKKADE------------LKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKK------ADEAK--K 1451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2371 RTLEAERQRQLEMSAEAERlklrVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvQTLEIQRQQSDHDA 2450
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAK----KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKA 1524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2451 ERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQALQQSFLSEKD---SLLQRERFIEQEKAKLEQLF-- 2525
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMkl 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2526 --QDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL 2603
Cdd:PTZ00121 1601 yeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2604 QLLEEQHR----AALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRlQEAGILSAEELQRLAQ 2679
Cdd:PTZ00121 1681 KKAEEDEKkaaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKI 1759
|
810
....*....|....*
gi 530389149 2680 GHTTVDELARREDVR 2694
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
44-149 |
3.71e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 82.63 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 44 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVK 121
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVD 77
|
90 100
....*....|....*....|....*...
gi 530389149 122 LVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21212 78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
45-147 |
1.35e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 Cd Length: 103 Bit Score: 80.85 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 45 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-K 121
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpE 76
|
90 100
....*....|....*....|....*..
gi 530389149 122 LVNIRNDDI-ADGNPKLTLGLIWTIIL 147
Cdd:cd00014 77 LDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
164-263 |
5.08e-17 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 79.51 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 530389149 244 ED-VDVPQPDEKSIITYVSSL 263
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
1490-2372 |
5.80e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1490 AEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQ 1569
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1570 VALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL 1649
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1650 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1729
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1730 GEQQRQLLeEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAA 1809
Cdd:pfam02463 403 EEKEAQLL-LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1810 RLRALAEEAKRQRQlaEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1889
Cdd:pfam02463 482 LQEQLELLLSRQKL--EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1890 AQHKADIEERLAQLRKASDSeLERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 1969
Cdd:pfam02463 560 VEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1970 AELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2049
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2050 KRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQ 2129
Cdd:pfam02463 719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2130 AQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNL 2209
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2210 LDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAarls 2289
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---- 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2290 vaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF 2369
Cdd:pfam02463 955 --------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
...
gi 530389149 2370 QRT 2372
Cdd:pfam02463 1027 VSI 1029
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
168-265 |
7.63e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.15 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 168 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 246
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 530389149 247 DVPQPDEKSIITYVSSLYD 265
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1418-2361 |
1.19e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.20 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1418 QQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA----- 1492
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1493 QKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAR------EKQRALQALEELRLQAEEAERrlrQAEVERAR 1566
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEL---EAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1567 QVQVALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwqlka 1643
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL--------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 nEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIR 1722
Cdd:TIGR02169 367 -EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1723 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAG 1799
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHG 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1800 RFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAigeatrlktEAEIALKEKEAENER---LRRLAE 1876
Cdd:TIGR02169 526 TVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1877 DEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELeRQKGLVEDTLRQRRQVEEEILALKAS--FEKAAAgkaeleLELG 1954
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGA------MTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1955 RIRSNAEDTLRSKEQAELEAARQRqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2034
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2035 Q-----ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAeeaeearvqAEREA 2109
Cdd:TIGR02169 716 RkigeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---------NDLEA 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2110 AQSRRQVEEAERLKQSAEeqaqaraqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQV 2189
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2190 EQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENraliLRDKDNTQR 2269
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSELKAK 925
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2270 fLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2349
Cdd:TIGR02169 926 -LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
970
....*....|..
gi 530389149 2350 RLQEDKEQMAQQ 2361
Cdd:TIGR02169 1004 AILERIEEYEKK 1015
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
166-277 |
1.94e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 78.11 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 530389149 246 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 277
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
968-1603 |
3.12e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 968 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEA-CETRTVHRLRLPLDKEPARECAQRIAEQQK-AQAEVEGLGKGV 1045
Cdd:TIGR02168 284 EELQKELYAL---ANEISRLEQQKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEeLKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1046 ARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSlSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVP 1124
Cdd:TIGR02168 361 EELEAElEELESRLEELEEQLETLRSKVAQLELQIASLNN-EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1125 ATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQ----T 1200
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1201 DVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQampLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQY 1280
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA---KKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1281 INAIKDYELQLVTYKAQLEPVASP---------------AKKPKVQSGSESVIQEYVDLRTHYS--------ELTTL-TS 1336
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1337 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAE----AHAQAKAQAEREAKElQQRMQEEVVRREEA 1412
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEelsrQISALRKDLARLEAE-VEQLEERIAQLSKE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1413 AVDAQQQKRSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1492
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEE-----------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1493 QKRQAQEEAERLRRQVQDESQRKRQAEVELASrvkaeaeaarekqrALQALEELRLQAEEAERRLRQAEVERArQVQVAL 1572
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIES--------------LAAEIEELEELIEELESELEALLNERA-SLEEAL 889
|
650 660 670
....*....|....*....|....*....|.
gi 530389149 1573 ETAqRSAEAELQSKRASFAEKTAQLERSLQE 1603
Cdd:TIGR02168 890 ALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1078-1605 |
3.98e-16 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 85.97 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1078 KLEQVRSLSAIYLEKLKTISLVIRgtqgAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDE 1157
Cdd:COG0419 186 KIEELEGQLSELLEDIEDLLEALE----EELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1158 LRGAQEVGERLQQRHGERDVEVERWRERVAQLLErwqavlaqtdvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQ 1237
Cdd:COG0419 262 ESLELEALKIREEELRELERLLEELEEKIERLEE-----------LEREIEELEEELEGLRALLEELEELLEKLKSLEER 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1238 IQAMpLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTyKAQLEPVASPAKKPKVQSGSESV 1317
Cdd:COG0419 331 LEKL-EEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLK-QLEEAIQELKEELAELSAALEEI 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1318 IQEYVDLRTHYSELTTLTSQY---IKFISETLRRMEEEERLAEQQRAE---------ERERLAEVEAALEKQRQLAE--- 1382
Cdd:COG0419 409 QEELEELEKELEELERELEELeeeIKKLEEQINQLESKELMIAELAGAgekcpvcgqELPEEHEKELLELYELELEElee 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1383 --AHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIR 1460
Cdd:COG0419 489 elSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLEDRL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1461 VVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DESQRKRQAEVELAS------RVKAEAEA 1532
Cdd:COG0419 569 QELKELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQslELSEAENELEEAEEEleseleKLNLQAEL 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1533 AREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQrsAEAELQSKRASFAEKTAQLERSLQEEH 1605
Cdd:COG0419 649 EELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQ--LEEELEQLREELEELLKKLGEIEQLIE 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
971-1880 |
4.14e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.28 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 971 QQLLQSLEQGAQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1050
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1051 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKEAQ 1121
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1122 AVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1200
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1201 dvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAmpladsqavreqlrqeqalleEIERHGEKVEECQRFAKQY 1280
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1281 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQR 1360
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1361 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKelqQRMQEEVVRREEAAVDAQQQKRS-------------IQEEL 1427
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1428 QQLRQSSEA----------EIQAKARQA-----------EAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1482
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvEFDPKYEPAfkyvfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1483 LRARAEEAEAQKRQAQEEA-ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEE----LRLQAEEAERRL 1557
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeekLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1558 RQAEVERarqvqvaletaqrsaeAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelE 1637
Cdd:TIGR02169 747 SSLEQEI----------------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------S 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1638 RWQLKANEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAE 1717
Cdd:TIGR02169 792 RIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1718 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAE 1797
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDP 939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1798 AGRFRELAEEAARLRALAEEAKR-QRQLAEEDAARQRA--EAERVLAEKLAAIGEATRLKTEAEiALKEKEAENERLRRL 1874
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKRE 1018
|
....*.
gi 530389149 1875 AEDEAF 1880
Cdd:TIGR02169 1019 VFMEAF 1024
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
169-264 |
5.99e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 76.63 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 169 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 247
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 530389149 248 VPQPDEKSIITYVSSLY 264
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1822-2524 |
6.77e-16 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 85.54 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1822 RQLAEEDAA-----RQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHKadI 1896
Cdd:COG1196 158 RKLIEEAAGvskykERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKA-ELRELELALLLAK--L 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1897 EERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAAR 1976
Cdd:COG1196 235 KELRKELEEL-EEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1977 QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQlAQEAAQKRLQAEE 2056
Cdd:COG1196 314 LENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFE-ALREELAELEAEL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2057 KAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQA 2136
Cdd:COG1196 393 AEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAEL 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2137 QAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQ--TLRQKAQVEQELTTL-------RLQ--LEETDH 2205
Cdd:COG1196 473 QEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVygPVAELIKVKEKYETAleaalgnRLQavVVENEE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2206 -QKNLLDEELQRLKAEAT--------EAARQRSQVEEELFSVRVQMEELSKLKARI---------------EAENRALIL 2261
Cdd:COG1196 553 vAKKAIEFLKENKAGRATflpldrikPLRSLKSDAAPGFLGLASDLIDFDPKYEPAvrfvlgdtlvvddleQARRLARKL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2262 RDKDNTQRFLQEEAEK-------MKQVAEEAARLSVAAQEAARLRQLAE--EDLAQQRALAEKMLKEKMQAVQEATRLKA 2332
Cdd:COG1196 633 RIKYRIVTLDGDLVEPsgsitggSRNKRSSLAQKRELKELEEELAELEAqlEKLEEELKSLKNELRSLEDLLEELRRQLE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2333 EAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFR 2412
Cdd:COG1196 713 ELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQ 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2413 KQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllQE 2492
Cdd:COG1196 793 EELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELK--------EE 864
|
730 740 750
....*....|....*....|....*....|..
gi 530389149 2493 TQALQQSFLSEKDSLLQRERFIEQEKAKLEQL 2524
Cdd:COG1196 865 LEELEAEKEELEDELKELEEEKEELEEELREL 896
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1683-2260 |
7.84e-16 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 85.20 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRQELEAE 1761
Cdd:COG0419 189 ELEGQLSELLEDIEDLLEALEeELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARL-LEIESLELE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1762 LAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARqRAEAERVLA 1841
Cdd:COG0419 268 ALKIREE-------ELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEER-LEKLEEKLE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1842 EKLAAIGEATRLKTEAEIALKEKEAEN----ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAsDSELERQKGL 1917
Cdd:COG0419 340 KLESELEELAEEKNELAKLLEERLKELeerlEELEKELEKALERLKQLEEAIQELKEELAELSAALEEI-QEELEELEKE 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1918 VEDTLRQRRQVEEEILALKASFEKAAAGKAELE-------------LELGRIRSNAEDTLRSKEQAELEAARQRQLAAEE 1984
Cdd:COG0419 419 LEELERELEELEEEIKKLEEQINQLESKELMIAelagagekcpvcgQELPEEHEKELLELYELELEELEEELSREKEEAE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1985 ERRRREAEERVQKSLAAEEEAARQRKAALEE-----VERLKAKVEEARRLRERAEQESARQL--QLAQEAAQKRLQAEEK 2057
Cdd:COG0419 499 LREEIEELEKELRELEEELIELLELEEALKEeleekLEKLENLLEELEELKEKLQLQQLKEElrQLEDRLQELKELLEEL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2058 AHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEaeearVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQ 2137
Cdd:COG0419 579 RLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQS-----LELSEAENELEEAEEELESELEKLNLQAELEELLQ 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2138 AAAEKLRKEAEQEAARRAQAEQAALRQKQAadaemekhkkfaEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRL 2217
Cdd:COG0419 654 AALEELEEKVEELEAEIRRELQRIENEEQL------------EEKLEELEQLEEELEQLREELEE-------LLKKLGEI 714
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 530389149 2218 KAEATEAARQRSQVEEelfsVRVQMEELSKLKARIEAENRALI 2260
Cdd:COG0419 715 EQLIEELESRKAELEE----LKKELEKLEKALELLEELREKLG 753
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
166-265 |
8.26e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 76.16 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 530389149 246 VDV--PQPDEKSIITYVSSLYD 265
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1861-2468 |
9.13e-16 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 84.81 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1861 LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFE 1940
Cdd:COG0419 166 LEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1941 KAAAGKAELELELGRIRSNAEDTLRSKEQAELEAAR---QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVE 2017
Cdd:COG0419 246 EEKERLEELKARLLEIESLELEALKIREEELRELERlleELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2018 RLKAKVEEARRLRE--RAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAA 2095
Cdd:COG0419 326 SLEERLEKLEEKLEklESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAAL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2096 EEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAeqaalrqKQAADAEMEKH 2175
Cdd:COG0419 406 EEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQEL-------PEEHEKELLEL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2176 KKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLkaEATEAARQRSQVEeelfsvrvQMEELSKLKARIEAE 2255
Cdd:COG0419 479 YELELEELEEELSREKEEAELREEIEELEKELRELEEELIEL--LELEEALKEELEE--------KLEKLENLLEELEEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2256 NRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQlAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE 2335
Cdd:COG0419 549 KEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELEELRE-RLKELKKKLKELEERLSQLEELLQSLELSEAENE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2336 LLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlrvaEMSRAQARAEEDAQRFRKQ 2414
Cdd:COG0419 628 LEEAEEELESELEKlNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLE----EKLEELEQLEEELEQLREE 703
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 530389149 2415 AEEIGEKLHRTElatqekvTLVQTLEIQRQQSdhdaERLREAIAELEREKEKLQ 2468
Cdd:COG0419 704 LEELLKKLGEIE-------QLIEELESRKAEL----EELKKELEKLEKALELLE 746
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
166-269 |
1.34e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 75.47 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 530389149 246 VDV--PQPDEKSIITYVSSLYDAMPR 269
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1379-1749 |
1.62e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 84.02 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1379 QLAEAHAQAKAQAEREAKELQQRMQEEVVRreeaavdaqQQKRSIQEELQQLRQSSEAEiqaKARQAEA-------AERS 1451
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1452 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEVELASRVK-AEA 1530
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1531 EAAREKQRALQALEELRLQAEEA-ERRLRQAEVERARqvqvaletaqrsaeaELQSKRASFAEKTAQLERSLQEEhvava 1609
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1610 qlreeaerraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQa 1688
Cdd:pfam17380 470 ---------------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE- 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1689 vrQRELAEQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1749
Cdd:pfam17380 534 --RRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
959-1598 |
2.22e-15 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 84.00 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 959 AEREYGSCSHHYQQLLQSLEQGAQEESRCQrciSELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEV 1038
Cdd:COG1196 244 LEEELSRLEEELEELQEELEEAEKEIEELK---SELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1039 --EGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKT-----ISLVIRGTQGAEEVLR 1111
Cdd:COG1196 321 leERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEalreeLAELEAELAEIRNELE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1112 AHEEQLKEAQAVPATLPE-LEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLL 1190
Cdd:COG1196 401 ELKREIESLEERLERLSErLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1191 ERWQAVLAQTDV--RQRELEQLGRQLRYYRESADP-----------------------LGAWLQ--------DARR---- 1233
Cdd:COG1196 481 KELSSLEARLDRleAEQRASQGVRAVLEALESGLPgvygpvaelikvkekyetaleaaLGNRLQavvveneeVAKKaief 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1234 -RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEEC-QRFAKQ------------------YINAIKDYELQLVT 1293
Cdd:COG1196 561 lKENKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDLIDFdPKYEPAvrfvlgdtlvvddleqarRLARKLRIKYRIVT 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1294 YK-AQLEPVASPAKKPKVQSGSESVIQEYVDLRthySELTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEA 1372
Cdd:COG1196 641 LDgDLVEPSGSITGGSRNKRSSLAQKRELKELE---EELAELEAQ-LEKLEEELKSLKNELRSLEDLLEELRRQLEELER 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1373 ALEKQRQLAEAHAQAKAQAEREAKELQQRM----------QEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKA 1442
Cdd:COG1196 717 QLEELKRELAALEEELEQLQSRLEELEEELeeleeeleelQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1443 RQAEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELQALRARAEEAEAQ--------------KRQAQEEAERLRRQV 1508
Cdd:COG1196 797 ELEEELEEAERRLDA----LERELESLEQRRERLEQEIEELEEEIEELEEKldeleeeleelekeLEELKEELEELEAEK 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1509 QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRA 1588
Cdd:COG1196 873 EELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIE 952
|
730
....*....|
gi 530389149 1589 SFAEKTAQLE 1598
Cdd:COG1196 953 RLEEEIEALG 962
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4047-4085 |
2.68e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 71.99 E-value: 2.68e-15
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 4047 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4085
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1204-1822 |
5.68e-15 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 82.50 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1204 QRELEQLGRQLRYYRESADplgawlQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECqrfAKQYINA 1283
Cdd:COG0419 184 KAKIEELEGQLSELLEDIE------DLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEE---KERLEEL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1284 IKDYELQLVTYKAQLEPVASPAKKpkvqsgSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEE 1363
Cdd:COG0419 255 KARLLEIESLELEALKIREEELRE------LERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1364 rERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQA--K 1441
Cdd:COG0419 329 -ERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAAleE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1442 ARQA-EAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA---QKRQAQEEAERLRRQVQDESQRKRQ 1517
Cdd:COG0419 408 IQEElEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKcpvCGQELPEEHEKELLELYELELEELE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1518 AEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQrsaEAELQSKRASFAEKTAQL 1597
Cdd:COG0419 488 EELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELE---ELKEKLQLQQLKEELRQL 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1598 ERSLQEEHVAVAQLreeaerraqqqaeaerareeaerELERWQLKANEALRLRLQAEEvAQQKSLAQAEAEKQKEEAERE 1677
Cdd:COG0419 565 EDRLQELKELLEEL-----------------------RLLRTRKEELEELRERLKELK-KKLKELEERLSQLEELLQSLE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1678 ArrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARlQREAAAATQKRQE 1757
Cdd:COG0419 621 L-------SEAENELEEAEEELESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIEN-EEQLEEKLEELEQ 692
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1758 LEAELAKVRAEMEVLLASKARAE--EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR 1822
Cdd:COG0419 693 LEEELEQLREELEELLKKLGEIEqlIEELESRKAELEELKKELEKLEKALELLEELREKLGKAGLRA 759
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3728-3766 |
8.00e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 70.83 E-value: 8.00e-15
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3728 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3766
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2810-2848 |
1.34e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 70.06 E-value: 1.34e-14
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 2810 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 2848
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
623-812 |
1.45e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.95 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 623 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 702
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 703 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 782
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 530389149 783 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 812
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1106-2054 |
1.48e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1106 AEEVLRAHEEQLKEAQAVpatLPELEATKASLKKLRAQAEaqqpTFDALRDELRGAqEVGERLQQrhgerdveverWRER 1185
Cdd:TIGR02169 175 ALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAE----RYQALLKEKREY-EGYELLKE-----------KEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1186 VAQLlerwQAVLAQTDVRQRELEQLGRQLRyyrESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1265
Cdd:TIGR02169 236 ERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1266 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTHYSELttltsqyikfiset 1345
Cdd:TIGR02169 309 ---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1346 lrrmeeeerlaeqqraeeRERLAEVEAALEKQRQlaeahaqaKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsiqE 1425
Cdd:TIGR02169 370 ------------------RAELEEVDKEFAETRD--------ELKDYREKLEKLKREINELKRELDRLQEELQRLS---E 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1426 ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqrggAEGELQALRARAEEAEAQKRQAQEEAERLR 1505
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKK------------------QEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1506 RqvqdesqRKRQAEVELAsRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQS 1585
Cdd:TIGR02169 483 K-------ELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVV 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1586 KRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQqkslaqa 1665
Cdd:TIGR02169 555 EDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE------- 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1666 eaekqkeeaereARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA------EQELIRLRAETEQGEQQRQLLEE 1739
Cdd:TIGR02169 628 ------------DIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGIlfsrsePAELQRLRERLEGLKRELSSLQS 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1740 ELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1816
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1817 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT-EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1895
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1896 IEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE--QAELE 1973
Cdd:TIGR02169 856 IENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELS 934
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1974 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2049
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
....*
gi 530389149 2050 KRLQA 2054
Cdd:TIGR02169 1015 KKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1640-2483 |
2.00e-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: 80.88 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1640 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1715
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1716 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1793
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1794 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLAEKLAaigeatrLKTEAEIALKEKEAENERLRR 1873
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINE-------LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1874 LAEDEAFQRRRLEEQAAQHkADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAELELEL 1953
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEY-DRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1954 GRIrsnaedtlRSKEQAELEAARQRQLAAEEERRRREAEERVQksLAAEEEAARqrkAALEEVERLKAKVEEARRLRERA 2033
Cdd:TIGR02169 531 GSV--------GERYATAIEVAAGNRLNNVVVEDDAVAKEAIE--LLKRRKAGR---ATFLPLNKMRDERRDLSILSEDG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2034 EQESARQLqlaqeaaqkrLQAEEK-AHAFAVQQKEQELQQTLQQEQSVLDQLR------------GEAEAARRAAEEAEE 2100
Cdd:TIGR02169 598 VIGFAVDL----------VEFDPKyEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtlegelfeksGAMTGGSRAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2101 ARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAE 2180
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2181 QTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLkaEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENRALi 2260
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKL- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2261 lrdkdNTQRFLQEEAEKMKQVAEEaARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQ 2340
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2341 KELAQEQARRLQEDKEQMAQQlaeetqgfqrtLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGE 2420
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-----EEELSLE 954
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 2421 KLHRTELATQEKvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2483
Cdd:TIGR02169 955 DVQAELQRVEEE---IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
166-267 |
2.35e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 72.04 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 530389149 246 -VDVPQPDEKSIITYVSSLYDAM 267
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
35-148 |
2.72e-14 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 71.93 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 35 DEQDERdrvqkkTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHK 104
Cdd:cd21219 2 GSREER------AFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKK 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530389149 105 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 148
Cdd:cd21219 64 VENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3469-3507 |
2.81e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 69.29 E-value: 2.81e-14
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3469 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 3507
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
164-264 |
3.29e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.03 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 243
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 530389149 244 ED-VDVPQPDEKSIITYVSSLY 264
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1106-1609 |
3.31e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1106 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRaqaeaqqptfDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1185
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1186 VAQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQA 1258
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1259 LLEEIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESVIQEYVDLRTHYSELTTLtsqy 1338
Cdd:PRK02224 385 EIEELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT---- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1339 ikfISETLRRMEEEERLAEQ-------QRAEERERLAEVEAALEKQRQLAEAHAQAKAQaereakelqqrmQEEVVRREE 1411
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------------VEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1412 AAVDAQQQKRSIqEELQQLRQSSEAEIqakARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGELQALRARAEEA 1490
Cdd:PRK02224 500 RAEDLVEAEDRI-ERLEERREDLEELI---AERRETIEEKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1491 EAQKRQAQ--EEAERLRR--QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEA--ERRLRQAEVER 1564
Cdd:PRK02224 576 ELNSKLAElkERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDK 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 530389149 1565 AR----QVQVALETAQRSAE-AELQSKRASFAEKTAQLErSLQEEHVAVA 1609
Cdd:PRK02224 656 ERaeeyLEQVEEKLDELREErDDLQAEIGAVENELEELE-ELRERREALE 704
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1830-2619 |
4.90e-14 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 79.37 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1830 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKaDIEERLAQLRKASDS 1909
Cdd:COG1196 150 INAKPEERRKLIEEAAGVSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAE-RYQELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1910 ELERQkglVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRR 1989
Cdd:COG1196 229 LLLAK---LKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1990 EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKR--LQAEEKAHAFAVQQKe 2067
Cdd:COG1196 306 LLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLsaLLEELEELFEALREE- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2068 qelqqtlqqeqsvLDQLRGEAEaarraaeeaeearvQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEA 2147
Cdd:COG1196 385 -------------LAELEAELA--------------EIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEEL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2148 EQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQ 2227
Cdd:COG1196 438 QTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGV 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2228 RSQVEEeLFSVRVQMEE-LSK-LKARIEAenralILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEED 2305
Cdd:COG1196 518 YGPVAE-LIKVKEKYETaLEAaLGNRLQA-----VVVENEEVAKKAIEFLKENKAGRATFLPLDRIKPLRSLKSDAAPGF 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2306 LAQQRAL--AEKMLKEKMQAVQEATRL-------KAEAELLQQQKELAQ---------------EQARRLQEDKEQMAQQ 2361
Cdd:COG1196 592 LGLASDLidFDPKYEPAVRFVLGDTLVvddleqaRRLARKLRIKYRIVTldgdlvepsgsitggSRNKRSSLAQKRELKE 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2362 LAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2441
Cdd:COG1196 672 LEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEE 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2442 QRQQSDHDAERLREAIAELEREKEKLQQE-AKLLQLKSEEMQTVQQEQLLQETQALQQSFLSE--KDSLLQRERFIEQEK 2518
Cdd:COG1196 752 ELEELQERLEELEEELESLEEALAKLKEEiEELEEKRQALQEELEELEEELEEAERRLDALERelESLEQRRERLEQEIE 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2519 AKLEQLfqDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR 2598
Cdd:COG1196 832 ELEEEI--EELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEK 909
|
810 820
....*....|....*....|.
gi 530389149 2599 LREQLQLLEEQHRAALAHSEE 2619
Cdd:COG1196 910 LRERLEELEAKLERLEVELPE 930
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
44-149 |
5.29e-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: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 44 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRH 117
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMAS 73
|
90 100 110
....*....|....*....|....*....|..
gi 530389149 118 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21213 74 KRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1074-1603 |
5.70e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1074 LTLGKLEQVRSLSAiylEKLKTISLVIRGTQGAEEVLRAHEEQlKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDA 1153
Cdd:PRK02224 159 LQLGKLEEYRERAS---DARLGVERVLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1154 LRDElrgAQEVGErlqqRHGERDVEVERWRERVAQLlerwQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARR 1233
Cdd:PRK02224 235 TRDE---ADEVLE----EHEERREELETLEAEIEDL----RETIAET---EREREELAEEVRDLRERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1234 RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1313
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1314 SESVIQEYVDlrthySELTTLTSQYiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAER 1393
Cdd:PRK02224 381 DRREEIEELE-----EEIEELRERF-GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE-----RVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1394 EAKELQQRMQE-EVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---------EIQAKARQAEAAERSRLRIEEEIRVVR 1463
Cdd:PRK02224 450 EAGKCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEveerleraeDLVEAEDRIERLEERREDLEELIAERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1464 LQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQ 1541
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIE 609
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 1542 ALEELR--LQAEEAERRLRQAEV-ERARQVQVALETAqrsAEAELQSKRASFAEKTAQLERSLQE 1603
Cdd:PRK02224 610 RLREKReaLAELNDERRERLAEKrERKRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1070-1935 |
5.94e-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: 79.34 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1070 SELELTLGKLEQVRslsaiylEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATK--ASLKKLRAQAEAQ 1147
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1148 QPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLaQTDVR--QRELEQLGRQLRYYRESadplg 1225
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIAEKERE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1226 awLQDARRRQEQIQAmpladsqavreqlrQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPA 1305
Cdd:TIGR02169 317 --LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1306 KKPKvqsgsesviQEYVDLRTHYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA 1385
Cdd:TIGR02169 381 AETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1386 QAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ 1465
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1466 LEATERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDESQRKRQaeVELASRVKA------EAEAAREK 1536
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEA--IELLKRRKAgratflPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1537 QRALQALEE-----LRLQAEEAERRLRQA--EVERARQVQVALETAQR--------SAEAELQSKRA-----SFAEKTAQ 1596
Cdd:TIGR02169 587 RRDLSILSEdgvigFAVDLVEFDPKYEPAfkYVFGDTLVVEDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1597 LERSLQEEHVAVAqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQaEEVAQQKSLAQAEAEKQKEEAER 1676
Cdd:TIGR02169 667 LFSRSEPAELQRL----------------------------RERLEGLKRELSSLQ-SELRRIENRLDELSQELSDASRK 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1677 EARRRGKAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQgeqqrqlLEEELARLQreAAAATQKRQ 1756
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSS-LEQEIENVKSELKELEARIEE-------LEEDLHKLE--EALNDLEAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1757 ELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1836
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1837 ERVLAEKLAAI----GEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQL--RKASDSE 1910
Cdd:TIGR02169 867 EEELEELEAALrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIedPKGEDEE 945
|
890 900
....*....|....*....|....*
gi 530389149 1911 LERQKGLVEDTLRQRRQVEEEILAL 1935
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
41-145 |
6.06e-14 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 70.64 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 41 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEE 77
|
90 100
....*....|....*....|....*....
gi 530389149 118 R-QVKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21225 78 DlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
164-261 |
7.24e-14 |
|
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: 70.49 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPgLCPDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 530389149 243 PEDVDVPQPDEKSIITYVS 261
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1064-1817 |
1.45e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.70 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1064 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTIslvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRA 1142
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSL-------HGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1143 QAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQlgRQLRYYRESAD 1222
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1223 PLGAWLQDARRRQEQI---QAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYElQLVTYKAQLE 1299
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1300 pvaspAKKPKVQSGSesviqeyvdlrthySELTTLTSQYIKFISETLRRMEEEERLAeqqRAEERERLAEVEAALekQRQ 1379
Cdd:TIGR00618 390 -----TLTQKLQSLC--------------KELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAEL--CAA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1380 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE-AAERSRLRIEEE 1458
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGP 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1459 IRVVRLQLEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQRKRQAEVELASRVKAEAE 1531
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSeedvYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1532 AAREKQRALQAlEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK--------RASFAEKTAQLERSLQE 1603
Cdd:TIGR00618 606 AEDMLACEQHA-LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehalsiRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1604 EHVAVAQLREEAER---RAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArr 1680
Cdd:TIGR00618 685 MQSEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE-- 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1681 rgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKR 1755
Cdd:TIGR00618 762 ----AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRL 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530389149 1756 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1817
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1812-2364 |
2.13e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 77.11 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1812 RALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ 1891
Cdd:COG0419 174 ELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1892 HKADIEE------RLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLR 1965
Cdd:COG0419 254 LKARLLEieslelEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1966 SKEQAELEAARQRQLAAEEERRRREAEERVQK------SLAAEEEAARQRKAALEEV-ERLKAKVEEA-RRLRERAEQES 2037
Cdd:COG0419 334 LEEKLEKLESELEELAEEKNELAKLLEERLKEleerleELEKELEKALERLKQLEEAiQELKEELAELsAALEEIQEELE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2038 ARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQ--LRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2115
Cdd:COG0419 414 ELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKcpVCGQELPEEHEKELLELYELELEELEEELSRE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2116 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTT 2195
Cdd:COG0419 494 KEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLEDRLQELKE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2196 LRLQLEETDHQKNLLDEELQRLKaeatEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFlQEEA 2275
Cdd:COG0419 574 LLEELRLLRTRKEELEELRERLK----ELKKKLKELEERLSQLEELLQSLELSEAENELEEAEEELESELEKLNL-QAEL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2276 EKMKQVAEEAARLSVAAQEAARLRqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDK 2355
Cdd:COG0419 649 EELLQAALEELEEKVEELEAEIRR---ELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRK 725
|
....*....
gi 530389149 2356 EQMAQQLAE 2364
Cdd:COG0419 726 AELEELKKE 734
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
164-264 |
2.76e-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: 68.90 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 243
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 530389149 244 ED-VDVPQPDEKSIITYVSSLY 264
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3062-3100 |
3.17e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 66.21 E-value: 3.17e-13
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3062 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 3100
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2180-2475 |
3.32e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.32 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2180 EQTLRQKAQVEQELTTLRLQLEETDHQKNLlDEELQRLKAEATEAARQRSQVEEELFSV--RVQMEELSKLK-------A 2250
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2251 RIEAENRALILRDKDNTQRFLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2330
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2331 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDaQR 2410
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-KR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 2411 FRKQAEEIGEKLHRTELAT--------QEKVTLVQTLEIQRQQSDHDAERLREaiAELEREKEKLQQEAKLLQ 2475
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEErkqamieeERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEERRRIQ 555
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1331-2225 |
4.60e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 76.35 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1331 LTTLTSQYIKFISETLRRMEEEERLaeQQRAEERERLAEVEAAlEKQRQLAEAHAQA---KAQAEREAKELQQ---RMQE 1404
Cdd:pfam01576 178 LNKLKNKHEAMISDLEDRLKKEEKG--RQELEKAKRKLEGESS-DLQEQIAELQAQIaelRAQLAKKEEELQAalaRLEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1405 EVVRREEAavdaQQQKRSIQEELQQLRQSSEAEIQAKARqaeaAERSRLRIEEEIRVVRLQLEATeRQRGGAEGELQALR 1484
Cdd:pfam01576 255 ETAQKNAA----LKKLRELEAQLSELQEDLESERAARAK----AEKQRRDLGEELEALKTELEDT-LDTTAAQQELRSKR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1485 ARaeEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsrvkaeaEAAREKQRALQALEELRlQAEEAERRLRQAEVER 1564
Cdd:pfam01576 326 EQ--EVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKASLEKAK-QALESENAELQAELRS 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1565 ARQVQVALETAQRSAEAELQSKRASFAEktAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1644
Cdd:pfam01576 396 LQQAKQDSEHKRKKLEGQLQELQSRLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1645 EalrlRLQAEEVAQQKSLAQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLR 1724
Cdd:pfam01576 474 Q----ELLQEETRQKLNLSSRLRQL---------------EDEKNSLQEQLEEEEEAKRNVE----RQLQTLQAQLSDLK 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1725 AETEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEA 1798
Cdd:pfam01576 531 KKLEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQ 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1799 GRFRELaeeaarlraLAEEAKRQRQLAEEdaaRQRAEAERVLAEKLA-----AIGEATRLKTEAEIALKEKEAENERLRR 1873
Cdd:pfam01576 604 KKFDQM---------LAEEKAISARYAEE---RDRAEAEAREKETKAlslarALEEALDAKEELERQNKQLRAEMEDLVS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1874 LAEDEAFQ-------RRRLEEQAAQHKADIEERLAQLRKASDSEL-------------------------ERQKGLVedt 1921
Cdd:pfam01576 672 SKDDVGKNvhelersKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnmqalkaqferdlqardeqgeEKRRQLV--- 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1922 lRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAA 2001
Cdd:pfam01576 749 -KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIEAANKGRDEAVKQLKKLQAQMKDLQRELDEARASRDEIFAQ 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2002 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQS 2079
Cdd:pfam01576 828 SKESEKKLKSLEAELLQLQEDLAAAERARRQAQQERDElAEEIASGNSGKSALLDEKRRLEArIAQLEEELEEEQSNTEL 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2080 VLDQLRgeaeaARRAAEEAEEARVQAEREAAQ----SRRQVEEAER--------LKQSAEEQAQARAQAQAAAEKLRKEA 2147
Cdd:pfam01576 908 LNDRLR-----KLTLQVEQLTTELAAERSTSQksesARQQLERQNKelkaklqeMEGTVKSKYKSSIAALEAKIAQLEEQ 982
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2148 EQEAARRAQAEQAALRQKQAADAE----MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQK---NLLDEELQRLKAE 2220
Cdd:pfam01576 983 LEQESRERQAANKLVRRTEKKLKEvllqVEDERRNADQYKDQAEKGNSRLKQLKRQLEEAEEEAsraNAARRKLQRELDD 1062
|
....*
gi 530389149 2221 ATEAA 2225
Cdd:pfam01576 1063 ATESA 1067
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
63-146 |
5.71e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 63 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGN 134
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGH 100
|
90
....*....|..
gi 530389149 135 PKLTLGLIWTII 146
Cdd:cd21223 101 REKTLALLWRII 112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1386-2471 |
1.52e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 74.43 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1386 QAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQqlrqsSEAEIQAKARQAEAAERSRLRIEEEIrvvrlq 1465
Cdd:pfam01576 8 QAKEEELQKVKEKQQKAESELKELEKKHQQLCEEKNILAEQLQ-----AETELFAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1466 leaterqrggaegeLQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEVELASRVKAEAEAAREKQRaLQALEE 1545
Cdd:pfam01576 77 --------------LHELEARLEEEEERSQQLQNEKKKMQQHIQDLEE---QLEEEEAARQKLQLEKVTTEAK-IKKMEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1546 LRLQAEEAERRL---RQAEVERARQVQVALETAQRSAEAeLQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQ 1622
Cdd:pfam01576 139 DILLLEDQNNKLqkeRKLLEERISEFTSNLAEEEEKSKS-LNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1623 AEAERAREEAERELE--RWQLKANE----ALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK-AEEQAVRQRELA 1695
Cdd:pfam01576 218 SDLQEQIAELQAQIAelRAQLAKKEeelqAALARLEEETAQKNAALKKLRELEAQLSELQEDLESERaARAKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1696 EQELEKQRQLAEGT-----AQQRLAA--EQELIRLR----AETEQGEQQRQ-----------LLEEELARLQREAAAATQ 1753
Cdd:pfam01576 298 GEELEALKTELEDTldttaAQQELRSkrEQEVTELKkaleEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKASLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1754 KRQELEAELAKVRAEMEVLLASKARaeeesrstSEKSKQRLEAEAGRFRELAEEAARLRALAEE--AKRQRQLAEEDAAR 1831
Cdd:pfam01576 378 AKQALESENAELQAELRSLQQAKQD--------SEHKRKKLEGQLQELQSRLSESERQRAELAEklSKLQSELESVSSLL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1832 QRAEAERV-LAEKLAAIG-----------EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdieeR 1899
Cdd:pfam01576 450 NEAEGKNIkLSKDVSSLEsqlqdtqellqEETRQKLNLSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQA----Q 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1900 LAQLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLrskeqaeLEAARQRQ 1979
Cdd:pfam01576 526 LSDLKK----KLEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQ 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1980 LAAEEERRRREAEErvqksLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekah 2059
Cdd:pfam01576 595 LVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKETKALSLARALEEALDAKEELERQNKQLRAE---- 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2060 afavqqkeqelqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqAA 2139
Cdd:pfam01576 666 ---------------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA------------TE 712
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2140 AEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKKfaeQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA 2219
Cdd:pfam01576 713 DAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEA 784
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2220 EATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMkQVAEEAARLSVAAQEAARLR 2299
Cdd:pfam01576 785 QIEAANKGRDEAVKQLKKLQAQMKDLQRELDEARASRDEIFAQSKESEKKLKSLEAELL-QLQEDLAAAERARRQAQQER 863
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2300 QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA---- 2375
Cdd:pfam01576 864 DELAEEIASGNSGKSALLDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQKSESArqql 943
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2376 ERQRQ------LEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDH 2448
Cdd:pfam01576 944 ERQNKelkaklQEMEGTVKsKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKD 1023
|
1130 1140
....*....|....*....|...
gi 530389149 2449 DAERLREAIAELEREKEKLQQEA 2471
Cdd:pfam01576 1024 QAEKGNSRLKQLKRQLEEAEEEA 1046
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4316-4354 |
2.37e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 63.90 E-value: 2.37e-12
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 4316 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4354
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1698-2479 |
2.75e-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: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1698 ELEKQRQLAEGTAQQRLAAEQELIRLRAE----TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvll 1773
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1774 askaRAEEESRSTSEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLAEKLAAIGEATRL 1853
Cdd:TIGR00618 251 ----AQEEQLKKQQLLKQLRARIE-----ELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1854 KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR-RQVEEEI 1932
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1933 LALKASFEKAAAGKAELELELGRIrsNAEDTLRSKEQAELEAAR-QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2011
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2012 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQEaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQlrgeaEAA 2091
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-----YAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2092 RRAAEEAEEARVQAEREAAQSRRqvEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEqeaarraqaeqaalRQKQAADAE 2171
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLK--EQMQEIQQSFSILTQCDNRSKEDIPNLQNITV--------------RLQDLTEKL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2172 MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQrLKAEATEAARQRsqVEEELFSVRVQMEELSKLKar 2251
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-LHALQLTLTQER--VREHALSIRVLPKELLASR-- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2252 ieaenralilrdkdntQRFLQEEAEKMKQVAEEAARLsvaAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK 2331
Cdd:TIGR00618 679 ----------------QLALQKMQSEKEQLTYWKEML---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2332 AEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRF 2411
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 2412 RKQAEEIGEKLHRTELATQEKVTLVQTLeiqRQQSDHDAERLReaiaeleREKEKLQQEAKLLQLKSE 2479
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEI---THQLLKYEECSK-------QLAQLTQEQAKIIQLSDK 877
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1995-2572 |
2.81e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 73.64 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1995 VQKSLAAEEEAARQRKAALEE-----VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAhafaVQQKEQE 2069
Cdd:COG0419 179 VIKEAKAKIEELEGQLSELLEdiedlLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEE----KERLEEL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2070 LQQTLQQEQSVLDQLRGEAEAARRAAEEAEearvQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQ 2149
Cdd:COG0419 255 KARLLEIESLELEALKIREEELRELERLLE----ELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEER 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2150 EAARRAQAEQAALRQKQAADAEMEKhKKFAEQTLRQKaqvEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRS 2229
Cdd:COG0419 331 LEKLEEKLEKLESELEELAEEKNEL-AKLLEERLKEL---EERLEELEKELEKALERLKQLEEAIQELKEELAELSAALE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2230 QVEEELFSVRVQMEELSKLKARIEAEnraliLRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarLRQLAEEDLAQQ 2309
Cdd:COG0419 407 EIQEELEELEKELEELERELEELEEE-----IKKLEEQINQLESKELMIAELAGAGEKCPVCGQE---LPEEHEKELLEL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2310 RALAEKMLKEKMQAVQEATRLKAEA-ELLQQQKELAQEQARRLQEDKEQMaQQLAEETQGFQRTLEAERQRQLEMSAEAE 2388
Cdd:COG0419 479 YELELEELEEELSREKEEAELREEIeELEKELRELEEELIELLELEEALK-EELEEKLEKLENLLEELEELKEKLQLQQL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2389 RLKLRVAEMSRAQARAEEDAQR-FRKQAEEIGEKLHRTELATQEKVTLVQTL-----EIQRQQSDHDAERLREAIAELER 2462
Cdd:COG0419 558 KEELRQLEDRLQELKELLEELRlLRTRKEELEELRERLKELKKKLKELEERLsqleeLLQSLELSEAENELEEAEEELES 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2463 EKEKLQQEAKLLQLKSEEMQTVQQEQllqetqalqQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQqlreeqqrq 2542
Cdd:COG0419 638 ELEKLNLQAELEELLQAALEELEEKV---------EELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQ--------- 699
|
570 580 590
....*....|....*....|....*....|
gi 530389149 2543 qqqmeqerqrLVASMEEARRRQHEAEEGVR 2572
Cdd:COG0419 700 ----------LREELEELLKKLGEIEQLIE 719
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
166-261 |
2.90e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.87 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 166 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 244
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPgLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 530389149 245 DVDVPQPDEKSIITYVS 261
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1722-2276 |
3.34e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1722 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1801
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1802 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE---AENERLRRLA 1875
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1876 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAEL 1949
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1950 ELELGRIRSNAEDtLRSKE---QAELEAARQR-----------------QLAAEEERRRREAEERVQKS-LAAEEEAARQ 2008
Cdd:PRK02224 411 EDFLEELREERDE-LREREaelEATLRTARERveeaealleagkcpecgQPVEGSPHVETIEEDRERVEeLEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2009 RKAALEE-VERLKAKVEEARRLRERAEQESArqlqLAQEAAQKRLQAEEKahafavQQKEQELQQTLQQEQSVLDQLRGE 2087
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEK------RERAEELRERAAELEAEAEEKREA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2088 AEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqaaaeklrkeaeQEAARRAQAEQAALRQKQA 2167
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-----------------------LAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2168 ADAEMEKHKKFAEQTLRQ-KAQVEQELTTLRlqLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELS 2246
Cdd:PRK02224 617 ALAELNDERRERLAEKRErKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
570 580 590
....*....|....*....|....*....|.
gi 530389149 2247 KLKARIEA-ENRALILRDkdntqrfLQEEAE 2276
Cdd:PRK02224 695 ELRERREAlENRVEALEA-------LYDEAE 718
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1129-1501 |
3.70e-12 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 73.21 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1129 ELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELE 1208
Cdd:COG1196 661 SSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1209 QLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYE 1288
Cdd:COG1196 741 ELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLE 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1289 LQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTHYSELTTLtsqyikfisetLRRMEEEERLAEQQRAEERERLA 1368
Cdd:COG1196 821 QRRERLEQEIE---------ELEEEIEELEEKLDELEEELEELEKE-----------LEELKEELEELEAEKEELEDELK 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1369 EVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS-EAEIQAKARQAEA 1447
Cdd:COG1196 881 ELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETElEREIERLEEEIEA 960
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1448 AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1501
Cdd:COG1196 961 LGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKET 1014
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
166-265 |
4.36e-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 Cd Length: 103 Bit Score: 65.05 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 241
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 530389149 242 DPEDVdVPQPDEKSIITYVSSLYD 265
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3138-3176 |
4.60e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 63.13 E-value: 4.60e-12
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3138 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 3176
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2734-2772 |
4.97e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 62.74 E-value: 4.97e-12
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 2734 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2772
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
166-266 |
5.78e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 65.07 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 530389149 246 VdVPQPDEKSIITYVSSLYDA 266
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3971-4009 |
6.41e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 62.74 E-value: 6.41e-12
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3971 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4009
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3804-3842 |
6.93e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 62.36 E-value: 6.93e-12
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3804 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3842
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
971-1536 |
8.94e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 71.72 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 971 QQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEveglgkgvarlsa 1050
Cdd:COG0419 221 IQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELE------------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1051 eaekvlalpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPEL 1130
Cdd:COG0419 288 ----------------EKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1131 EATKASLKKLRaqaeaqqptFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQL 1210
Cdd:COG0419 352 KNELAKLLEER---------LKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1211 GRQLRYYRESADPLGAWLQDARRRQEQIQAM---------------PLADSQAVREQLRQEQALLEEIERHGEKVEECQR 1275
Cdd:COG0419 423 ERELEELEEEIKKLEEQINQLESKELMIAELagagekcpvcgqelpEEHEKELLELYELELEELEEELSREKEEAELREE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1276 fakqyinaIKDYELQLVTYKAQLEP--VASPAKKPKVQSGSESVIQEYVDLRTHYSElttLTSQYIKFISETLRRMEEEE 1353
Cdd:COG0419 503 --------IEELEKELRELEEELIEllELEEALKEELEEKLEKLENLLEELEELKEK---LQLQQLKEELRQLEDRLQEL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1354 RLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRM---QEEVVRREEAAVDAQQQKRSIQEELQQL 1430
Cdd:COG0419 572 KELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLElseAENELEEAEEELESELEKLNLQAELEEL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1431 RQSSEAEIQAKARQAEAaersRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1510
Cdd:COG0419 652 LQAALEELEEKVEELEA----EIRRELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAE 727
|
570 580
....*....|....*....|....*.
gi 530389149 1511 esQRKRQAEVELASRVKAEAEAAREK 1536
Cdd:COG0419 728 --LEELKKELEKLEKALELLEELREK 751
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1478-2056 |
2.11e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1478 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevELASRVKAEAEAAREKQRALQALEELRLQAEEA--ER 1555
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1556 RLRQAEVERARQVQVALETA---QRSAEAELQSKRASFAEKTAQLERSLQEehvavaqlreeaerraqqqAEAERAREEA 1632
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------------------LEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1633 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE--REARRRGKAEEQAVRQRELA---EQELEKQRQLAE 1707
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAaelESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1708 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR---AEMEVLLA---------- 1774
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1775 ----SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAARQRAEAERVLAEKLAAIG 1848
Cdd:PRK02224 461 vegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1849 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---------ERLAQLRKASDSELERQKGLVE 1919
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1920 ------DTLRQRRqveEEILALKASFEKAAAGKAELElelgriRSNAEDTLR--SKEQAELEAARQRqlaaeeerrrrea 1991
Cdd:PRK02224 621 lnderrERLAEKR---ERKRELEAEFDEARIEEARED------KERAEEYLEqvEEKLDELREERDD------------- 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 1992 eerVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2056
Cdd:PRK02224 679 ---LQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
46-152 |
2.60e-11 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 63.41 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 46 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1129-1510 |
3.12e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1129 ELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWqavlAQTDVRQRELE 1208
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI----AQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1209 QLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQAlleEIERHGEKVEECQRFAKQYINAIKDYE 1288
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1289 LQLVTYKAQLEpvaspaKKPKVQSGSESVIQEYvdlrthyselttltsqyikfiSETLRRMEEEERLAEQQRAEERERLA 1368
Cdd:TIGR02168 838 RRLEDLEEQIE------ELSEDIESLAAEIEEL---------------------EELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1369 EVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAA 1448
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1449 ERSRLRIEEEI-RVVRLQLEATErqrggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1510
Cdd:TIGR02168 971 RRRLKRLENKIkELGPVNLAAIE--------EYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1431-2057 |
3.45e-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: 70.25 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1431 RQSSEAEIQAKARQAEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1504
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1505 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAeLQ 1584
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1585 SKRASFAEKTAQLERSLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1663
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1664 QAEAEKQKEEAEREARRRGKAEEQAV-RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelA 1742
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE--L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1743 RLQREAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1816
Cdd:pfam12128 526 ELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1817 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1896
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1897 EERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEkaaagkAELELELGRIRSN--AEDTLRSKEQAELEA 1974
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSGAKAELKALET 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1975 ARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAA------------LEEVERLKAKVEEARRLRERAEQESARQl 2041
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREiRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAISELQQQLARL- 833
|
650
....*....|....*.
gi 530389149 2042 qlaQEAAQKRLQAEEK 2057
Cdd:pfam12128 834 ---IADTKLRRAKLEM 846
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1787-2524 |
8.34e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1787 SEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIgEATRLKTEAEIALKEK-- 1864
Cdd:TIGR02169 170 RKKEKALEELE-----EVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKea 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1865 -EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAA 1943
Cdd:TIGR02169 242 iERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1944 AGKAELELELGRIRSNAEDtlrSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR---KAALEEVERLK 2020
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2021 AKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAA 2091
Cdd:TIGR02169 399 REINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2092 RraaeeaeearvQAEREAAQSRRQVEEAE-RLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA 2170
Cdd:TIGR02169 479 D-----------RVEKELSKLQRELAEAEaQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2171 EME-----------------KHKKFAEQTLRQKAQVEQELTTLRLQLEE--TDHQKNLLDEELQRlkAEATEAARQRSQV 2231
Cdd:TIGR02169 548 RLNnvvveddavakeaiellKRRKAGRATFLPLNKMRDERRDLSILSEDgvIGFAVDLVEFDPKY--EPAFKYVFGDTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2232 EEELFSVRVQMeelskLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRA 2311
Cdd:TIGR02169 626 VEDIEAARRLM-----GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL--SSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2312 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLK 2391
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2392 LRVAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEA 2471
Cdd:TIGR02169 779 EALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 530389149 2472 KLLQLKSEEMQTVQQEQLLQETQalqqsfLSEKDSLLQRERfiEQEKAKLEQL 2524
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRD------LESRLGDLKKER--DELEAQLREL 901
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4392-4430 |
8.96e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 59.27 E-value: 8.96e-11
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 4392 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 4430
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1318-1816 |
1.10e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1318 IQEYVDLRTHYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKE 1397
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1398 LQQRMQeevvrreeAAVDAQQqkrSIQEELQQlrqsSEAEIQAKARQAEAAErsrlRIEEEIRVVRlqlEATERQrggae 1477
Cdd:PRK04863 326 LEQDYQ--------AASDHLN---LVQTALRQ----QEKIERYQADLEELEE----RLEEQNEVVE---EADEQQ----- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1478 gelqalraraEEAEAQKRQAQEEAERLRRQVQD-----ESQRKR----QAEVELASRVKA-------EAEAAREKQRALQ 1541
Cdd:PRK04863 379 ----------EENEARAEAAEEEVDELKSQLADyqqalDVQQTRaiqyQQAVQALERAKQlcglpdlTADNAEDWLEEFQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1542 A-LEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAeAELQSKRASfaEKTAQLERSLQEEHVAVAQLreeaerraq 1620
Cdd:PRK04863 449 AkEQEATEELLSLEQKLSVAQ-AAHSQFEQAYQLVRKIA-GEVSRSEAW--DVARELLRRLREQRHLAEQL--------- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1621 qqaeaeRAREEAERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELE 1700
Cdd:PRK04863 516 ------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---------------------DEDELEQLQEELEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1701 KQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQREAAAATQKRQELEAELAKvraemevlLASKA 1777
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------LLERE 640
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 530389149 1778 RAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1816
Cdd:PRK04863 641 RELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1534-1886 |
1.20e-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: 67.84 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1534 REKQRALQALEELRLQaEEAERRLRqaEVERARQvqvaLETAQRSAEAELQSKRASFAEKtaqlERSLQEEHvavaqlre 1613
Cdd:pfam17380 287 RQQQEKFEKMEQERLR-QEKEEKAR--EVERRRK----LEEAEKARQAEMDRQAAIYAEQ----ERMAMERE-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1614 eaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEQAVRQRE 1693
Cdd:pfam17380 348 --------------------RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1694 LaeQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQ-QRQLLEEELARLQREAAAATQKRQ-------ELEAELAKV 1765
Cdd:pfam17380 406 I--LEEERQRKIQQ--------QKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1766 RAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLAE 1842
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530389149 1843 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1886
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
1882-2619 |
1.71e-10 |
|
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: 67.69 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1882 RRRLEEQAA--QHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 1959
Cdd:pfam02463 155 RLEIEEEAAgsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1960 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2039
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2040 QLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRgeaeaarraaeeaeearvQAEREAAQSRRQV 2116
Cdd:pfam02463 315 KLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK------------------LQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2117 EEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2196
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2197 RLQLEEtdhqKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAE 2276
Cdd:pfam02463 457 ELKLLK----DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2277 KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAvqeaTRLKAEAELLQQQKELAQEQARRLQEDKE 2356
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK----LRLLIPKLKLPLKSIAVLEIDPILNLAQL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2357 QMAQQLAEETQGFQRTLEAERQRQLEMSaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLV 2436
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2437 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQalQQSFLSEKDSLLQRERFIEQ 2516
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ--KIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2517 EKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGvrrkqEELQQLEQQRRQQEELLAEEN 2596
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL-----EEEQLLIEQEEKIKEEELEEL 838
|
730 740
....*....|....*....|...
gi 530389149 2597 qRLREQLQLLEEQHRAALAHSEE 2619
Cdd:pfam02463 839 -ALELKEEQKLEKLAEEELERLE 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2184-2417 |
2.55e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 65.90 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2184 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEA---ENRALI 2260
Cdd:COG4942 38 KQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVqerEQRRRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2261 LRDKDNTQRFLQEEAEKMKQVAEEAARlsvAAQEAARLRQLAEEDLAQQRALAEKMlkeKMQAVQEATRLKAEAELLQQQ 2340
Cdd:COG4942 118 AEQLAALQRSGRNPPPALLVSPEDAQR---SVRLAIYYGALNPARAERIDALKATL---KQLAAVRAEIAAEQAELTTLL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 2341 KELAQEQAR--RLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2417
Cdd:COG4942 192 SEQRAQQAKlaQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAK 270
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1743-2480 |
3.18e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.92 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1743 RLQREAAAATQKRQELEAELAKVRAEMEVLLASKA-------RAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL- 1814
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIyrvhrtlRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1815 -------AEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR 1884
Cdd:TIGR00618 133 hdllkldYKTFTRVVLLPQGEFAQflkAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1885 LEEQAAQHKADIEERLAQLRKASDSELERQKGLVE--DTLRQRRQVEEEILALKASFEKAAAGKAELEL---ELGRIRSN 1959
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqeRINRARKA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1960 AEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2039
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRA-----KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2040 QLQLAQeaaqkrlQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEA 2119
Cdd:TIGR00618 368 REISCQ-------QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2120 ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQ------------------ 2181
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscihpnparqdi 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2182 -----TLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEA-------ARQRSQVEEELFSVRVQMEEL---- 2245
Cdd:TIGR00618 521 dnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsfsilTQCDNRSKEDIPNLQNITVRLqdlt 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2246 ---SKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQE---------AARLRQLAEEDLAQQRA 2311
Cdd:TIGR00618 601 eklSEAEDMLACEQHALLrkLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqervrehALSIRVLPKELLASRQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2312 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEdkeqmaQQLAEETQGFQRTLEAERQRQLEMSAEAER-- 2389
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE------IENASSSLGSDLAAREDALNQSLKELMHQArt 754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2390 -LKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAtQEKVTLVQTLEIQRQQ-----------SDHDAERLREAI 2457
Cdd:TIGR00618 755 vLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEIGQeipsdedilnlQCETLVQEEEQF 833
|
810 820
....*....|....*....|...
gi 530389149 2458 AELEREKEKLQQEAKLLQLKSEE 2480
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEE 856
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
36-143 |
3.34e-10 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 60.52 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 36 EQDERDRVqkktFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQN 107
Cdd:cd21300 4 EGEREARV----FTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVEN 72
|
90 100 110
....*....|....*....|....*....|....*.
gi 530389149 108 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 143
Cdd:cd21300 73 TNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
45-146 |
3.41e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 Cd Length: 114 Bit Score: 60.28 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 45 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 114
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 530389149 115 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 146
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
527-716 |
4.81e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.46 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 527 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 603
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 604 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 680
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 530389149 681 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 716
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1683-1897 |
5.89e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 65.24 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEEQAVRQRELAEQELEKQRQLAEGTAQ-----QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA-AATQKRQ 1756
Cdd:COG2268 236 IAIAEANRDAKLVELEVEQQPAGKTAEQTrevkiILAETEAEVAAWKAETRREAEQAEILAEQAIQEEKAQAeQEVQHAK 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1757 ELEAElakvraEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL-----AEEAKRQR--------- 1822
Cdd:COG2268 316 ALEAR------EMRVGLIERQKETELEPQERSYFINAAQRQAQEEAKAAANIAEAIGAqaeaaVETARETEeaeraeqaa 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1823 --QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAedEAFQRRRLEEQAAQHKADIE 1897
Cdd:COG2268 390 lvAAAEAAEQEQVEIAVRAEAAKAEAEAQAAEIKAEAEAIREKGKAEAEAKRALA--EAIQVLGDAAAAELFKALVQ 464
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1359-1911 |
6.37e-10 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 65.82 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1359 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAE 1437
Cdd:COG5281 35 QASRFLAQGVRRGEEFNSVNESGDRAVRALAAGVGKaAADLRQMADAQALAADKAVPSLISLKEQLRDEYPEPVQFTDIA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1438 IQ-AKA-----RQAEAAERSRLRIEEEIRVVRLQLEATERQ---RGGAEGELQALRARAEEAEAQkrqAQEEAERLRRQV 1508
Cdd:COG5281 115 TQlAGGqwpwlINLQQGGQATLSFGLIGPAARIANVLTAAGalvAVGAAGYAAALGAGAMAWYAG---AQETEAFNKVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1509 QDESQRKRQAEvelasRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA--ELQSK 1586
Cdd:COG5281 192 LTGEYAGTTAA-----QLRAGAAAGITQHQAAEVLAQLVAAGVATAEQLGDVAQAAARFASASGESIDKTIKAfsKLTDD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1587 RASFAEK-TAQLER--SLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERwqlkANEALRLRLQAEEVAQQKSLA 1663
Cdd:COG5281 267 PVNGAKAlNRQFHYltAAQLEQIAALQRAGDTAAAAAAAAEAAAAMDDRTARVKE----NMGTLETAWDALADAAKKMWD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1664 QAEAEKQKEEAEREARRRGKAEEQA--VRQRELAEQELEKQRQLAE---GTAQQRLAAEQELIRLRAETEQGEQQRQLLE 1738
Cdd:COG5281 343 AVLGIGREDKQAALLAAKLAAEKLArvTAQGALNARLKLAQDDLTQaelNYAAADQAANQEGALNAREDEAEVLSTQEER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1739 EELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESrsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1818
Cdd:COG5281 423 RDILKNLLADAEKRTARQEELNKALAKAKILQADKAAKAYQEDIL--QREAQSRGKTAAAERSQEQMTAALKALLAFQQQ 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1819 KRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1898
Cdd:COG5281 501 IADLSGAKEKASDQKSLLWKAEEQYALLKEEAKQRQLQEQKALLEHKKETLEYTSQLAELLDQQADRFELSAQAAGSQKE 580
|
570
....*....|...
gi 530389149 1899 RLAQLRKASDSEL 1911
Cdd:COG5281 581 RGSDLYREALAQN 593
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1337-1976 |
6.39e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 65.89 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1337 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDA 1416
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1417 QQQKRSIQEELQQLRQ---SSEAEIQA-KARQAEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1486
Cdd:pfam15921 162 EDMLNDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTIHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1487 --AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEVELASrVKAEAEAAREKQRALQAleelrlQAEEAERRLRQAEVE 1563
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITG-LTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1564 RARQVQvALETAQRSAEAELQSKRASFAEKTAQLERSLQeehVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1643
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 NEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1714
Cdd:pfam15921 391 KE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1715 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1790
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1791 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAIGEATRL-KTEAEIALKEK 1864
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1865 EAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASDSELERQKGL--VEDTLRQRRQVEEEILALKAS 1938
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDYEVLKRN 682
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 530389149 1939 F----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAAR 1976
Cdd:pfam15921 683 FrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMK 727
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1356-1554 |
6.49e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1356 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREeaavdAQQQKrsiQEELQQLRQSS 1434
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1435 EAEIQAKARQAEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDESQR 1514
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 530389149 1515 KRQAEV-ELASRVKAEAEAAREKQRALQALEELRLQAEEAE 1554
Cdd:PRK09510 218 KAAAEAkAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1107-1297 |
6.56e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.08 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1107 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1186
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1187 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1265
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|..
gi 530389149 1266 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1297
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1417-1595 |
7.26e-10 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 64.58 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1417 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqLEATERQRGGAEGELQALRARAEEAEAQKRQ 1496
Cdd:COG3064 67 IQSQQSSAKKGEQQRKKKEEQVAEELKPKQAAEQERLKQLEKER-----LKAQEQQKQAEEAEKQAQLEQKQQEEQARKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1497 AQEEAERlrrqvQDESQRKRQAEvelASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQ-----AEVERARQVQVA 1571
Cdd:COG3064 142 AAEQKKK-----AEAAKAKAAAE---AAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAeaeakAAAEKAKAEAEA 213
|
170 180
....*....|....*....|....
gi 530389149 1572 LETAQRSAEAELQSKRASFAEKTA 1595
Cdd:COG3064 214 KAKAEKKAEAAAEEKAAAEKKKAA 237
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1342-1598 |
1.12e-09 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 64.28 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1342 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQrmqeEVVRREEAAVDAQQQKR 1421
Cdd:COG4372 79 IRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQ----ELARLTKQAQDLQTRLK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1422 SIQEELQQLrqsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATErqrggAEGELQALRARAEEAEAQKRQAQEEA 1501
Cdd:COG4372 155 TLAEQRRQL------EAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQ-----IEQEAQNLATRANAAQARTEELARRA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1502 ERLRRQVQDESQRKRQAEvELASRVKAEAEAAREKQRALQALE--ELRLQAEEAE--------RRLRQAEVERAR-QVQV 1570
Cdd:COG4372 224 AAAQQTAQAIQQRDAQIS-QKAQQIAARAEQIRERERQLQRLEtaQARLEQEVAQleayyqayVRLRQQAAATQRgQVLA 302
|
250 260 270
....*....|....*....|....*....|
gi 530389149 1571 --ALETAQRSAEAELQSKRASFAEKTAQLE 1598
Cdd:COG4372 303 gaAQRVAQAQAQAQAQAQLLSSANRPAALR 332
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1108-1885 |
1.25e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1108 EVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERva 1187
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1188 qlLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLRQEQALLE----EI 1263
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1264 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKK-------PKVQSGSESVIQEYVDLRTHYSELTT 1333
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1334 LTSQYikfisETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQA-------EREAKELQ 1399
Cdd:PRK04863 518 LRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1400 QRMQEEVVRREE--AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATErQRGGAE 1477
Cdd:PRK04863 593 ARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSE 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1478 GE-LQALRARA--------------EEA-------------------EAQKRQAQE-----------------------E 1500
Cdd:PRK04863 672 DPrLNALAERFggvllseiyddvslEDApyfsalygparhaivvpdlSDAAEQLAGledcpedlyliegdpdsfddsvfS 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1501 AERLRRQV-QDESQRK----RQAEVELASRvkaeaeAAREKQralqaLEELRLQAEEAERRLRQAEVERaRQVQVALETA 1575
Cdd:PRK04863 752 VEELEKAVvVKIADRQwrysRFPEVPLFGR------AAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAF 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1576 QR------------SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlKA 1643
Cdd:PRK04863 820 SRfigshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA----DR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 NEALRLRLQAEEVAQQkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQ--------------LAEG 1708
Cdd:PRK04863 896 VEEIREQLDEAEEAKR-FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDyQQAQQTQRDAKQqafaltevvqrrahFSYE 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1709 TAQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRQELEAELAK--VRAEMEV 1771
Cdd:PRK04863 975 DAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGA 1054
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1772 LLASKARAEE---------ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAARQRAEAER 1838
Cdd:PRK04863 1055 EERARARRDElharlsanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERR 1133
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1839 VLAEKLAAiGEATRLKTEAEI---ALKEKEAENERLR---RLAEDEAFQRRRL 1885
Cdd:PRK04863 1134 LHRRELAY-LSADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRPERKV 1185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2273-2714 |
1.28e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2273 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2349
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2350 RLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlRVAEMSRAQ--ARAEE--DAQRFRKQAEEIGEKLHRT 2425
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdaKKAEAvkKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2426 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQalQQSFLSEKD 2505
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKADEAKKKAEEA--KKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2506 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvaSMEEARRRQHEAEEGVRRKQEELQQLEQqr 2585
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK--KKEEAKKKADAAKKKAEEKKKADEAKKK-- 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2586 rqqeellAEENQRLREQLQLLEEQHRAA---LAHSEEVTASQVAATKtlpngrdaldgpaaeAEPEHSFDGLRRKVSAQR 2662
Cdd:PTZ00121 1400 -------AEEDKKKADELKKAAAAKKKAdeaKKKAEEKKKADEAKKK---------------AEEAKKADEAKKKAEEAK 1457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 530389149 2663 LQEAGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLLLKATNEK 2714
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
2305-2497 |
1.49e-09 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 63.89 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2305 DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRT------------ 2372
Cdd:COG4372 82 QLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLqtrlktlaeqrr 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2373 -LEAERQ----RQLEMSAEAERLKLRVAEMSRAQARAEE---DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQ 2444
Cdd:COG4372 162 qLEAQAQslqaSQKQLQASATQLKSQVLDLKLRSAQIEQeaqNLATRANAAQARTEELARRAAAAQQTAQAIQQRDAQIS 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530389149 2445 QSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQ 2497
Cdd:COG4372 242 QKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQAAA 294
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1372-1596 |
1.54e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.29 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1372 AALEKQRQLAEAHAQAKAQAEREAKELQQrmQEEVvrREEAAVDAQQQKRSIQEELQ---QLRQSSEAEIQAKARQAEAA 1448
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1449 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEVELASRVK 1527
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1528 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1596
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1365-1838 |
1.57e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 64.52 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1365 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAkelqqRMQEEVVRREEAAVDAQQQKRSIQEELQqLRQSSEAEIQAKARQ 1444
Cdd:COG3096 280 ERRVHLDQALEFRRELYTSRQQLAAEQYRHV-----DMSRELAELNGAEGDLEADYQAASDHLN-LVQTALRQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1445 AEAAERSRLRIEEEIRVVRlqlEATERQrggaegelqalraraEEAEAQKRQAQEEAERLRRQVQDESQRkrqaevelas 1524
Cdd:COG3096 354 QADLEELTIRLEEQNEVVE---EANERQ---------------EENEARAEAAELEVDELKSQLADYQQA---------- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1525 rVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEverarqvqvaletaqrSAEAELQSKRASFAEKTAQLERSLQEE 1604
Cdd:COG3096 406 -LDVQQTRAIQYQQAIAALERAKELCHLPDLTADSAE----------------EWLETFQAKEEEATEKLLSLEQKMSMA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1605 HVAVAQLREEAERRAQQQAEAERAreeaerelERWQlKANEALRLRLQAEEVAQQKSlaqaeaekqkeeaerearrrgka 1684
Cdd:COG3096 469 QAAHSQFEQAYQLVVAIAGELARS--------EAWD-VARELLREGPDQRHLAEQVQ----------------------- 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1685 eEQAVRQRELaEQELEKQRQ----LAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEA 1760
Cdd:COG3096 517 -PLRMRLSEL-EQRLRQQQSaerlLADFCKRQGKNLDAE--ELEALHQELEALIESLSDSVSNAREQRMALRQEQEQLQS 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1761 ELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAA 1830
Cdd:COG3096 593 RIQSLMQRAPVWLAAQNALEqlseqsgeefTDSQDVTEYMQQLLEREREATVERDELGARKNALDEEIERLSQPGGSEDQ 672
|
....*...
gi 530389149 1831 RQRAEAER 1838
Cdd:COG3096 673 RLNALAER 680
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1697-2543 |
2.46e-09 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 64.03 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1697 QELEKQRQLAEGtAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA----------KVR 1766
Cdd:pfam01576 106 QDLEEQLEEEEA-ARQKLQLEK--VTTEAKIKKMEEDILLLEDQNNKLQKERKLLEERISEFTSNLAeeeekskslnKLK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1767 AEMEVLLAS---KARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervLAEK 1843
Cdd:pfam01576 183 NKHEAMISDledRLKKEEKGRQELEKAKRKLEGESS---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1844 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRrrleEQAAQHKADIEErlaqlrkasdsELERQKGLVEDTLR 1923
Cdd:pfam01576 249 LARLEEETAQKNAALKKLRELEAQLSELQEDLESERAAR----AKAEKQRRDLGE-----------ELEALKTELEDTLD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1924 Q-------RRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSK-EQAELEAARQRQLAAEEERRRREAEERV 1995
Cdd:pfam01576 314 TtaaqqelRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQlEQAKRNKASLEKAKQALESENAELQAEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1996 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAeQESARQLQLAQEAAQKRL-QAEEKAHAFAvqqkeqelqQTL 2074
Cdd:pfam01576 394 RSLQQAKQDSEHKRKKLEGQLQELQSRLSESERQRAEL-AEKLSKLQSELESVSSLLnEAEGKNIKLS---------KDV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2075 QQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARR 2154
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEAL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2155 AQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLeetDHQKNLL----------DEELQRLKAEATEA 2224
Cdd:pfam01576 544 EEGRKRLQRELEALTQRLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVsnlekkqkkfDQMLAEEKAISARY 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2225 ARQRSQVEEE-------LFSVRVQMEELSKLKARIEAENRAL------ILRDKDNTQRFLQEeAEKMKQVAEeaarlsva 2291
Cdd:pfam01576 621 AEERDRAEAEareketkALSLARALEEALDAKEELERQNKQLraemedLVSSKDDVGKNVHE-LERSKRALE-------- 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2292 aQEAARLR-QLAE-EDLAQQRALAEKMLKEKMQAvqeatrLKAEAEL-LQQQKELAQEQARRLQEDKEQMAQQLAEETQg 2368
Cdd:pfam01576 692 -QQVEEMKtQLEElEDELQATEDAKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLVKQVRELEAELEDERK- 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2369 fQRTLEAERQRQLEMsaEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDH 2448
Cdd:pfam01576 764 -QRAQAVAAKKKLEL--DLKELEAQIEAANKGRDEAVKQLKKLQAQMKDLQRELDEARASRDEIFAQSKESEKKLKSLEA 840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2449 DAERLREAIAELEREKEKLQQEAKLLQlksEEMQtvqqeqllqetqalqqSFLSEKDSLLQRERFIEQEKAKLEQLFQDE 2528
Cdd:pfam01576 841 ELLQLQEDLAAAERARRQAQQERDELA---EEIA----------------SGNSGKSALLDEKRRLEARIAQLEEELEEE 901
|
890
....*....|....*
gi 530389149 2529 VAKAQQLREEQQRQQ 2543
Cdd:pfam01576 902 QSNTELLNDRLRKLT 916
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1738-2055 |
2.49e-09 |
|
Caldesmon;
Pssm-ID: 426572 [Multi-domain] Cd Length: 490 Bit Score: 63.35 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1738 EEELARLQREAAAATQKRQ-ELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALA 1815
Cdd:pfam02029 3 EEEAARERRRRAREERRRQkESEEPSSQEDSQPEV--NAQEEAEEEDSELKPSGQGGLDEEEAFLDRTAKrEERRQKRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1816 EEAKRQRQL----AEEDAARQR-----AEAERVLAEKLAAIGEATRLKTEAEIAL---KEKEAENERLRRLAEDEAFQRR 1883
Cdd:pfam02029 81 EALERQKELdptiTDEQASKPRstentPEEKNNTEEEEKSSTRKERYEIEEREVSeksYEKDDKKAVPKEEEEEEDAKTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1884 RLEEQAAQHKADIEERLAQLRKASDSE--LERQKG------------LVEDTLRQRRQVEEEILALKASFEKAAAGKAEL 1949
Cdd:pfam02029 161 EEEEEEEEEKKVSKKKKEKLKDEYTSKvfLDQKKGhpeqksqngaleEVTSMTVKLKRTERTFSQKSLVAEDEEEGAAFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1950 ELE--LGRIRSNAEDtlrsKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEaaRQRKAalEEVERLKAKVEEAR 2027
Cdd:pfam02029 241 EAEqkLEELRRRRQE----KESQEFEKLRQKQQEAELELEELKKKREERRKILEEEE--QRRKQ--EEAERKAREEEEKR 312
|
330 340
....*....|....*....|....*...
gi 530389149 2028 RLRERAEQESArqlqlaqEAAQKRLQAE 2055
Cdd:pfam02029 313 RMKEEIERRRA-------EAAEKRQKME 333
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1497-2032 |
2.90e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1497 AQEEAERLRRQVQDESQRKR---QAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRqAEVERARQVQVALE 1573
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1574 TAQRSAEAELQSKRAsFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQA 1653
Cdd:PRK03918 242 ELEKELESLEGSKRK-LEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1654 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRA 1725
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1726 ETEQGEQQRQLLEEELAR--LQREAAAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR-----------S 1785
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytaelK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1786 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLAEKLAAIGEAT 1851
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1852 RLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SDSELERQKGLVE 1919
Cdd:PRK03918 543 SLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1920 DTLRQRRQVEEEILALKASFEKAaagKAELElELGRIRSnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSL 1999
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590
....*....|....*....|....*....|...
gi 530389149 2000 AAEEEAARQRKAALEEVERLKAKVEEARRLRER 2032
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
164-266 |
3.02e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.77 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 164 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPgLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 530389149 243 PEDVDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1694-1925 |
3.26e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.17 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1694 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1773
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1774 AsKARAEEESRSTSEKSKQRLEAEAGRFRelAEEAARLRAlAEEAKRQRQLAE---EDAARQRAEAER-VLAEKLAAIGE 1849
Cdd:TIGR02794 124 A-KAKQAAEAKAKAEAEAERKAKEEAAKQ--AEEEAKAKA-AAEAKKKAEEAKkkaEAEAKAKAEAEAkAKAEEAKAKAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1850 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 1925
Cdd:TIGR02794 200 AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1352-1603 |
3.53e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.04 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1352 EERLAEQQRaEERERLAEVEAALEKQR---QLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQ 1428
Cdd:PRK05035 456 EARQARLER-EKAAREARHKKAAEARAakdKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1429 QLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1508
Cdd:PRK05035 535 AEKQAAAAADPKKAAVAAAIARAKAKKAA-------QQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQV 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1509 QDESQRKrqaevelasrVKAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEVERARQVQVALETAQRSAEAELQSKR 1587
Cdd:PRK05035 608 AEVDPKK----------AAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAEDPKK 677
|
250
....*....|....*.
gi 530389149 1588 ASFAEKTAQLERSLQE 1603
Cdd:PRK05035 678 AAVAAAIARAKAKKAA 693
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1686-1903 |
3.58e-09 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 62.73 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1686 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1765
Cdd:COG4372 91 GTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1766 RAEMEVLLASKARAEEEsrstseksKQRLEAEAGRFRELAEEAARLRALAEEakRQRQLAEEDAARQRAEAErvlAEKLA 1845
Cdd:COG4372 171 QASQKQLQASATQLKSQ--------VLDLKLRSAQIEQEAQNLATRANAAQA--RTEELARRAAAAQQTAQA---IQQRD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1846 AIgeATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 1903
Cdd:COG4372 238 AQ--ISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQAA 293
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1022-1607 |
3.68e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1022 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKLEQVRSlsaiyleklktiSLVI 1100
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLSESVS------------EARE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1101 RGTQgaeevLRAHEEQLK-EAQAVPATLPELEATKASLKKLRAQAEAQQPTFDAL-----------------RDELRGAQ 1162
Cdd:PRK04863 580 RRMA-----LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVteymqqllerereltveRDELAARK 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1163 EV----GERLQQRHGERDveverwrERVAQLLERWQAVLAQTDVRQRELEQLGrqlrYYResadplgAWLQDARrrqeqi 1238
Cdd:PRK04863 655 QAldeeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YFS-------ALYGPAR------ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1239 QAMPLADSQAVREQLRQEQALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK-- 1309
Cdd:PRK04863 711 HAIVVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKri 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1310 --VQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRAEERERLAEVEAALEKQRQLAE 1382
Cdd:PRK04863 789 eqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLE 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1383 AHAQAKAQAEREAKE--------LQQRM---QEEVVRREEAAVDAQQQKRSI-------------QEELQQLRQSSEaei 1438
Cdd:PRK04863 869 QAKEGLSALNRLLPRlnlladetLADRVeeiREQLDEAEEAKRFVQQHGNALaqlepivsvlqsdPEQFEQLKQDYQ--- 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1439 QAKARQAEAaeRSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKR 1516
Cdd:PRK04863 946 QAQQTQRDA--KQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYN 1019
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1517 QAEVELASRVKAEAEAAREkqrALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--KR 1587
Cdd:PRK04863 1020 QVLASLKSSYDAKRQMLQE---LKQELQDLGVPAdSGAEERARarrdelHARLSANRSRRNQLEKQLTFCEAEMDNltKK 1096
|
650 660
....*....|....*....|
gi 530389149 1588 ASFAEKTAQLERSLQEEHVA 1607
Cdd:PRK04863 1097 LRKLERDYHEMREQVVNAKA 1116
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1340-1588 |
4.37e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 433539 [Multi-domain] Cd Length: 341 Bit Score: 61.47 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1340 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQ 1419
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEDLRILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1420 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQlEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1499
Cdd:pfam13868 168 EEEREAERREIKEEKEREIARLRAQQEKAQDEK-AERDELRAKLYQ-EEQERKWRQKEREEAEKKARQRQELQQAREEQI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1500 EAERLRRQVQ---DESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRlRQAEVERARQVQVALETAQ 1576
Cdd:pfam13868 246 ELKERRLAEEaerEEEEFERMLRKQAEDEEIEQEEAEKRREKRLEHRRELEKQIEERERQ-RAAEREEELEEGERLREEE 324
|
250
....*....|..
gi 530389149 1577 RSAEAELQSKRA 1588
Cdd:pfam13868 325 AERRERIEEERQ 336
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1417-1961 |
4.41e-09 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 428594 [Multi-domain] Cd Length: 562 Bit Score: 62.74 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1417 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1494
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1495 RQAQEEAERLRRQVQDESQRKRQAEVELASrVKAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEVERAr 1566
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1567 QVQVALETAQRS-AEAELQSKRASFA--EKTAQLERSLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLKA 1643
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 NEALRLRLQAEEVAQQKSlaqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1720
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1721 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1800
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1801 frelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1878
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1879 AFQR-------------RRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAG 1945
Cdd:pfam05701 466 DSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKEG 544
|
570
....*....|....*.
gi 530389149 1946 KAELELELGRIRSNAE 1961
Cdd:pfam05701 545 KLAAEQELRKWRAEHE 560
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
2003-2631 |
4.73e-09 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 63.19 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2003 EEAARQRKAALEEVERLKAKVEEARRLRERAEqesaRQLQLAQEAaqKRLQAEEKAHAFAVQQKEQELQQTLqqeqsvLD 2082
Cdd:COG1196 175 EEAERKLERTEENLERLEDLLEELEKQLEKLE----RQAEKAERY--QELKAELRELELALLLAKLKELRKE------LE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2083 QLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2162
Cdd:COG1196 243 ELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2163 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEET----DHQKNLLDEELQRLKAEATEAARQRSQVEEELFSV 2238
Cdd:COG1196 323 ERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELeeklSALLEELEELFEALREELAELEAELAEIRNELEEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2239 RVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2318
Cdd:COG1196 403 KREIESLEERLERLSERLEDLKEELKELEAELEELQTEL-EELNEELEELEEQLEELRDRLKELERELAELQEELQRLEK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2319 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQqLAEETQGFQRTLE-----------------AERQRQL 2381
Cdd:COG1196 482 ELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAE-LIKVKEKYETALEaalgnrlqavvveneevAKKAIEF 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2382 EMSAEAERLKL----RVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLReaI 2457
Cdd:COG1196 561 LKENKAGRATFlpldRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDTLVVDDLEQARRLARKLRIKYR--I 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2458 AELE---------------REKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLE 2522
Cdd:COG1196 639 VTLDgdlvepsgsitggsrNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2523 QLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEE---GVRRKQEELQQLEQQRRQQEELLAEENQRL 2599
Cdd:COG1196 719 EELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEeleSLEEALAKLKEEIEELEEKRQALQEELEEL 798
|
650 660 670
....*....|....*....|....*....|..
gi 530389149 2600 REQLQLLEEQHRAALAHSEEVTASQVAATKTL 2631
Cdd:COG1196 799 EEELEEAERRLDALERELESLEQRRERLEQEI 830
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4314-4351 |
4.96e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 4.96e-09
10 20 30
....*....|....*....|....*....|....*...
gi 530389149 4314 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4351
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1690-1946 |
5.20e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 62.05 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1690 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEM 1769
Cdd:COG4942 38 KQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQRRRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1770 EVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEEaaRLRALAEEAKRQRQLA--EEDAARQRAEAERVLAEKL 1844
Cdd:COG4942 118 AEQLAALQRSGRNPPPAllvSPEDAQRSVRLAIYYGALNPA--RAERIDALKATLKQLAavRAEIAAEQAELTTLLSEQR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1845 AAIGEATRL-----KTEAEIAlKEKEAENERLRRLAEDEAFQRR---RLEEQAA--QHKADIEERLAQLRKASDSELERQ 1914
Cdd:COG4942 196 AQQAKLAQLleerkKTLAQLN-SELSADQKKLEELRANESRLKNeiaSAEAAAAkaREAAAAAEAAAARARAAEAKRTGE 274
|
250 260 270
....*....|....*....|....*....|..
gi 530389149 1915 KGLVEDTLRQRRQVEEEILALKASFEKAAAGK 1946
Cdd:COG4942 275 TYKPTAPEKMLISSTGGFGALRGQLAWPVTGR 306
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
159-261 |
6.42e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 159 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 237
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPgLCPDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 530389149 238 TRLLDPEDVDVPQPDEKSIITYVS 261
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1683-1868 |
7.34e-09 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 61.12 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEEQA--VRQRELAEQE----LEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQkrq 1756
Cdd:COG3064 84 KEEQVAeeLKPKQAAEQErlkqLEKERLKAQ--EQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKKKAEAAKAKAAA--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1757 elEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1836
Cdd:COG3064 159 --EAAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEAE-----AKAAAEKAKAEAEAKAKAEKKAEAAAEEKAAA 231
|
170 180 190
....*....|....*....|....*....|..
gi 530389149 1837 ERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1868
Cdd:COG3064 232 EKKKAAAKAKADKAAAAAKAAERKAAAAALDD 263
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1721-2026 |
7.51e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.89 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1721 IRLRA-ETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1793
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1794 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlaeklaaigeatrlkteAEIALKEKEAENERLRR 1873
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1874 LAEDEAFQRRrleeqaaqhkadieerlAQLRKASdselerQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELEL 1953
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAA------QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1954 grIRSNAEDTLRSKEQAELEAARQRQLAAeeerrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 2026
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1107-1766 |
7.67e-09 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 62.48 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1107 EEVLRAHEEQLKE-----AQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVER 1181
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1182 WRERV-------AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLR 1254
Cdd:pfam01576 417 LQSRLseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSSRLR-QLE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1255 QEQALLEEieRHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESVIQEY-------- 1321
Cdd:pfam01576 496 DEKNSLQE--QLEEEEEAKRNVERQ----LQTLQAQLSDLKKKLEEDAGAVEaleegRKRLQRELEALTQRLeekaaayd 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1322 -----------------VDLRTHYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAH 1384
Cdd:pfam01576 570 klektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR-AEAEAREKETKALSLAR 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1385 A-----QAKAQAEREAKELQQRMQEEV------------VRREEAAVDAQQQKRSIQEE-------------------LQ 1428
Cdd:pfam01576 644 AleealDAKEELERQNKQLRAEMEDLVsskddvgknvheLERSKRALEQQVEEMKTQLEeledelqatedaklrlevnMQ 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1429 QLRQSSEAEIQAKARQAEAAERSRLRieeEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEA 1501
Cdd:pfam01576 724 ALKAQFERDLQARDEQGEEKRRQLVK---QVRELEAELEDERKQRAQAvaakkklELDLKELEAQIEAANKGRDEAVKQL 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1502 ERLRRQVQDesqrkRQAEVELASRVKAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEVERAR-QVQVALETA 1575
Cdd:pfam01576 801 KKLQAQMKD-----LQRELDEARASRDEIFAqSKESEKKLKSLEAELLQLQEdlaaAERARRQAQQERDElAEEIASGNS 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1576 QRSAeaeLQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELE-----RWQL-KANEALRL 1649
Cdd:pfam01576 876 GKSA---LLDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQksesaRQQLeRQNKELKA 952
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1650 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQEL 1720
Cdd:pfam01576 953 KLQEMEGTVKSKYKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRNADQYKDQAEKGNSRL 1032
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 530389149 1721 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR 1766
Cdd:pfam01576 1033 KQLKRQLEEAEEEASRANAARRKLQRELDDATESAEAMNREVTTLR 1078
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1166-1473 |
9.76e-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: 61.68 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1166 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdvRQRELEqlgRQLRYYRESAdplgawlQDARRRQEQIQAMPLAD 1245
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1246 SQAVREQLRQEQALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1318
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1319 QEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKEL 1398
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 1399 QQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAeAAERSRLRIEEEIRVVRLQLEATERQR 1473
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1658-1853 |
1.23e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.59 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1658 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1737
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1738 EEELARLQREAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1817
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 530389149 1818 AKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1853
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
159-266 |
1.62e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 159 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 237
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPgLCPDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 530389149 238 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1695-1882 |
1.86e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1695 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevllA 1774
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE-----A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1775 SKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVlAEKLAAIGEATRLK 1854
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAEAK 224
|
170 180
....*....|....*....|....*...
gi 530389149 1855 TEAEIALKEKEAENERLRRLAEDEAFQR 1882
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
35-149 |
1.96e-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: 55.29 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 35 DEQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQI 110
Cdd:cd21222 8 DEAPEKLAEVKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKL 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 530389149 111 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21222 83 ALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
34-148 |
2.32e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 54.82 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 34 QDEQDERdrvqkkTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNV 108
Cdd:cd21299 1 ETSREER------CFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENC 67
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 530389149 109 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 148
Cdd:cd21299 68 NQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
168-263 |
2.55e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 55.38 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 168 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNL-----------------------EN 223
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 530389149 224 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 263
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1052-1547 |
2.94e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1052 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEaqaVPATLPELE 1131
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1132 ATKASLKKLRAQAEAQQpTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLG 1211
Cdd:PRK03918 280 EKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1212 RQLRYYRE------------------SADPLGAWLQDARRRQEQIQAmPLADSQAVREQLRQEQALL----EEIERHGEK 1269
Cdd:PRK03918 359 ERHELYEEakakkeelerlkkrltglTPEKLEKELEELEKAKEEIEE-EISKITARIGELKKEIKELkkaiEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1270 VEECQR---------FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTHYSELTTLTSQYIK 1340
Cdd:PRK03918 438 CPVCGRelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES---ELIKLKELAEQLKELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1341 FISETLRRMEEE-----ERLA-----------EQQRAEERE-RLAEVEAAL-EKQRQLAEAHAQAKAQAEREAKELQQRM 1402
Cdd:PRK03918 515 YNLEELEKKAEEyeklkEKLIklkgeikslkkELEKLEELKkKLAELEKKLdELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1403 Q--EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGE 1479
Cdd:PRK03918 595 KelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRE 674
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1480 LQALRARAEEAEAQKRQAQEEAERLRRQVqdESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1547
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1417-1598 |
3.26e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1417 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqleaterqrggaegelqalraraEEAEAQKRQ 1496
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1497 AQEEAER-LRRQVQDESQRKRQAEvelASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER---ARQVQVAL 1572
Cdd:PRK09510 120 AEEAAKQaALKQKQAEEAAAKAAA---AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAA 196
|
170 180
....*....|....*....|....*.
gi 530389149 1573 ETAQRSAEAELQSKRASFAEKTAQLE 1598
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1330-2018 |
3.41e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 60.29 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1330 ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEE---RERLAEVEAALEKQRQLAEAHAQAKAQAEReAKELQQRMQEEV 1406
Cdd:COG3096 359 ELTIRLEEQNEVVEEANERQEENEARAEAAELEVdelKSQLADYQQALDVQQTRAIQYQQAIAALER-AKELCHLPDLTA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1407 VRREEAAVDAQQQKRSIQEELQQLRQSSEAEiQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQA---- 1482
Cdd:COG3096 438 DSAEEWLETFQAKEEEATEKLLSLEQKMSMA-QAAHSQFEQAYQLVVAIAGELARSEAWDVARELLREGPDQRHLAeqvq 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1483 -LRARAEEAEAQKRQaQEEAERLRRQ--------VQDESQRKRQAEVE-LASRVKAEAEAAREKQRAL-QALEELRLQAE 1551
Cdd:COG3096 517 pLRMRLSELEQRLRQ-QQSAERLLADfckrqgknLDAEELEALHQELEaLIESLSDSVSNAREQRMALrQEQEQLQSRIQ 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1552 EAERRlrqAEVERArqVQVALETAQRSAEAELQSKRASFAEKTAQLERSlQEEHVAVAQLREEAERRAQQqaeaeraree 1631
Cdd:COG3096 596 SLMQR---APVWLA--AQNALEQLSEQSGEEFTDSQDVTEYMQQLLERE-REATVERDELGARKNALDEE---------- 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1632 aereLERW-QLKANEALRLRLQAEEVAQQ------------------------------KSLAQAEAEKQKEEAEREARR 1680
Cdd:COG3096 660 ----IERLsQPGGSEDQRLNALAERFGGVllseiyddvtiedapyfsalygpsrhaivvPDLSQVKEHLEGLTDCPEDLY 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1681 RGKAEEQAVRQRELAEQELEK-------QRQL-----AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA 1748
Cdd:COG3096 736 LIEGDPQSFDDSVFSVDELEKavvvkiaDRQWrysrfPEIPLFGRAAREQRLESLHAERDVLSERHATLSFDVQKTQRLH 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1749 AAATQ------------KRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAE---AGRFRELAEEAarLRA 1813
Cdd:COG3096 816 QAFSRfigshlavafeaDPEAEIRQLNSRRNELERALSNHENDNQQQRIQFDQAKEGVTALnrlIPQLNLLADES--LAD 893
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1814 LAEEAKRQRQLAEEDAARQRAEAerVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAF------QRRRL-- 1885
Cdd:COG3096 894 RVEEIRERLDEAQEAARFIQQHG--NTLSKLEPIASVLQSDPEQFEQLKEDYAQAQQMQRQARQQAFaltevvQRRAHfs 971
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1886 ---EEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIrsnaed 1962
Cdd:COG3096 972 ysdSAEMLSENSDLNEKLRQRLEQAEAERTRAREQLRQHQAQLSQYNQVLASLKSSYDTKKELLNELQQELQDI------ 1045
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1963 TLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVER 2018
Cdd:COG3096 1046 GVRADSGAEERARIRRDELHAQLSTNRSRRNQLEKQLTFCEAEMDNLTRKLRKLER 1101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2202-2416 |
3.44e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 59.35 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2202 ETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQv 2281
Cdd:COG4942 35 ADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQ- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2282 aeeaaRLSVAAQEAARLRQLAEEDLA----QQRALAEKMLKEKMQAVQEAtRLKAEAELLQQQKELAQEQARRLQEDKEQ 2357
Cdd:COG4942 114 -----RRRLAEQLAALQRSGRNPPPAllvsPEDAQRSVRLAIYYGALNPA-RAERIDALKATLKQLAAVRAEIAAEQAEL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 2358 MAQ--QLAEETQGFQRTLEA----ERQRQLEMSAEAER---LKLRVAEMSRAQARAEEDAQRFRKQAE 2416
Cdd:COG4942 188 TTLlsEQRAQQAKLAQLLEErkktLAQLNSELSADQKKleeLRANESRLKNEIASAEAAAAKAREAAA 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1129-1887 |
3.56e-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: 60.24 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1129 ELEATKASLKKLRAQAEAQQPTFDALRDELRgaqevgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELE 1208
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1209 Q-LGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEEcqRFAKQYINAikdy 1287
Cdd:pfam12128 333 AfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD--KLAKIREAR---- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1288 ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYvDLRTHYSELTTLTSQYIkFISETLRRMEEEERLAEQQRAEERERL 1367
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQAT-ATPELLLQLENFDERIERAREEQEAAN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1368 AEVEAAlekQRQLAEAHAQAKAQAEReakelqqrmqeevVRREEAAVdaQQQKRSIQEELQQLRQSSEAEIQAKARQAEA 1447
Cdd:pfam12128 485 AEVERL---QSELRQARKRRDQASEA-------------LRQASRRL--EERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1448 AERSRLRIEEEIRVVRLQL--EATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQV-----QDESQRKRQAEV 1520
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLdpEVWDGSVGG-ELNLYGVKLDLKRIDVPEWAASEEELRERLDKaeealQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1521 ELASRVKAEAEAAREKQRALQALEelrlQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQskraSFAEKTAQLERS 1600
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALK----NARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN----SLEAQLKQLDKK 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1601 LQeehvavaqlreeaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQkslaqaeaekqKEEAEREARR 1680
Cdd:pfam12128 698 HQ-------------------------------AWLEEQKEQKREARTEKQAYWQVVEG-----------ALDAQLALLK 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1681 RGKAEEQAVRQRELAEQELEKQRQLAE-GTAQQRLAA-EQELIRLRAETEQGEQQRQLLeEELARLQREaaAATQKRQEL 1758
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASlGVDPDVIAKlKREIRTLERKIERIAVRRQEV-LRYFDWYQE--TWLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1759 EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlaeeakRQRQLAEEDAARQRAEAER 1838
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANSEQAQG 886
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1839 VLAEKLAAiGEATRLKTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 1887
Cdd:pfam12128 887 SIGERLAQ-LEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1683-1838 |
3.95e-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: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1762
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1763 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EAARLRALAEEAKRQRQLAeedAARQRAEAER 1838
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEAAKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1346-1563 |
4.23e-08 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 58.81 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1346 LRRMEEEERLAEQQRAEERERLAEveaALEKQRQlaeahaqAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQE 1425
Cdd:COG3064 67 IQSQQSSAKKGEQQRKKKEEQVAE---ELKPKQA-------AEQERLKQLEKERLKAQEQQKQAEEAEKQAQLEQKQQEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1426 elQQLRQSSEAEIQAKARQAEAAERSRlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1505
Cdd:COG3064 137 --QARKAAAEQKKKAEAAKAKAAAEAA----------KLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAA 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1506 RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVE 1563
Cdd:COG3064 205 EKAKAEAEAKAKAEKKAEAAAEEKAAAEKKKAAAKAKADKAAAAAKAAERKAAAAALD 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1152-1584 |
4.54e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1152 DALRDELRGAQEVGERLQQRHGERDVEVERWRE-----------RVAQLLERWQAV---LAQTDVRQRELEQLGRQLRYY 1217
Cdd:PRK04863 743 DSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgraarekRIEQLRAEREELaerYATLSFDVQKLQRLHQAFSRF 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1218 RES-------ADPLGAWLQDARRRQEQIQAMPLADSQAVR-----EQLRQEQALLEEI---------ERHGEKVEECQ-- 1274
Cdd:PRK04863 823 IGShlavafeADPEAELRQLNRRRVELERALADHESQEQQqrsqlEQAKEGLSALNRLlprlnlladETLADRVEEIReq 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1275 --------RFAKQYINAIkdyelqlvtykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKF 1341
Cdd:PRK04863 903 ldeaeeakRFVQQHGNAL-----------AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHF 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1342 -ISETLRRMEEEERLAEQQRAeereRLAEVEAALEKQRqlaEAHAQAKAQAeREAKELQQRMQEEVVRreeaavdAQQQK 1420
Cdd:PRK04863 972 sYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERTRAR---EQLRQAQAQL-AQYNQVLASLKSSYDA-------KRQML 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1421 RSIQEELQQL--RQSSEAEIQAKARQAEaaersrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1498
Cdd:PRK04863 1037 QELKQELQDLgvPADSGAEERARARRDE--------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1499 EEAE-------RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKqrALQALeelrlqaeeaerRLRQAEVERARQVQVA 1571
Cdd:PRK04863 1109 EQVVnakagwcAVLRLVKDNGVERRLHRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRL 1174
|
490
....*....|...
gi 530389149 1572 LETAQRsAEAELQ 1584
Cdd:PRK04863 1175 SEDPKR-PERKVQ 1186
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1694-1912 |
6.33e-08 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 58.42 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1694 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRQELEAELAKVRAEMEvll 1773
Cdd:COG3064 59 AVVQQYGRIQSQQSSAKK---GEQQRKKKEEQVAEELKPKQAAEQERLKQLEKERLKA-QEQQKQAEEAEKQAQLEQ--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1774 asKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAARLRALAE---EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1850
Cdd:COG3064 132 --KQQEEQARKAAAEQKKKAEAAKA----KAAAEAAKLKAAAEakkKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530389149 1851 TRLKTEAEIALKEKEAEnerlrRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELE 1912
Cdd:COG3064 206 KAKAEAEAKAKAEKKAE-----AAAEEKAAAEKKKAAAKAKADKAAAAAKAAERKAAAAALD 262
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1347-1602 |
6.64e-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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 58.00 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1347 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1426
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKQYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1427 LQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVR--LQLEATERQRGGAEGELQALRARAEEAEAQKRQ---AQEEA 1501
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEedLRILEYLKEKAEREEEREAERREIKEEKEREIArlrAQQEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1502 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1581
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERKWRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE 275
|
250 260
....*....|....*....|.
gi 530389149 1582 ELQSKRASFAEKTAQLERSLQ 1602
Cdd:pfam13868 276 IEQEEAEKRREKRLEHRRELE 296
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1397-1610 |
7.06e-08 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 58.50 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1397 ELQQRMQEEVVRREEAAVdAQQQKRSIQEELQQLRQSSEA---EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1473
Cdd:COG4372 75 QLDDIRPQLRALRTELGT-AQGEKRAAETEREAARSELQKarqEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1474 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEvelasrvkAEAEAAREKQRALQALEElRLQAEEA 1553
Cdd:COG4372 154 KTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIE--------QEAQNLATRANAAQARTE-ELARRAA 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1554 ERRLRQAEV-ERARQV-QVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ 1610
Cdd:COG4372 225 AAQQTAQAIqQRDAQIsQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQ 283
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1428-1595 |
7.89e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1428 QQLRQSsEAEIQAKARQAEAAERSRLRIEEeiRVVRLQLEATERQrggaegelqalrARAEEAEAQKRQAQEEA-----E 1502
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAARE------------ARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1503 RLR-RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1581
Cdd:PRK05035 494 RVKaKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170
....*....|....
gi 530389149 1582 ELQSKRASFAEKTA 1595
Cdd:PRK05035 574 EVDPKKAAVAAAIA 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1366-1587 |
8.12e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 58.19 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1366 RLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAK---A 1442
Cdd:COG4942 39 QLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQRrrlA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1443 RQAEAAERS--------RLRIEEEIRVVRLQ------LEATERQRGGAEGELQALRARAEEAEAQKRQAQ-------EEA 1501
Cdd:COG4942 119 EQLAALQRSgrnpppalLVSPEDAQRSVRLAiyygalNPARAERIDALKATLKQLAAVRAEIAAEQAELTtllseqrAQQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1502 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1581
Cdd:COG4942 199 AKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAKRTGETYKP 278
|
....*.
gi 530389149 1582 ELQSKR 1587
Cdd:COG4942 279 TAPEKM 284
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4045-4081 |
8.65e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 8.65e-08
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 4045 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4081
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1357-2036 |
9.82e-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: 58.90 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1357 EQQRAEERERLAEVEAALEKQRQLAE---AHAQAKAQAEREAKELQQRMQE------------------EVVRREEAAVD 1415
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNeikALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyhnhqrTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1416 AQQQKRSIQEELQQLRQSS---EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG----------------GA 1476
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfhtlvieRQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1477 EGELQALRARAEEAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRlq 1549
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRdekkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1550 aeEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLER---------SLQEEHVAVAQLREEAERRAQ 1620
Cdd:TIGR00606 482 --KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqmeMLTKDKMDKDEQIRKIKSRHS 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1621 QQAEAERAREEAERELERW-QLKANEALRLRLQAEEVaqQKSLAQAEAEKQKEEAerearrrgkaeeqavRQRELAEQEL 1699
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKL--NKELASLEQNKNHINN---------------ELESKEEQLS 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1700 EKQRQLAEGTAQQrlAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEM 1769
Cdd:TIGR00606 623 SYEDKLFDVCGSQ--DEESDLERLKEEIEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1770 EVLLASKARAEEESRSTSEKSKQRLEAEAGRF-----------RELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAE 1837
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqsiidlkeKEIPELRNKLQKVNRDIQRLKNdIEEQETLLGTIMPE 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1838 RVLAEKLAA-IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD------------IEERLAQLR 1904
Cdd:TIGR00606 781 EESAKVCLTdVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQ 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1905 --KASDSELERQKGLVEDTLRQRRQVEE-------EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAA 1975
Cdd:TIGR00606 861 hlKSKTNELKSEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530389149 1976 RQRQLAAEEERRRREAEERVQKSLaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2036
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1347-1608 |
1.24e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 434789 [Multi-domain] Cd Length: 374 Bit Score: 57.36 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1347 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAK--ELQQRMQEEVVRREEAAVDAQQQKRSIQ 1424
Cdd:pfam15558 21 QLMRELQQQAALAWEELRRSDQKVQETLERERRLLLQQSQEQWQAQKEQRkrRLGREERRRRDRREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1425 EELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqleaterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1504
Cdd:pfam15558 101 EDQENQRQEKLERAAQEAEQRKQCQEQNLKEKEEEL------------QALREQNGLQLQERLEQAC-HKRQLKELEEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1505 RRQVQDESQRKRQA--EVELASRVKAEAEAARE--KQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAE 1580
Cdd:pfam15558 168 KVQENNLSELLNHQarKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKLRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 530389149 1581 AELQSKRASFAEKTAQLERSLQEEHVAV 1608
Cdd:pfam15558 248 EQQEHKEALAELADQKIQQARSVAHKTV 275
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
46-145 |
1.27e-07 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 52.72 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 46 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQ 119
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARG 75
|
90 100
....*....|....*....|....*.
gi 530389149 120 VKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21286 76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1345-1610 |
1.33e-07 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 58.11 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1345 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKELQQRMQEEVVRREEAAVDAQQQKRSIQ 1424
Cdd:COG5281 301 AAAAAAEAAAAMDDRTARVKENMGTLETAWDALADAAKKMWDAVLGIGRE-DKQAALLAAKLAAEKLARVTAQGALNARL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1425 EELQQLRQSSEAEiQAKARQAEAAERSRLRIEEEIRVVRLQLE---ATERQRGGAEGELQALRARAEE-AEAQKRQAQEE 1500
Cdd:COG5281 380 KLAQDDLTQAELN-YAAADQAANQEGALNAREDEAEVLSTQEErrdILKNLLADAEKRTARQEELNKAlAKAKILQADKA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1501 AERLRRQV---QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERArQVQVALETAQR 1577
Cdd:COG5281 459 AKAYQEDIlqrEAQSRGKTAAAERSQEQMTAALKALLAFQQQIADLSGAKEKASDQKSLLWKAEEQYA-LLKEEAKQRQL 537
|
250 260 270
....*....|....*....|....*....|...
gi 530389149 1578 SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ 1610
Cdd:COG5281 538 QEQKALLEHKKETLEYTSQLAELLDQQADRFEL 570
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1781-2066 |
1.45e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1781 EESRSTSEKSKQ----RLEAEagRFRELAEEAARlralaeEAKRQRQLAEEDAARQrAEAERvlaeKLAAIGEATRLKTE 1856
Cdd:pfam17380 279 QHQKAVSERQQQekfeKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1857 AE-----IALKEKEAENERLRR--LAEDEAFQRR--RLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTL----- 1922
Cdd:pfam17380 346 RErelerIRQEERKRELERIRQeeIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVemeqi 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1923 ---------RQRRQVEEEilaLKASFEKAAAGKAELELELGRIRSNAEDtlRSKEQAELEAARQRQLAAEEERRRREAEE 1993
Cdd:pfam17380 426 raeqeearqREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1994 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHAFAVQQK 2066
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMERE 574
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2172-2475 |
2.04e-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: 57.34 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2172 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKAR 2251
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2252 IEAENRAL------ILRDKDNTQRFLQEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2323
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2324 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLeaerqrqlemsaeaERLKLRVAEMSRAQAR 2403
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI--------------EELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530389149 2404 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2475
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1108-1834 |
2.05e-07 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 57.55 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1108 EVLRAHEEQLKEAQAvpaTLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQ----------RHGERDV 1177
Cdd:COG4717 164 EVLNKEADSLYKPSG---RNPQINQLLEKLKQERNEIDEAEKEYATYHKLLESRRAEHARLAElrselradrdHIRALRD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1178 EVERWRervaqLLERWQAVLAQTDVRQRELEQLGR----QLRYYRESADPLGAWLQDARRRQEQI-----QAMPLADS-- 1246
Cdd:COG4717 241 AVELWP-----RLQEWKQLEQELTRRREELATFPRdgvlRLEKREAHLQKTEAEIDALLVRLAELkdlasQLIPAKEAvl 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1247 QAVREQLRQEQALLEEIERHGEKVEECQRFAKQYInaikdyelqlvtykAQLEPVASPAKKPKVQSGSEsvIQEYVDLRT 1326
Cdd:COG4717 316 QALVRLHQQLSEIKASAFELTETLAGIEADLRDKE--------------EAAGNGFEAERVHDLRSLEC--MLRYQSSQR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1327 hysELTTLTSQYIKFISE-TLRRMEEEERLAEQQRAEERERLAEVEAALEKQ---RQLAEAHAQAKAQAEREAKELQQRM 1402
Cdd:COG4717 380 ---ELKQTEAAYCKRLDEkRLFEDEAEEEARQRLADDEEEVRAGDEAREEKIaanSQVIDKEEVCNLYDRRDTAWQKQRF 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1403 ---QEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRlqleaterqrggaege 1479
Cdd:COG4717 457 lreKQTAFERQKTEHTKIIALRLAGMLLVALSRLLTSLIFQIIFAVAQIVFLSAEIKSSSRAVR---------------- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1480 lqALRARAEEAEAQKRQAQEEAERLRRQV-QDESQRKRQAEVELASRVKaeaeaarEKQRALQALEElRLQAEEAERRLR 1558
Cdd:COG4717 521 --EEKAAVTDIPEELARLLITDELPELAVdLLVQSRIRQHWQQLRKALD-------QLEAAYEALEG-RFAAAEAAMAEW 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1559 QAEVERA-------RQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREE 1631
Cdd:COG4717 591 QSEWEEAldelglsRELSPEQQLDILSTMKDLKKLMQKKAELTHQVARLREEQAAFEERVEGLLAVLEAQFIDLSTLFCV 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1632 AERELERwqLKANEALRLRLQA-EEVAQQKSLAQAEAEKQKEEAEREARRRGKA-EEQAVRQRELAEQELEKQRQLAEGT 1709
Cdd:COG4717 671 QRLRVAA--ELQKEEARLALEGnIERTKELNDELRAELELHRKEILDLFDCGTAdTEDAFREAAREEQQLTQRESRLESL 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1710 AQQRLAAEQElirlRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEK 1789
Cdd:COG4717 749 EAQLEGVAAE----AYELSASLDQRELKEEELALLEEAIDALDEEVEELHAQVAALSRQIAQL---------EGGGTVAE 815
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 530389149 1790 SKQRLEAEAGRFRELAEEAARLRA---LAEEAKRQRQLAEEDAARQRA 1834
Cdd:COG4717 816 LRQRRESLKEDLEEKARKWASLRLavqVLEEALRLFKERRLPAVIQEA 863
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1344-1566 |
2.10e-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: 56.39 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQkr 1421
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1422 siqeelqqlrqsseaeiQAKARQAEAAersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE- 1500
Cdd:TIGR02794 146 -----------------EEAAKQAEEE--------------AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1501 ---AERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1566
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1357-1603 |
2.40e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 57.15 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1357 EQQRAEERERLAEVEAALEKQRQLAEA--HAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQ--QLRQ 1432
Cdd:COG2268 215 RIAQVLQDAEIAENEAEKETEIAIAEAnrDAKLVELEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAETRREaeQAEI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1433 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1512
Cdd:COG2268 295 LAEQAIQEEKAQAEQEVQHAKALEAREMRVGLIERQKETELEPQERSYFINAAQRQAQEEAKAAANIAEAIGAQAEAAVE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1513 QRKRQAEVELASRVKAE--AEAAREKQRALQALEELRLQAEEAE--RRLRQAEVERARQvQVALETAQRSAEAELQSKRA 1588
Cdd:COG2268 375 TARETEEAERAEQAALVaaAEAAEQEQVEIAVRAEAAKAEAEAQaaEIKAEAEAIREKG-KAEAEAKRALAEAIQVLGDA 453
|
250
....*....|....*
gi 530389149 1589 SFAEKTAQLERSLQE 1603
Cdd:COG2268 454 AAAELFKALVQALPE 468
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1370-1589 |
2.47e-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: 56.01 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1370 VEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAE 1449
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKL----EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1450 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEAERLRRQVQDESQRKRQAEVELASRVKAE 1529
Cdd:TIGR02794 114 AEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKA-KAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1530 AEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRAS 1589
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGA 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1832-2222 |
2.73e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.06 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1832 QRAEAERVLAEKLAAIgEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasDSEL 1911
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1912 ERQKglVEDTLRQRRQVEEEILALKASFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAARQRQLAaeeerrrre 1990
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1991 aeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHafavQQKEQE 2069
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLR----QQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2070 LQQTLQQEQSVLDQLRGEAEAARRAaeeaeearvqaEREAAQSRRQVEEAERlKQSAEEQAQARAQAQAAAEKLRKEAEQ 2149
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEEQRRKIL-----------EKELEERKQAMIEEER-KRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 2150 EaarraqaeqaalRQKQaadAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKNLLDEELQRLKAEAT 2222
Cdd:pfam17380 541 E------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1351-1535 |
2.85e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1351 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAKELQQRMqeevvrrEEAAVDAQQQKRSIQEELQQL 1430
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRA-------AAAAKKAAAEAKKKAEAEAAK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1431 RQSSEAEIQAKARQAEAAersrlrieeeirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1510
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKA------------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 530389149 1511 ESQRKRQAEVELASRVKAEAEAARE 1535
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1350-1515 |
3.33e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.62 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1350 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQ 1429
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1430 LRQSSEAEIQAKARQAEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1498
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 530389149 1499 EEAERLRRQVQDESQRK 1515
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2263-2612 |
3.44e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.67 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2263 DKDNTQRFLQEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEKmlkEKMQAVQEATRLKAEAELLQQQKE 2342
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDRQ---AAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2343 LAQEQARRLQEDKEQMAQQLAEETQGFQ--RTLEAERQRQlEMSAeAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2420
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQmeRQQKNERVRQ-ELEA-ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2421 -KLHRTELATQEKVTLVQTLEIQRQqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqllqetqaLQQS 2499
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQ---QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-----------LEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2500 FLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAQQLREEQQRQqqqmeqerqrlvasmEEARRRQHEAEEGvRRKQEELQ 2579
Cdd:pfam17380 501 LEERKQAMIEEER-----KRKLLEKEMEERQKAIYEEERRREA---------------EEERRKQQEMEER-RRIQEQMR 559
|
330 340 350
....*....|....*....|....*....|...
gi 530389149 2580 QLEQQRRQQeellaEENQRLREQLQLLEEQHRA 2612
Cdd:pfam17380 560 KATEERSRL-----EAMEREREMMRQIVESEKA 587
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1457-1653 |
3.67e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 56.19 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1457 EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE---AERLRRQVQDESQRKRQAEVELAS---RVKAEA 1530
Cdd:COG4372 88 TELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNlakAQQELARLTKQAQDLQTRLKTLAEqrrQLEAQA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1531 EAAREKQRALQALEElRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRAS---FAEKTAQLERSLQEEHVA 1607
Cdd:COG4372 168 QSLQASQKQLQASAT-QLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELARRAAAaqqTAQAIQQRDAQISQKAQQ 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530389149 1608 VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQA 1653
Cdd:COG4372 247 IAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQA 292
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1198-1898 |
3.80e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 56.65 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1198 AQTDVRQRE---LEQLGRQLR---YYRESADPLGA-WLQDARRRQEQIQAMPLAdSQAVREQLRQeqALLEEIERHGEKV 1270
Cdd:pfam15921 128 AMADIRRREsqsQEDLRNQLQntvHELEAAKCLKEdMLNDSNTQIEQLRKMMLS-HEGVLQEIRS--ILVDFEEASGKKI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1271 EECQRFAKQYINA--------IKDYELQLVTYKAQLEPVAS--PAKKPKVQSGSESVIQEYVD-----LRTHYSELTTLT 1335
Cdd:pfam15921 205 YEHDSMSTIHFRSlgsaiskiLRELDTEISYLKGRIFPVEDqlEALKSESQNKIELLLQQHQDrieqlISEHEVEITGLT 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1336 SQ-------------YIKFISET--------LRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQ-AKAQAE 1392
Cdd:pfam15921 285 EKassarsqansiqsQLEIIQEQarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSElTEARTE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1393 REA---------KELQQRMQEEVVRREEAAVDAQQQKRsiqeeLQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVR 1463
Cdd:pfam15921 365 RDQfsqesgnldDQLQKLLADLHKREKELSLEKEQNKR-----LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1464 LQLEA-TERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQVQDESQRKrqAEVELASRVKAEAEAA-REKQRALQ 1541
Cdd:pfam15921 440 SECQGqMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKK--MTLESSERTVSDLTASlQEKERAIE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1542 A----LEELRLQAEEAERRLRQAEVErarqvqvalETAQRSAEAELQSKRASFAEKTAQLErSLQEEHVAVAQLreeaer 1617
Cdd:pfam15921 514 AtnaeITKLRSRVDLKLQELQHLKNE---------GDHLRNVQTECEALKLQMAEKDKVIE-ILRQQIENMTQL------ 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1618 raqqqaEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKSlaqaeaekqkeeaerearrRGKAEEQAVRQRELae 1696
Cdd:pfam15921 578 ------VGQHGRTAGAMQVEKAQLeKEINDRRLELQEFKILKDKK-------------------DAKIRELEARVSDL-- 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1697 qELEKQRQLAEGTAQQRLAAE--QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQ----ELEAELAKVRAEME 1770
Cdd:pfam15921 631 -ELEKVKLVNAGSERLRAVKDikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELE 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1771 V---LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAI 1847
Cdd:pfam15921 710 QtrnTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA 789
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1848 GEATRLKTEaEIALKEKEAENE-----RLRRLAEDEAFQRRRLEEQAA---QHKADIEE 1898
Cdd:pfam15921 790 GELEVLRSQ-ERRLKEKVANMEvaldkASLQFAECQDIIQRQEQESVRlklQHTLDVKE 847
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1731-1906 |
4.22e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1731 EQQRQLLEEELAR-LQREAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1809
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1810 RLRALAEeakrqrQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1889
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 530389149 1890 AQHKADIEERLAQLRKA 1906
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2308-2609 |
4.95e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2308 QQRALAEKMLKEKMQavqeatrlKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAEETQGfqrTLEAERQR-QLEMSA 2385
Cdd:pfam17380 280 HQKAVSERQQQEKFE--------KMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQA---AIYAEQERmAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2386 EAERLKLRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTELATQEKVTLV-QTLEIQRQQSDHDAERLREaIAELEREK 2464
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVrQELEAARKVKILEEERQRK-IQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2465 EKL---QQEAKLLQLK--SEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQ 2539
Cdd:pfam17380 423 EQIraeQEEARQREVRrlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2540 QRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRrqqeellaEENQRLREQLQLLEEQ 2609
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2184-2480 |
5.25e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2184 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILR- 2262
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERf 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2263 -----DKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAE-------------------------------EDL 2306
Cdd:PRK02224 401 gdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvetieedrervEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2307 AQQRALAE---KMLKEKMQAVQEATRLKAEAELLQQQKELAQE---QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2380
Cdd:PRK02224 481 EAELEDLEeevEEVEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2381 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK-------------QAEEIGEKL-HRTELATQEKVTLVQTLEIQRQ-Q 2445
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKReALAELNDERRERLAEKRERKRElE 640
|
330 340 350
....*....|....*....|....*....|....*
gi 530389149 2446 SDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2480
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4148-4176 |
5.42e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 48.49 E-value: 5.42e-07
10 20
....*....|....*....|....*....
gi 530389149 4148 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4176
Cdd:pfam00681 11 IIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1925-2480 |
5.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1925 RRQVEEEILALKaSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEE 2004
Cdd:PRK03918 147 REKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2005 AARQRKaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL 2084
Cdd:PRK03918 225 KLEKEV---KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2085 RGEAEAARRAAEEAEEARvqaEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ 2164
Cdd:PRK03918 302 YEEYLDELREIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2165 KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE-----LFSVR 2239
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2240 VQMEELSKLKARIEAENRALiLRDKDNTQRFLQEEAE--KMKQVAEEAARLSvaaqeaARLRQLAEEDLAQQRALAEKML 2317
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKL-RKELRELEKVLKKESEliKLKELAEQLKELE------EKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2318 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2396
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2397 msRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2476
Cdd:PRK03918 612 --KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
....
gi 530389149 2477 KSEE 2480
Cdd:PRK03918 688 RREE 691
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3726-3761 |
6.38e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 6.38e-07
10 20 30
....*....|....*....|....*....|....*.
gi 530389149 3726 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3761
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DUF3523 |
pfam12037 |
Domain of unknown function (DUF3523); This presumed domain is functionally uncharacterized. ... |
1325-1458 |
7.24e-07 |
|
Domain of unknown function (DUF3523); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 257 to 277 amino acids in length. This domain is found associated with pfam00004. This domain has a conserved LER sequence motif.
Pssm-ID: 432279 [Multi-domain] Cd Length: 264 Bit Score: 53.83 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1325 RTHYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreakelQQ 1400
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqleIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEE------LL 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1401 RMQEEVVRREEAAVDAQQQKRSIQEEL----QQLRQSSEAEIQAKARQAEAA-----ERSRLRIEEE 1458
Cdd:pfam12037 130 RMQEESVAKQEAMRIQAQRRQTEEHEAelrrETEMAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2321-2466 |
9.12e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.41 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2321 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLAEEtQGFQRTLEAERQRQLEMSAEAERLKL 2392
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 2393 RVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2466
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2279-2483 |
1.02e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2279 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2358
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2359 AQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2438
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530389149 2439 LEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2483
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1742-2472 |
1.02e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1742 ARLQREAAAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1818
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1819 KRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIalkekEAENERLR---RLAEDEAfQRRRLEEQAAQH 1892
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRV-----QAENARLEmhfKLKEDHE-KIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1893 KADIEERLAQLRKASDSELERQKGL---VEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSkeq 1969
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1970 aeleaarQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV---EEARRLRERAEQESARQLQLAQE 2046
Cdd:pfam05483 312 -------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcslEELLRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2047 AAQKRLQAEEKAHAFAVQQKEQelqqtlqqeqsvLDQLRgeaeaarraaeeaeeaRVQAEREAA-QSRRQVEE-AERLKQ 2124
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE------------LEELK----------------KILAEDEKLlDEKKQFEKiAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2125 SAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEME--KHKKFAEQTLRQKAQVEQELTTLRLQLEE 2202
Cdd:pfam05483 437 KEQELIFLLQA---------------------------REKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2203 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELskLKARIEAENRALILRDKDNTQR--FLQEEAE---K 2277
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--LKQIENLEEKEMNLRDELESVReeFIQKGDEvkcK 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2278 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2357
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2358 MAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQ---------------ARAEEDAQRFRKQAEEIGEKL 2422
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSEL 727
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 530389149 2423 HRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAK 2472
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| DUF812 |
pfam05667 |
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ... |
2164-2349 |
1.05e-06 |
|
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.
Pssm-ID: 428574 [Multi-domain] Cd Length: 601 Bit Score: 55.02 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2164 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKNLLDEELQRLKAEATeaarqrsQVEEELFSVRVQME 2243
Cdd:pfam05667 310 NEEAPAATSSPPTKAETEEELQQQR-EEELEELQEQLEELESSIEELEKEIKKLESSIK-------QVEEELEELKEQNE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2244 ELS---KLKARI-----EAENRALILrdkdntQRFLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALA 2313
Cdd:pfam05667 382 ELEkqyKVKKKTldllpDAEENIAKL------QALVEASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKESESQRKLE 455
|
170 180 190
....*....|....*....|....*....|....*....
gi 530389149 2314 E-KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2349
Cdd:pfam05667 456 EiKELREKIKEVAEEARSKEElyKQLVAEYERLPKDVNR 494
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1352-1979 |
1.16e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.19 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1352 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAKELQQRMQEEVVRREEA 1412
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1413 AVDAQQQKRSIQEELQQLRQ-SSEAEIQAKARQAEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1487
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1488 EEAEAQKRQAQEEAERLR---RQVQDESQRKRQAEVElasrvKAEAEAAREKQRALQALEELRLQAEEaerrlRQAEVER 1564
Cdd:PRK10246 410 EVAAALAQHAEQRPLRQRlvaLHGQIVPQQKRLAQLQ-----VAIQNVTQEQTQRNAALNEMRQRYKE-----KTQQLAD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1565 ARQVqvaleTAQRSAEAELQSKRASF-AEKTAQLERSlqEEHVAVAQLREEAERRAQQQAEAERAreeaerelERWQLKa 1643
Cdd:PRK10246 480 VKTI-----CEQEARIKDLEAQRAQLqAGQPCPLCGS--TSHPAVEAYQALEPGVNQSRLDALEK--------EVKKLG- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 NEALRLRLQAEEVAQQKSlaqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRL 1723
Cdd:PRK10246 544 EEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPW 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1724 RAETEQGEQQRQLLEEELArLQREAAAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAE 1797
Cdd:PRK10246 602 LDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1798 AGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAIGEATrLKTEAEIALKEKEAENERlRRLAE- 1876
Cdd:PRK10246 681 QNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKa 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1877 ----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASDSELERQKGLVEdtlrQRRQVEEEILALKASFEKAAAGKAE 1948
Cdd:PRK10246 751 qaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQ 826
|
650 660 670
....*....|....*....|....*....|....*.
gi 530389149 1949 LELEL----GRIRSNAEDTLRSKEQAELEA-ARQRQ 1979
Cdd:PRK10246 827 IQQELaqlaQQLRENTTRQGEIRQQLKQDAdNRQQQ 862
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
32-151 |
1.21e-06 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 50.77 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 32 WAQDEQDERdrvQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHK 104
Cdd:cd21331 14 WTLLEGETR---EERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKK 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 530389149 105 LQNVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21331 84 LENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1039-1606 |
1.38e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1039 EGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLK 1118
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQE--QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1119 EAQAvpaTLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERlqQRHGERDVEVERWRERVAQLLERWQavla 1198
Cdd:TIGR00606 482 KAER---ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL--NHHTTTRTQMEMLTKDKMDKDEQIR---- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1199 qtDVRQRELEQLGRQLRYYRESADpLGAWLQDARRRQEQIQ------AMPLADSQAVREQLR-QEQALLEEIERHGEKVE 1271
Cdd:TIGR00606 553 --KIKSRHSDELTSLLGYFPNKKQ-LEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINnELESKEEQLSSYEDKLF 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1272 EcqrfakqyINAIKDYELQLVTYKAQLEpvaSPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYIKFISETLR 1347
Cdd:TIGR00606 630 D--------VCGSQDEESDLERLKEEIE---KSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1348 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrreeAAVDAQQQKRSIQEEL 1427
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK-------VNRDIQRLKNDIEEQE 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1428 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1507
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1508 VQDESQRKRQAEV---ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAEAELQ 1584
Cdd:TIGR00606 852 IQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAK-EQDSPLETFLEKDQQEKEELIS 930
|
570 580
....*....|....*....|..
gi 530389149 1585 SKRASfaEKTAQLERSLQEEHV 1606
Cdd:TIGR00606 931 SKETS--NKKAQDKVNDIKEKV 950
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2163-2619 |
1.43e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2163 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQ--LEETDHQKnllDEELQRLKAEATEAARQRSQVEEELFSVRV 2240
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQ---EIHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2241 QMEELSKLKARIEAENRAL-ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2319
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELdILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2320 KMQAVQEATRLKAEAE-LLQQQKELAQEQARRLQEDKEQ------------MAQQLAEETQGFQRTLEAERQRQLEMSAE 2386
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEqIHLQETRKKAVVLARLLELQEEpcplcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2387 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTelaTQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2466
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS---KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2467 LQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDsllqrerfiEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQM 2546
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER---------VREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 2547 EQERQRLVASMEEARRRQHEAEEGVRRkqeELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE 2619
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDR---EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE 761
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2184-2469 |
1.55e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2184 RQKAQVEQELTTLRLQLeeTDHQknlldeelQRLKAEATEAArQRSQVEEELFSVRVQME----ELSKLKARIEAenraL 2259
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQ--------QALDVQQTRAI-QYQQAVQALERAKQLCGlpdlTADNAEDWLEE----F 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2260 ILRDKDNTQRFLQEE-----AEKMKQVAEEAARL------SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKE 2319
Cdd:PRK04863 448 QAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQ 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2320 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEEtqgfqrtLEAERQRQLEMSAEAERLKLRVAE-MS 2398
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAA 600
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 2399 RAQA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLREAIAELEREKEKLQQ 2469
Cdd:PRK04863 601 RAPAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1797-2065 |
1.65e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 54.07 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1797 EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAErvLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAE 1876
Cdd:COG2268 209 DALGRRRIAQVLQDAEIAENEAEKETEIAIAEANRDAKLVE--LEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAETR 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1877 DEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERqkglVEDTLRQRRQVEEE------ILALKASFEKAAAGKAELE 1950
Cdd:COG2268 287 REAEQAEILAEQAIQEEKAQAEQEVQHAKALEAREMR----VGLIERQKETELEPqersyfINAAQRQAQEEAKAAANIA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1951 LELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVeEARRLR 2030
Cdd:COG2268 363 EAIGAQAEAAVETARETEEAERAEQAALVAAAEAAEQEQVEIAVRAEAAKAEAEAQAAEIKAEAEAIREKGKA-EAEAKR 441
|
250 260 270
....*....|....*....|....*....|....*
gi 530389149 2031 ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2065
Cdd:COG2268 442 ALAEAIQVLGDAAAAELFKALVQALPEVAEEAAQP 476
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1342-2249 |
1.73e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1342 ISETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreAKELQQRMQEEVVRREEAAVDaqqqkr 1421
Cdd:TIGR00606 178 IFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQIT--SKEAQLESSREIVKSYENELD------ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1422 siqeelqqlrqsseaEIQAKARQAEAAERSRLRIEEEIRvvrlQLEATERQRGGAEGELQALraRAEEAEAQKRQAQEEA 1501
Cdd:TIGR00606 249 ---------------PLKNRLKEIEHNLSKIMKLDNEIK----ALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLY 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1502 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER-ARQVQVALETAQRSAE 1580
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIqSLATRLELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1581 AELQSKRASFAEKtaqleRSLQEEHVAVAQLREeaerraqqqaeaerareeaerelerwQLKANEALRLRlQAEEVAQQK 1660
Cdd:TIGR00606 388 SERQIKNFHTLVI-----ERQEDEAKTAAQLCA--------------------------DLQSKERLKQE-QADEIRDEK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1661 SLAQAEAEKqkeeaerearrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAE---------TEQGE 1731
Cdd:TIGR00606 436 KGLGRTIEL-------------KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERElskaeknslTETLK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1732 QQRQLLEEELARLQREAAAATQKRQELEAElAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL 1811
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1812 RALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEI----ALKEKEAENERLRRLAEDEAFQRRRLE 1886
Cdd:TIGR00606 580 HSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEKSSKQRAMLA 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1887 EQAAQHKADIEER---------LAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKaaagKAELELELGRIR 1957
Cdd:TIGR00606 660 GATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK----RRDEMLGLAPGR 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1958 SNAEDtLRSKEQAELEAARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2036
Cdd:TIGR00606 736 QSIID-LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2037 SaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2115
Cdd:TIGR00606 815 L-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2116 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEK--------HKKFAEQTLRQKA 2187
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLK 973
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530389149 2188 QVEQELTTLRLQLEETDHQKNLLDEELqRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2249
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDM-RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1697-1854 |
1.79e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 54.25 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1697 QELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqrEAAAATQKRQELEAELAKVRAemevllAS 1775
Cdd:PTZ00491 647 DSLQKSVQLAiEITTKSQEAAARHQAELLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES------SG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1776 KARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLK 1854
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI-EATKFE 791
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3931-3968 |
2.17e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.17e-06
10 20 30
....*....|....*....|....*....|....*...
gi 530389149 3931 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3968
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
2193-2463 |
2.44e-06 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 53.49 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2193 LTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALilrdKDNTQRFLQ 2272
Cdd:COG4372 62 LFLLNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAA----RQNLAKAQQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2273 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVqeatRLKAEAELLQQQKELAQEQARRLQ 2352
Cdd:COG4372 138 ELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVL----DLKLRSAQIEQEAQNLATRANAAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2353 E------DKEQMAQQLAEETQgfQRTLEAErQRQLEMSAEAERLKLRVAEMSR---AQARAEEDAQRFRKQAEEigeklh 2423
Cdd:COG4372 214 ArteelaRRAAAAQQTAQAIQ--QRDAQIS-QKAQQIAARAEQIRERERQLQRletAQARLEQEVAQLEAYYQA------ 284
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530389149 2424 RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELERE 2463
Cdd:COG4372 285 YVRLRQQAAATQRGQVLAGAAQRVAQAQAQAQAQAQLLSS 324
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1685-1983 |
2.94e-06 |
|
Caldesmon;
Pssm-ID: 426572 [Multi-domain] Cd Length: 490 Bit Score: 53.33 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1685 EEQAVRQREL-AEQELEKQRQLAEGTAQQR--------LAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1755
Cdd:pfam02029 3 EEEAARERRRrAREERRRQKESEEPSSQEDsqpevnaqEEAEEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1756 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKsKQRLEAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1835
Cdd:pfam02029 83 LERQKELDPTITDEQASKPRSTENTPEEKNNTEE-EEKSSTRKER-YEIEEREVSEKSYEKDDKKAVPKEEEEEEDAKTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1836 AERVLAEKlaaigEATRLKTEAEIALKEKEAE--NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELER 1913
Cdd:pfam02029 161 EEEEEEEE-----EKKVSKKKKEKLKDEYTSKvfLDQKKGHPEQKSQNGALEEVTSMTVKLKRTERTFSQKSLVAEDEEE 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 1914 QKGLVE-----DTLRQRRQvEEEILALKASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAARQRQLAAE 1983
Cdd:pfam02029 236 GAAFLEaeqklEELRRRRQ-EKESQEFEKLRQKQQEAELELE-ELKKKREERRKILEEEEQRRKQEEAERKAREE 308
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1682-2065 |
3.15e-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: 411407 [Multi-domain] Cd Length: 684 Bit Score: 53.47 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1682 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1754
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1755 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1829
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1830 ARQRAEAERvlaeklaaiGEATRLKteaEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL------ 1903
Cdd:NF033838 209 AKAKVESKK---------AEATRLE---KIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLgepatp 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1904 ------RKASDSELERQKgLVEDTLRQRRQVEEEILALKASFEKAAAGKAE------------LELELgrirsnAEDTLR 1965
Cdd:NF033838 277 dkkendAKSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEI------AESDVK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1966 SKEqAELEAARQRQLAAEEERRRREAEERVQKSLAAE---EEAARQRKAALEEVERlkaKVEEARRLRER-AEQ-ESARQ 2040
Cdd:NF033838 350 VKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKR---KAAEEDKVKEKpAEQpQPAPA 425
|
410 420
....*....|....*....|....*.
gi 530389149 2041 LQLAQEAAQKRLQAEE-KAHAFAVQQ 2065
Cdd:NF033838 426 PQPEKPAPKPEKPAEQpKAEKPADQQ 451
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1721-2608 |
3.34e-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: 53.82 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1721 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1798
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1799 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdE 1878
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1879 AFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQkglvedtlrQRRQVEEeilalkasfeKAAAGKAELELELGRIRS 1958
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1959 NAEdtLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2038
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2039 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL-RGEAEAARRAAEEAEEARVQAEREAAQSRRQVE 2117
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2118 EAERLKQSAEEQAQARAQAQAAAEKlRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR 2197
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2198 LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELsklkarieaenralilrdkdntQRFLQEEAEK 2277
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------------------QDLTEKLSEA 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2278 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlkekmqavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQ 2357
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA-----------LKLTALHALQLTLTQERV--REHALSIRVLPKE 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2358 MAQQlaeetqgfqrtleaerqrqlemsaeaerlklrvaemsraQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2437
Cdd:TIGR00618 674 LLAS---------------------------------------RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2438 TLEIQRQQSdhdAERLREAIAELEREKEKLQQEAKLLQlksEEMQTVQQEQLLQETQALQQSFLsekdsLLQRERFIEQE 2517
Cdd:TIGR00618 715 EYDREFNEI---ENASSSLGSDLAAREDALNQSLKELM---HQARTVLKARTEAHFNNNEEVTA-----ALQTGAELSHL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2518 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQ 2597
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
890
....*....|.
gi 530389149 2598 RLREQLQLLEE 2608
Cdd:TIGR00618 864 LTQEQAKIIQL 874
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1735-1947 |
3.35e-06 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 52.64 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1735 QLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvllasKARAEEESRSTSEKSKQRLEAEAGRfreLAEEAARLRAL 1814
Cdd:COG3064 58 GAVVQQYGRIQSQQSSAKKGEQQRKKKEEQVAEELK-----PKQAAEQERLKQLEKERLKAQEQQK---QAEEAEKQAQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1815 aeEAKRQRQLAEEDAARQRAEAErvlAEKLAAIGEATRLKTEAE---IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ 1891
Cdd:COG3064 130 --EQKQQEEQARKAAAEQKKKAE---AAKAKAAAEAAKLKAAAEakkKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAA 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1892 HKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKA 1947
Cdd:COG3064 205 EKAKAEAEAKAKAEKKAEAAAEEKAAAEKKKAAAKAKADKAAAAAKAAERKAAAAA 260
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1488-1860 |
3.40e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 434873 [Multi-domain] Cd Length: 521 Bit Score: 53.03 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1488 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1567
Cdd:pfam15709 162 QETPASISHERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1568 VQVALETA----QRSAEAELQSKRASFAEKTAQLERSLQeeHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1643
Cdd:pfam15709 242 LEVAAELSgpdvINSKETEDASERGAFSSDSVVEDPWLS--SKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDP 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 NEALRLRLQAEEVAQQKslaqaeaEKQKEEAEREARRRGKAEEQAvRQRELAEQELEKQRQLAEG--TAQQRLAAEqelI 1721
Cdd:pfam15709 320 SKALLEKREQEKASRDR-------LRAERAEMRRLEVERKRREQE-EQRRLQQEQLERAEKMREEleLEQQRRFEE---I 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1722 RLRAETEQGEQQRQLLEEELARLQREAAA--ATQKRQELEAELAKvraemevlLASKARAEEESRSTSEKSKQRLEAEag 1799
Cdd:pfam15709 389 RLRKQRLEEERQRQEEEERKQRLQLQAAQerARQQQEEFRRKLQE--------LQRKKQQEEAERAEAEKQRQKELEM-- 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 1800 rfrELAEEAARLRALAEEAK----RQRQLAEEdAARQRAEAERVLAEKLAAIGEATRLKTEAEIA 1860
Cdd:pfam15709 459 ---QLAEEQKRLMEMAEEERleyqRQKQEAEE-KARLEAEERRQKEEEAARLALEEAMKQAQEQA 519
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
2187-2483 |
3.56e-06 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226883 [Multi-domain] Cd Length: 570 Bit Score: 53.15 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2187 AQVEQELTTLRLQLEE-----TDHQKNLLDEeLQRLKAEAteaarqRSQVEEELFSVRVQME-ELSKLKARIEAENRALI 2260
Cdd:COG4477 200 EEAEEHMIALRSIMERipsllAELQTELPGQ-LQDLKAGY------RDMKEEGYHLEHVNIDsRLERLKEQLVENSELLT 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2261 LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQEATRLkAEAELLQQQ 2340
Cdd:COG4477 273 QLELDEAEEELGLIQEKIESLYDLLEREVEAKNVVEENLPILPDYLEKAKENNEH-LKEEIERVKESYRL-AETELGSVR 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2341 KelAQEQARRLQEDKEQMAQQLAEETQGF---QRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2417
Cdd:COG4477 351 K--FEKELKELESVLDEILENIEAQEVAYselQDNLEEIEKALTDIEDEQEKVQEHLTSLRKDELEARENLERLKSKLHE 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 2418 IGEKLHRTELAtqekvTLVQTLEIQRQQSDHdaeRLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2483
Cdd:COG4477 429 IKRYMEKSNLP-----GLPETFLSLFFTAGH---EIQDLMKELSEVPINMEAVSALVDIATEDMNT 486
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
971-1510 |
3.79e-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: 53.43 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 971 QQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIA-EQQKAQAEVEGLGKGVARLS 1049
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1050 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRGTQGAEEVLRAHEEQLKEAQAVpaTLPE 1129
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1130 LEATKASLKKLRAQAEAQQPTFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1200
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1201 DVRQRELEQLGRQLRYYRESADPLGAWLQDARR---RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfa 1277
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1278 kQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAE 1357
Cdd:TIGR00618 643 -LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1358 QQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAEREAKELQQRMQEEVV------RREEAAVDAQQQKRSIQEELQQL 1430
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAalqtgaELSHLAAEIQFFNRLREEDTHLL 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1431 RQsSEAEIQAKARQAEAAersRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1510
Cdd:TIGR00618 802 KT-LEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2808-2844 |
3.84e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.84e-06
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 2808 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 2844
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3399-3431 |
4.08e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 46.18 E-value: 4.08e-06
10 20 30
....*....|....*....|....*....|...
gi 530389149 3399 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 3431
Cdd:pfam00681 7 ATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1411-1610 |
4.75e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.16 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1411 EAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvRLQLEATERQrggaeGELQALRARAEEA 1490
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ----RAAAEKAAKQ-----AEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1491 EAQKRQAQEEAErlrrqvqdesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL---RQAEVERARQ 1567
Cdd:TIGR02794 120 QAEEAKAKQAAE-----------AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530389149 1568 VQValETAQRSAEAElQSKRASFAEKTAQLERSLQEEHVAVAQ 1610
Cdd:TIGR02794 189 AKA--EEAKAKAEAA-KAKAAAEAAAKAEAEAAAAAAAEAERK 228
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3933-3971 |
4.92e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 45.79 E-value: 4.92e-06
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3933 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3971
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1330-2063 |
5.08e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.83 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1330 ELTTLTSQYIKFIS---ETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQAEREA---KELQQRMQ 1403
Cdd:pfam07111 56 EGSQALSQQAELISrqlQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1404 EEVVRREeaavdAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSrlrieeeirvvrlqLEATERQRGGAEGELQal 1483
Cdd:pfam07111 135 EEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQLA-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1484 raraeeaeaqkrQAQEEAERLRRQVQdESQRKRQAEVELASRVKaeaeaareKQRALQALEELRLQAEEAERRLRQAEVE 1563
Cdd:pfam07111 194 ------------EAQKEAELLRKQLS-KTQEELEAQVTLVESLR--------KYVGEQVPPEVHSQTWELERQELLDTMQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1564 RARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQLKA 1643
Cdd:pfam07111 253 HLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSL-----------------LNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1644 NeALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREarrrGKAEEQAVRQRELaeqelekqrqlaegtaqQRLAAEQELIRL 1723
Cdd:pfam07111 316 F-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVT----SQSQEQAILQRAL-----------------QDKAAEVEVERM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1724 RAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSekskQRLEAEAGRFRE 1803
Cdd:pfam07111 374 SAKGLQMELSRA--QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS----NRLSYAVRKVHT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1804 LAEEAARLRALAEeaKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 1883
Cdd:pfam07111 448 IKGLMARKVALAQ--LRQESCPPPPPAPPVDADLSLELEQLRE--ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1884 RLEEQAAQHKADIEERLAQLRKASDSELERQKGLVED--TLRQRRQVEEEILAlKASFEKAAagkaelELELgRIRSNAE 1961
Cdd:pfam07111 524 EVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEaaSLRQELTQQQEIYG-QALQEKVA------EVET-RLREQLS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1962 DTLRskeqaeleaarqrqlaaeeerRRREAEERVQK---SLAAEEEAARQRKAALEEVERLK--AKVEEARRLRERAEQ- 2035
Cdd:pfam07111 596 DTKR---------------------RLNEARREQAKavvSLRQIQHRATQEKERNQELRRLQdeARKEEGQRLARRVQEl 654
|
730 740
....*....|....*....|....*...
gi 530389149 2036 ESARQLQLAQEAAQKRLQAEEKAHAFAV 2063
Cdd:pfam07111 655 ERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1683-1977 |
5.16e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 380155 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRQE 1757
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1758 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1814
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1815 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 1894
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDES 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1895 DIEERlaqlRKASDSELERQKGLVEDtlrqrrqVEEEILALKASFEKAAAGKaelelelgrirsNAEDtLRSKEQAELEA 1974
Cdd:NF012221 1778 DKPNR----QGAAGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG-LTEQEQEALEG 1833
|
...
gi 530389149 1975 ARQ 1977
Cdd:NF012221 1834 ATN 1836
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; |
1339-1452 |
5.32e-06 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];
Pssm-ID: 223783 [Multi-domain] Cd Length: 161 Bit Score: 49.60 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1339 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAvdAQ 1417
Cdd:COG0711 32 LKALDERQAKIADDLAEAERLKEEAQALLAEYEQELEEaREQASEIIEQAKKEAEQIAEEIKAEAEEELERIKEAA--EA 109
|
90 100 110
....*....|....*....|....*....|....*
gi 530389149 1418 QQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSR 1452
Cdd:COG0711 110 EIEAEKERALEELRAEVAELAVAIAEKLLGKKVDE 144
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1715-1810 |
5.84e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.03 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1715 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1794
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 530389149 1795 EAEAGRFrELAEEAAR 1810
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1344-1504 |
6.09e-06 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 51.87 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERErlAEVEAALEKQRQLAEAHAQAKAQAERE--AKELQQRMQEEVVRREEAAVDAQQQKR 1421
Cdd:COG3064 115 EQQKQAEEAEKQAQLEQKQQEE--QARKAAAEQKKKAEAAKAKAAAEAAKLkaAAEAKKKAEEAAKAAEEAKAKAEAAAA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1422 SIqeelqqlrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1501
Cdd:COG3064 193 KK-----------KAEAEAKAAAEKAKAEAEAKAKAEKKAEAAAEEKAAAEKKKAAAKAKADKAAAAAKAAERKAAAAAL 261
|
...
gi 530389149 1502 ERL 1504
Cdd:COG3064 262 DDI 264
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
2111-2364 |
6.36e-06 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 52.33 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2111 QSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVE 2190
Cdd:COG4372 85 ALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2191 QELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRf 2270
Cdd:COG4372 165 AQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELARRAAAAQQTAQAIQQRDAQISQK- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2271 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2350
Cdd:COG4372 244 AQQIAARAEQIRERERQLQRLETAQARLEQEVAQ--LEAYYQAYVRLRQQAAATQRGQVLAGAAQRVAQAQAQAQAQAQL 321
|
250
....*....|....
gi 530389149 2351 LQEDKEQMAQQLAE 2364
Cdd:COG4372 322 LSSANRPAALRLRR 335
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2171-2608 |
6.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2171 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA------EATEAARQRSQVEEELFSVRVQMEE 2244
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2245 LSKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2322
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2323 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2397
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2398 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-EAKL 2473
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2474 LQLKSEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQqrqqqqmeqerqrl 2553
Cdd:PRK03918 542 KSLKKELEK--------------LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER-------------- 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 2554 VASMEEARRRQHE---AEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE 2608
Cdd:PRK03918 594 LKELEPFYNEYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
159-266 |
6.70e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 47.88 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 159 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 237
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPgLCPDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 530389149 238 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1383-1871 |
6.86e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1383 AHAQAKAQAEREAKELQQR------MQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERsrlr 1454
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAkaaktpAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDnfPKLSAELRQQLNNER---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1455 ieEEIRVVRLQLEAterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRrQVQDESQRKRQAEVElASRVKAEAEaar 1534
Cdd:PRK10929 93 --DEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAR-EISDSLSQLPQQQTE-ARRQLNEIE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1535 ekqRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSA--EAELQSKRASFAEK-TAQLERSLQeehvavaql 1611
Cdd:PRK10929 158 ---RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1612 reeaerraqqqaeaerareeaerelerwqlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgkaeeqavRQ 1691
Cdd:PRK10929 226 ----------------------------------ALRNQLNSQ-----------------------------------RQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1692 RElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQK-RQELEA------ELAK 1764
Cdd:PRK10929 237 RE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlreqsqWLGV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1765 VRAEMEVLLASKARAEEESRStsekskQRLEAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAE 1842
Cdd:PRK10929 315 SNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDA 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 530389149 1843 KLAA---------------IGEATRLK---TEAEIALKE-KEAENERL 1871
Cdd:PRK10929 384 QLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1344-1937 |
6.98e-06 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 52.54 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLaEQQRAEERERLAEV-------EAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDA 1416
Cdd:COG4717 243 ELWPRLQEWKQL-EQELTRRREELATFprdgvlrLEKREAHLQKTEAEIDALLVRLAELKDLASQLIPAKEAVLQALVRL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1417 QQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLrieEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1496
Cdd:COG4717 322 HQQLSEIKASAFELTET-LAGIEADLRDKEEAAGNGF---EAERVHDLRSLECMLRYQSSQRELKQTEAAYCKRLDEKRL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1497 AQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQ 1576
Cdd:COG4717 398 FEDEAEEEARQRLADDEEEVRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTAWQKQRFLREKQTAFERQKTEHTKIIAL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1577 RSAEAELQSKRASFAEKTAQL---ERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQA 1653
Cdd:COG4717 478 RLAGMLLVALSRLLTSLIFQIifaVAQIVFLSAEIKSSSRAVREEKAAVTDIPEELARLLITDELPELAVDLLVQSRIRQ 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1654 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEkqRQLAEGTAQQRLAAEQELIRLRAETEQGEQQ 1733
Cdd:COG4717 558 HWQQLRKALDQLEAAYEALEGRFAAAEAAMAEWQSEWEEALDELGLS--RELSPEQQLDILSTMKDLKKLMQKKAELTHQ 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1734 RQLLEEELARLQREAAAATqkrQELEAELAKVRAEMEV--LLASKARAEEESRSTSEKSKQRLEAEAGRFR-ELAEEAAR 1810
Cdd:COG4717 636 VARLREEQAAFEERVEGLL---AVLEAQFIDLSTLFCVqrLRVAAELQKEEARLALEGNIERTKELNDELRaELELHRKE 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1811 LRALAEEAKrqrqLAEEDAARQRAEAERVLAEKLAAIGEATRlKTEAEIALKEKEAENERLRRLAEDEAfqrRRLEEQAA 1890
Cdd:COG4717 713 ILDLFDCGT----ADTEDAFREAAREEQQLTQRESRLESLEA-QLEGVAAEAYELSASLDQRELKEEEL---ALLEEAID 784
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 530389149 1891 QHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKA 1937
Cdd:COG4717 785 ALDEEVEELHAQVAALSRQIAQLEGGGTVAELRQRRESLKEDLEEKA 831
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1344-1519 |
7.57e-06 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 51.87 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERERLAEVE----AALEKQRQLAEAHAQAKAQaEREAKELQQRMQEEVVRREEAAVDAQQQ 1419
Cdd:COG3064 80 QRKKKEEQVAEELKPKQAAEQERLKQLEkerlKAQEQQKQAEEAEKQAQLE-QKQQEEQARKAAAEQKKKAEAAKAKAAA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1420 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1499
Cdd:COG3064 159 EAAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKAEAEAKAKAEKKAEAAAEEKAAAEKKKAAA 238
|
170 180
....*....|....*....|.
gi 530389149 1500 EAERLR-RQVQDESQRKRQAE 1519
Cdd:COG3064 239 KAKADKaAAAAKAAERKAAAA 259
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1686-1977 |
7.76e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteristic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.61 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1686 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRQEL 1758
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1759 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1837
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1838 rvlaEKLAAIGEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SDSELERQ 1914
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1915 KGLVEDTLRQRRQVEEEILALKASFEKAAagkAELELELGRIRSNaedtlRSKEQAELEAARQ 1977
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQAN---RRLKEELQRERAE-----RALAQGALEIARE 399
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3099-3135 |
7.92e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 7.92e-06
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 3099 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 3135
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2252-2479 |
8.00e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 52.14 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2252 IEAENRALILRDKdNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavQEATRLK 2331
Cdd:COG2268 208 LDALGRRRIAQVL-QDAEIAENEAEKETEIAIAEANRDAKLVELEVEQQPAGKTAEQTREVKIILAETE----AEVAAWK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2332 AEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSA-EAERLKLRVAEMSRAQARAE-EDA 2408
Cdd:COG2268 283 AETRREAEQAEILAEQAIQEEKAQAEQEVQHAKaLEAREMRVGLIERQKETELEPqERSYFINAAQRQAQEEAKAAaNIA 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530389149 2409 QRFRKQAEEIGEKLHRTELA-TQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSE 2479
Cdd:COG2268 363 EAIGAQAEAAVETARETEEAeRAEQAALVAAAEAAEQEQVEIAVRAEAAKAEAEAQAAEIKAEAEAIREKGK 434
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
624-716 |
8.05e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 624 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 703
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 530389149 704 ALQTQWSWMLQLC 716
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3467-3503 |
8.91e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 8.91e-06
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 3467 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 3503
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1232-1447 |
1.01e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 51.76 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1232 RRRQEQIQAMPladSQAVREQLRQEQALLEEIERHGEKVE--ECQRFAKQYINAIKDYELQLV-------TYKAQLEPVA 1302
Cdd:COG2268 213 RRRIAQVLQDA---EIAENEAEKETEIAIAEANRDAKLVEleVEQQPAGKTAEQTREVKIILAeteaevaAWKAETRREA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1303 SPAKKPKVQSGSESVIQEYVDLRT-HYSELTTLTSQYIKFISET-LRRMEEEERLAEQQRAEERERLAEVEAAL------ 1374
Cdd:COG2268 290 EQAEILAEQAIQEEKAQAEQEVQHaKALEAREMRVGLIERQKETeLEPQERSYFINAAQRQAQEEAKAAANIAEaigaqa 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1375 ----EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEA 1447
Cdd:COG2268 370 eaavETARETEEAERAEQAALVAAAEAAEQEQVEIAVRAEAAKAEAEAQAAEIKAEAEAIREKGKAEAEAKRALAEA 446
|
|
| FimV |
COG3170 |
Tfp pilus assembly protein FimV [Cell motility, Extracellular structures]; |
1355-1581 |
1.03e-05 |
|
Tfp pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 225711 [Multi-domain] Cd Length: 755 Bit Score: 51.84 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1355 LAEQQRAEERERLAEVEA-----ALEKQRQLAEAHAQAKAQA----EREAKELQQRMQEEvvrreeaavdaQQQKRSIQE 1425
Cdd:COG3170 248 AAQILRESPQEALAEVKAqtaafAGEPSKADRVGKPVAKAPAkvakERALAELPARVAEL-----------QAQLNKAQH 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1426 ELQQLRQSSEAEIQAKARQAEAAERSRLRIEeeirvvrlQLEATERQRGGAEGELqaLRARAEEAEAQKRQAQEEAERLR 1505
Cdd:COG3170 317 ELAQKAAPLAAAQAALDAPAETATAPSAPAP--------QVSAESSPAQPGSYLL--AAPGDAPLGELAQAQSARERLAE 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1506 RQVQDESQRKRQAEVELASRVKAEAEA-AREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1581
Cdd:COG3170 387 ESVPAAEPRSRLAPVAAVEQPFAEVESpLSSLPAPLLALGLVALDGGWLVLRRAQQPPVETQGFQNRLLNRADTLLA 463
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1774-1973 |
1.09e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.35 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1774 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAIGEATRL 1853
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1854 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEIL 1933
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530389149 1934 ALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1973
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1019-1611 |
1.10e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1019 EPARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISL 1098
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1099 VIRGTQGAEEVLRAHEEQLKEAQAVPATLPELeatkaslkklrAQAEAQQPTFDALRDELRG-----AQEVGERLQQRhg 1173
Cdd:PRK10246 317 NTRLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1174 erdveveRWRERVAQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLQDARRRQEQIQAmplADSQA 1248
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1249 VREQLRQEQALLEEIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1301
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1302 ASPAKKPKVQSGSESVIQEYVDLRthySELTTLTSQYIKFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1381
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1382 EAHAQAKAQAEREAKELQQRMQEEVVRREEAAvdAQQQKRSIQEELQQLRQSSEAEIQAKARQ--AEAAERSRL--RIEE 1457
Cdd:PRK10246 596 DDIQPWLDAQEEHERQLRLLSQRHELQGQIAA--HNQQIIQYQQQIEQRQQQLLTALAGYALTlpQEDEEASWLatRQQE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1458 EIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DESQRKRQAEVE 1521
Cdd:PRK10246 674 AQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQAQ 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1522 LASRVKAEAEAAREKQRALQALEELRLQAEEAERRLrqaevERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1601
Cdd:PRK10246 754 FDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQ 828
|
650
....*....|
gi 530389149 1602 QEEHVAVAQL 1611
Cdd:PRK10246 829 QELAQLAQQL 838
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1457-2056 |
1.15e-05 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 51.77 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1457 EEIRVVRLQLEATERQRGGAEGEL---QALRARAEEAEAQKRQAQEEAERLRRQVQ--DESQRKRQAEVELASRVKAEAE 1531
Cdd:COG4717 188 EKLKQERNEIDEAEKEYATYHKLLesrRAEHARLAELRSELRADRDHIRALRDAVElwPRLQEWKQLEQELTRRREELAT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1532 AAREKQRALQALEElRLQAEEAERRLRQAEVERARQVQVALETAQRSA-------EAELQSKRASFAEKTAQL---ERSL 1601
Cdd:COG4717 268 FPRDGVLRLEKREA-HLQKTEAEIDALLVRLAELKDLASQLIPAKEAVlqalvrlHQQLSEIKASAFELTETLagiEADL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1602 QEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1681
Cdd:COG4717 347 RDKEEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEAAYCKRLDEKRLFEDEAEEEARQRLADDEEEVRAGDEAREE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1682 GKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQgEQQRQLLEEELARLQREAAAATQKRQELEAE 1761
Cdd:COG4717 427 KIAANSQVIDKEEVCNLYDRRDTAWQ---KQRFLREKQTAFERQKTEH-TKIIALRLAGMLLVALSRLLTSLIFQIIFAV 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1762 LAKVRAEMEVLLASKARAEEESRSTS-EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1840
Cdd:COG4717 503 AQIVFLSAEIKSSSRAVREEKAAVTDiPEELARLLITDELPELAVDLLVQSRIRQHWQQLRKALDQLEAAYEALEGRFAA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1841 AEKLAAIGEATRLKTEAEIALKEKEAENERLrrlaedEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVED 1920
Cdd:COG4717 583 AEAAMAEWQSEWEEALDELGLSRELSPEQQL------DILSTMKDLKKLMQKKAELTHQVARLREEQAAFEERVEGLLAV 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1921 TLRQRRQVEEEILALKAsfekaaagKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEErvqkslA 2000
Cdd:COG4717 657 LEAQFIDLSTLFCVQRL--------RVAAELQKEEARLALEGNIERTKELNDELRAELELHRKEILDLFDCGT------A 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 2001 AEEEAARQrkaALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2056
Cdd:COG4717 723 DTEDAFRE---AAREEQQLTQRESRLESLEAQLEGVAAEAYELSASLDQRELKEEE 775
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1803-2121 |
1.28e-05 |
|
Caldesmon;
Pssm-ID: 426572 [Multi-domain] Cd Length: 490 Bit Score: 51.41 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1803 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLKTEAEIALKEKEAENERLRRLAEDeafQR 1882
Cdd:pfam02029 1 EDEEEAARERRRRAREERRRQKESEEPSSQEDSQPEVNAQEEAEE-EDSELKPSGQGGLDEEEAFLDRTAKREER---RQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1883 RRLEEQAAQHK---ADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILalkasfEKAAAGKAELELELGRIRSN 1959
Cdd:pfam02029 77 KRLQEALERQKeldPTITDEQASKPRSTENTPEEKNNTEEEEKSSTRKERYEIE------EREVSEKSYEKDDKKAVPKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1960 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR--KAALEEVER-LKAKVEEARRLRERAEQE 2036
Cdd:pfam02029 151 EEEEEDAKTEEEEEEEEEEKKVSKKKKEKLKDEYTSKVFLDQKKGHPEQKsqNGALEEVTSmTVKLKRTERTFSQKSLVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2037 SARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAE-----REAAQ 2111
Cdd:pfam02029 231 EDEEEGAAFLEAEQKLEELRRRRQEKESQEFEKLRQKQQEAELELEELKKKREERRKILEEEEQRRKQEEaerkaREEEE 310
|
330
....*....|
gi 530389149 2112 SRRQVEEAER 2121
Cdd:pfam02029 311 KRRMKEEIER 320
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1757-2414 |
1.37e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 51.64 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1757 ELEAELAKVRAEMEVLLAskaraEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1836
Cdd:pfam15921 246 QLEALKSESQNKIELLLQ-----QHQDRIEQLISEHEVEITG-----LTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1837 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASDSELERQKG 1916
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1917 LVEDTLRQRRQVEEEIlalkasfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAARQrqlaaeeerrrrEAEERVQ 1996
Cdd:pfam15921 393 LSLEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1997 KSLAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQL-AQEAAQKRLQAEEKAHAFAVQQKEQELQQTL 2074
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLeSSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2075 QQEQSVLDQLRgeaeaaRRAAEEAEEARVQAEREAAqsRRQVEEAERLKQsaeeqaqaraqaqaaaeklrkeaeqeaarr 2154
Cdd:pfam15921 524 SRVDLKLQELQ------HLKNEGDHLRNVQTECEAL--KLQMAEKDKVIE------------------------------ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2155 aqaeqaALRQKQAADAEM-EKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQV-- 2231
Cdd:pfam15921 566 ------ILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvn 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2232 --EEELFSVRVQMEELSKLKARIE---------AENRALILRDKDNTQRFLQEEAEKMK------QVAEEAARLSVAAQE 2294
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKtsrnelnslSEDYEVLKRNFRNKSEEMETTTNKLKmqlksaQSELEQTRNTLKSME 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2295 AARLRQLAEEDLAQQRALAEK----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaEETQGF 2369
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKRgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQ 798
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 530389149 2370 QRTLeaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2414
Cdd:pfam15921 799 ERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1350-1604 |
1.45e-05 |
|
Caldesmon;
Pssm-ID: 426572 [Multi-domain] Cd Length: 490 Bit Score: 51.02 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1350 EEEERLAEQQRAEERERLAEVEAALEKQRQL--------------AEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVD 1415
Cdd:pfam02029 59 DEEEAFLDRTAKREERRQKRLQEALERQKELdptitdeqaskprsTENTPEEKNNTEEEEKSSTRKERYEIEEREVSEKS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1416 AQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAE----RSRLRIEEEIRVVRLQ---LEATERQRGGAEGE--------- 1479
Cdd:pfam02029 139 YEKDDKKAVPKEEEEEEDAKTEEEEEEEEEEKKVskkkKEKLKDEYTSKVFLDQkkgHPEQKSQNGALEEVtsmtvklkr 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1480 ------LQALRARAEEAEAQKRQAQEEAERLRRQVQD-ES-------QRKRQAEVELasrvkAEAEAAREKQRALQALEE 1545
Cdd:pfam02029 219 tertfsQKSLVAEDEEEGAAFLEAEQKLEELRRRRQEkESqefeklrQKQQEAELEL-----EELKKKREERRKILEEEE 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1546 LRLQAEEAERRLRQAEVERarqvQVALETAQRSAEAelqskrasfAEKTAQLERSLQEE 1604
Cdd:pfam02029 294 QRRKQEEAERKAREEEEKR----RMKEEIERRRAEA---------AEKRQKMEDTSSAE 339
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1090-1558 |
1.45e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 51.27 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1090 LEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraQAEAQQpTFDALRDELRGAQEVGERLQ 1169
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKNLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRQE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1170 QRHGERDVEVERWRERVAQLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLQDARRRQEQIqampl 1243
Cdd:pfam05557 125 LELSSTNSELEELQERLDLQKAKAQEAeqlRQNLEAQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1244 ADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQ 1311
Cdd:pfam05557 200 PELERELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEGYREELATLELEKEKLEQELKSweklaqdtglnlRSPE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1312 SGSESVIQEYVDLRTHYSELTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL---------- 1380
Cdd:pfam05557 280 DLSRRIEQLQQREITLKEENSSLTSS-ARQLEKAQRELEQELAQYLKNIEDLNKKLKRHKALVRRlQRRVllltkerdgm 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1381 ------------AEAHAQAKAQAEREAKELQQRMQeevVRREEAAVDAQQQKRSIQEELQQLrQSSEAEIQAKARQAEAA 1448
Cdd:pfam05557 359 railesydkeltPSNYSPQLLERIEEAEDMTQDMQ---AHNEEMEAQLSVAEEELGGYKQQA-TTLERELQALRQQESLA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1449 ERSRLRIE-----EEIRVVRLQLEATERQRGGAEGEL--QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVE 1521
Cdd:pfam05557 435 DPSYSKEEvdslrRKLETLEAERQRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRANDLEKLQAEIE 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 530389149 1522 LASRVKAEAEAAREKQRAL---------QALEELRLQAEEAERRLR 1558
Cdd:pfam05557 515 RLKRRLKKLEDDLEQVGSLpettstmnfKEVLELRKELESAELKNQ 560
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1683-1898 |
1.53e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.10 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ-------------LLEEEL 1741
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVikagarpdnsaviAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1742 ARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1821
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1822 RQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1898
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1786-2057 |
1.65e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 433539 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1786 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA-EIALKEK 1864
Cdd:pfam13868 21 NKERDAQIEEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKQYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1865 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfeKAAA 1944
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEDLRILEYLKEKAEREEEREA---ERRE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1945 GKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK-V 2023
Cdd:pfam13868 178 IKEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKWRQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270
....*....|....*....|....*....|....
gi 530389149 2024 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2057
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRREKRLE 290
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1683-1842 |
1.77e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 50.49 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEEQAVRQRE-LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLE---------EELARLQREAAAAT 1752
Cdd:COG4942 105 ALEVQEREQRRrLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAEridalkatlKQLAAVRAEIAAEQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1753 QKRQELEAELAKVRAEMEVLLaskaraeEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQ 1832
Cdd:COG4942 185 AELTTLLSEQRAQQAKLAQLL-------EERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAA 257
|
170
....*....|
gi 530389149 1833 RAEAERVLAE 1842
Cdd:COG4942 258 EAAAARARAA 267
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1110-1325 |
1.85e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 50.79 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1110 LRAHEEQLKEAQ-AVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1188
Cdd:COG4372 83 LRALRTELGTAQgEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1189 LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMP--LADSQAVREQLRQeqalleEIERH 1266
Cdd:COG4372 163 LEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTeeLARRAAAAQQTAQ------AIQQR 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1267 GEKVEECQRFAKQYINAIKDYELQLVTYKAQLepvaspAKKPKVQSGSESVIQEYVDLR 1325
Cdd:COG4372 237 DAQISQKAQQIAARAEQIRERERQLQRLETAQ------ARLEQEVAQLEAYYQAYVRLR 289
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1339-1551 |
1.88e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 50.49 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1339 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-------LAEAHAQAKAQAEREAKELQQRMQEEVVRREE 1411
Cdd:COG4942 89 LKKLRKQIADLNARLNALEVQEREQRRRLAEQLAALQRSGRnpppallVSPEDAQRSVRLAIYYGALNPARAERIDALKA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1412 AAVDAQQQKRSI---QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEaterQRGGAEGELQALRARAE 1488
Cdd:COG4942 169 TLKQLAAVRAEIaaeQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLE----ELRANESRLKNEIASAE 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1489 EAEAQKRQAQEEAERlrrqvqdESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAE 1551
Cdd:COG4942 245 AAAAKAREAAAAAEA-------AAARARAAEAKRTGETYKPTAPEKMLISSTGGFGALRGQLA 300
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1630-2120 |
1.89e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 50.88 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1630 EEAERELERWQLKANEAL-RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEg 1708
Cdd:pfam05557 37 SALARQLERESDRNQELQkRIRLLEKREAEAEEALREQAELNRLKKKNLEALNKKLNEKESQLADAREVISCLKNELSE- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1709 TAQQRLAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKar 1778
Cdd:pfam05557 116 LRRQIQRQELELSSTNSELEELQERLDLQKakaqeaeqlrQNLEAQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSK-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1779 AEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLA--AIGEATRL 1853
Cdd:pfam05557 194 SELARIPELERELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEGYREELATLELEKEKLEQELKSweKLAQDTGL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1854 KTEAEIALKEK--EAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASDSE---LERQKGLVEDTLRQRRQV 1928
Cdd:pfam05557 274 NLRSPEDLSRRieQLQQREITLKEENSSLTSSARQLEKAQ--RELEQELAQYLKNIEDLnkkLKRHKALVRRLQRRVLLL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1929 EEEILALKA---SFEKAAAGKAELELELGRIRSNAEDTLRSKEQ-AELEAARQRQLAAEEERRRREAEERVQKSLAAEEE 2004
Cdd:pfam05557 352 TKERDGMRAileSYDKELTPSNYSPQLLERIEEAEDMTQDMQAHnEEMEAQLSVAEEELGGYKQQATTLERELQALRQQE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2005 AARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQEAAQKR---LQAEEKAHAFAVQQKEQELQQTLQ 2075
Cdd:pfam05557 432 SLADPSYSKEEVDSLRRKLETLEaerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAEAYQQRANDLEKLQA 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 530389149 2076 QEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE 2120
Cdd:pfam05557 512 EIERLKRRLKKLEDDLEQVGSLPETTSTMNFKEVLELRKELESAE 556
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2163-2343 |
1.90e-05 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 50.33 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2163 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEElfsVRVQM 2242
Cdd:COG3064 81 RKKKEEQVAEELKPKQAAEQERLKQLEKERLKAQEQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKKKAEAA---KAKAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2243 EELSKLKARIEAENRA-LILRDKDNTQRFLQEEAEKMKQVAEEAARLSVA--AQEAARLRQLAEEDLAQQRALAEKMLKE 2319
Cdd:COG3064 158 AEAAKLKAAAEAKKKAeEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAkaEAEAKAKAEKKAEAAAEEKAAAEKKKAA 237
|
170 180
....*....|....*....|....
gi 530389149 2320 KMQAVQEATRLKAEAELLQQQKEL 2343
Cdd:COG3064 238 AKAKADKAAAAAKAAERKAAAAAL 261
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1342-1609 |
1.93e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 51.18 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1342 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaQAKAQAEREAKELQQRMQEEvvrREEAAVDAQQQKR 1421
Cdd:COG5281 344 VLGIGREDKQAALLAAKLAAEKLARVTAQGALNARLKLAQ----DDLTQAELNYAAADQAANQE---GALNAREDEAEVL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1422 SIQEELQQLRQSSEAEiqakARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1501
Cdd:COG5281 417 STQEERRDILKNLLAD----AEKRTARQEELNKALAKAKILQADKAAKAYQEDILQREAQSRGKTAAAERSQEQMTAALK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1502 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERarqvQVALETAQRSAEA 1581
Cdd:COG5281 493 ALLAFQQQIADLSGAKEKASDQKSLLWKAEEQYALLKEEAKQRQLQEQKALLEHKKETLEYTS----QLAELLDQQADRF 568
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 530389149 1582 EL--------------------QSKRASFAEKTAQLERSLQEEHVAVA 1609
Cdd:COG5281 569 ELsaqaagsqkergsdlyrealAQNAAALNKALNELAAYWSALDLLQG 616
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2004-2348 |
2.08e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2004 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2075
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2076 qeqsvLDQLRgEAEAARRAAEEAEEARVQAEREAAQSR--RQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQeaAr 2153
Cdd:pfam17380 362 -----LERIR-QEEIAMEISRMRELERLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE--A- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2154 raqaeqaalRQKQAADAEMEKhkkfaeqtlrqkaqvEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEE 2233
Cdd:pfam17380 433 ---------RQREVRRLEEER---------------AREMERVRLEEQERQQQ-------VERLRQQEEERKRKKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2234 ElfsvrvqmeelSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALA 2313
Cdd:pfam17380 482 E-----------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
330 340 350
....*....|....*....|....*....|....*....
gi 530389149 2314 EKMLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2348
Cdd:pfam17380 551 RRRIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1824-2055 |
2.13e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 50.41 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1824 LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEeQAAQHKADIEERLAQL 1903
Cdd:COG4372 64 LLNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELA-AARQNLAKAQQELARL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1904 RKASDSELERQKGLVEdtlrQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTlrskEQAELEAARQRQlaae 1983
Cdd:COG4372 143 TKQAQDLQTRLKTLAE----QRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQI----EQEAQNLATRAN---- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530389149 1984 eerrrreAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAqEAAQKRLQAE 2055
Cdd:COG4372 211 -------AAQARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRL-ETAQARLEQE 274
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1367-1461 |
2.14e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1367 LAEVEAALEKQRQLAEAHAQAKAQAEREAkelqQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR-QSSEAEIQAKARQA 1445
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 530389149 1446 EAAERSRLRI---EEEIRV 1461
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
2346-2470 |
2.26e-05 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 49.17 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2346 EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2425
Cdd:pfam00769 2 EEAEREKQELEERLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEMEAEEKEQL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530389149 2426 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQE 2470
Cdd:pfam00769 82 ERELREAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAKEK 126
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2171-2611 |
2.31e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2171 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEelfsVRVQMEELSKLKA 2250
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2251 RIEAENRALILRDKdNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqraLAEKMLKEKMQAVQEATRL 2330
Cdd:PRK03918 249 SLEGSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2331 KAEAELLQQQKELAQEQARRLQEDKEQMA--QQLAEETQGFQRTLEAERQRQLEMSAEAERLK-LRVAEMSRAQARAEED 2407
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKelEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2408 AQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---------SDHDAERLREAIAELER-EKEKLQQEAKLLQLK 2477
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRiEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2478 SEEMQTvqqeqllqetqalqQSFLSEKDSLLQRERFIEQEKA---KLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLV 2554
Cdd:PRK03918 480 KELREL--------------EKVLKKESELIKLKELAEQLKEleeKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 2555 ASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHR 2611
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1357-1484 |
2.37e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 49.50 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1357 EQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAKELQQRMQEEVVrreeaavdaQQQKRSIQEELQQLRQSSE 1435
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEaAEQERKLLEEQQRELEQKL---------EDQERSYEEHLRQLKEKME 247
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530389149 1436 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1484
Cdd:cd16269 248 EERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1344-1581 |
2.40e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAEREAKelqqrmqeevvrreeAAVDAQQ 1418
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAK---------------AAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1419 QKRSIQEELQQLRQSSEAEIQAKARqAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqalRARAEEAEAQKRQAQ 1498
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAK-AKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA------KAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1499 EEAERlrrqvQDESQRKRQAEVELASRVKAEAeAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1578
Cdd:PRK07735 151 EEVTE-----EEEETDKEKAKAKAAAAAKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
...
gi 530389149 1579 AEA 1581
Cdd:PRK07735 225 QGN 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1411-1611 |
2.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 50.11 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1411 EAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA 1490
Cdd:COG4942 31 FSAAADDKQLKQIQKEIAAL----EKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1491 EAQKRqaqEEAERLRRQVqDESQRKRqAEVELASRVKaeAEAAREKQRALQAL----EELRLQAEEAERRLRQ-----AE 1561
Cdd:COG4942 107 EVQER---EQRRRLAEQL-AALQRSG-RNPPPALLVS--PEDAQRSVRLAIYYgalnPARAERIDALKATLKQlaavrAE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530389149 1562 VERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1611
Cdd:COG4942 180 IAAEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEEL 229
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2696-2734 |
2.51e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 43.87 E-value: 2.51e-05
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 2696 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 2734
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1356-1517 |
2.55e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 50.67 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1356 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1435
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1436 AEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDESQRK 1515
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 530389149 1516 RQ 1517
Cdd:PRK12678 216 EE 217
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2165-2367 |
2.59e-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: 380155 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2165 KQAADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDHQknlldeelqrlkAEATEAARQRSQVEEELF 2236
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2237 SVRVqmeELSKLKARIEA----------------ENRALILRDK-----DNTQRFLQEEAEKMKQ--------VAEEAAR 2287
Cdd:NF012221 1617 AVTK---ELTTLAQGLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2288 LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQ 2367
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2287-2453 |
2.62e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2287 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2363
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2364 ------EETQGFQRTLEAERQRQLEMSAEAERLK-------LRVAEMSRAQAR----------AEEDAQRFRKQAEEIGE 2420
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKeillekveeeARHEAAVLIKEIEEEAK 183
|
170 180 190
....*....|....*....|....*....|....
gi 530389149 2421 klhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2453
Cdd:PRK12704 184 -----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
2223-2389 |
2.89e-05 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 48.78 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2223 EAARQRSQVEEELfsvrVQMEELSKL--KARIEAENRALILrdkdntqrflqeeAEKMKQVAEEAARLSVAAQEAarlrq 2300
Cdd:pfam00769 3 EAEREKQELEERL----KQYEEETRKaqEELEESEETAELL-------------EEKLRVAEEEAELLEQKAQEA----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2301 laEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2380
Cdd:pfam00769 61 --EEEKERLEESAEMEAEEKEQLERELREAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAKEKLLAASTSPSHHH 138
|
....*....
gi 530389149 2381 LEMSAEAER 2389
Cdd:pfam00769 139 SEESENEDD 147
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2186-2738 |
2.97e-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: 50.49 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2186 KAQVEQELTTLRLQLEETDHQKNLLDEELQRlkaEATEAARQRSQVEEELFSVRVQMEELSKLKAriEAENRALILRDKD 2265
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2266 NTQ-RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2340
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2341 ----KELAQEQARRLQEDKEQMaQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQAE 2416
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2417 EIGEKLHRTElatQEKVTLVQT-------LEIQ----RQQSDHDAERLREAIAELEREKEK---LQQEAKLLQLKSEEMq 2482
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQArekeihdLEIQltaiKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKEL- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2483 TVQQEQLLQETQALQQSFLSEKDsllQRERFIEQekakLEQLFQDEVakaqqlreeqqRQQQQMEQERQRLVASMEEARR 2562
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKK---QEERMLKQ----IENLEEKEM-----------NLRDELESVREEFIQKGDEVKC 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2563 RQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE--QHRAALAHSEEVTASQVAATKTLPNGRDaLDG 2640
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLE-LEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2641 PAAEAEPEHSFDGLRRKVSAQRLQEAGIL--------SAEELQRLAQ------GHTTVDELARREDVRH----YLQGRSS 2702
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLeevekakaIADEAVKLQKeidkrcQHKIAEMVALMEKHKHqydkIIEERDS 725
|
570 580 590
....*....|....*....|....*....|....*.
gi 530389149 2703 IAGLLLKATNEKLSVYAALQRQLLSPGTALILLEAQ 2738
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1348-1566 |
3.00e-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: 50.00 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1348 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1427
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1428 QQLRQSSEAEIQAKARQAeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1507
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1508 VQDESQRKRQaevELASRVKAEAEAAREKQR---------ALQALEELRLQAEEAERRLRQAEVERAR 1566
Cdd:pfam05262 333 VAEDLQKTKP---QVEAQPTSLNEDAIDSSNpvyglkvvdPITNLSELVLIDLKTEVRLRESAQQTIR 397
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1652-1828 |
3.18e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1652 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1727
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1728 EQGEQQRQLLEEELArlQREAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1802
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 530389149 1803 ELAEEAARLRALAEEAKRQRQLAEED 1828
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1236-1551 |
3.32e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1236 EQIQAMPLADSQAVREQLRQEQALLEEIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE 1315
Cdd:PRK10929 33 EQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1316 SVIQEYVDLRTHYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAer 1393
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1394 eakelqqrMQEEVVRReEAAVDaqqqkrsiQEELQQLRQSSEAEIqakAR-QAEAAERSRLRIEEEIRVVRLQLEaTERQ 1472
Cdd:PRK10929 178 --------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQALRNQLN-SQRQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1473 RggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL---ASRVKAEA----EAAREKQRALQALEE 1545
Cdd:PRK10929 237 R------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQALNT 304
|
....*.
gi 530389149 1546 LRLQAE 1551
Cdd:PRK10929 305 LREQSQ 310
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1688-2056 |
3.39e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1688 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--REAAAATQKRQELEA 1760
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1761 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvl 1840
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1841 aEKLAAIGEATRLKTEAEIALKEKEAenerlrrlaedeafqrrRLEEQAAQHKADIEERLaqlrkasdsELERQKGLVED 1920
Cdd:PRK04863 418 -QAVQALERAKQLCGLPDLTADNAED-----------------WLEEFQAKEQEATEELL---------SLEQKLSVAQA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1921 TLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR-QLAAEEERRRREAEERVQKSL 1999
Cdd:PRK04863 471 AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 2000 AAEEEAARQRKAALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQAEE 2056
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2268-2477 |
3.85e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 433539 [Multi-domain] Cd Length: 341 Bit Score: 49.14 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2268 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2347
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKQYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2348 ARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2427
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEDL---RILEYLKEKAEREEEREAERREIKEEKEREIARLR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530389149 2428 ATQEKvtlvqTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2477
Cdd:pfam13868 191 AQQEK-----AQDEKAERDELRAKLYQEEQERKWRQKEREEAEKKARQRQ 235
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1424-1542 |
3.86e-05 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 48.40 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1424 QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE---E 1500
Cdd:pfam00769 8 KQELEERLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEMEAEEKEQLERelrE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530389149 1501 AERLRRQVQDESQRKrQAEVElasRVKAEAEAAREKQRALQA 1542
Cdd:pfam00769 88 AQEEVARLEEESERK-EEEAE---RLQEELEEAREEEEEAKE 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
2273-2691 |
3.97e-05 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 50.10 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2273 EEAE-KMKQVAEEAARLSVAAQEaaRLRQLaeEDLAQQRALAEKMLKekmqavQEATRLKAEAELLQQQKELAQEQARRL 2351
Cdd:COG1196 175 EEAErKLERTEENLERLEDLLEE--LEKQL--EKLERQAEKAERYQE------LKAELRELELALLLAKLKELRKELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2352 QEDKEQMAQQLAEETQGFQrtleaerqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLhrtelatqe 2431
Cdd:COG1196 245 EEELSRLEEELEELQEELE-----------EAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEI--------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2432 kvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvqqeqllqetqalqqsflsekdSLLQRE 2511
Cdd:COG1196 305 -----SLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQ----------------------LLAELE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2512 RFIEQEKAKLEQLFQDEVAKAQQlreeqqrqqqqmeqerqrLVASMEEARRRQHEAEEGVRRKQEELQQleqqRRQQEEL 2591
Cdd:COG1196 358 EAKEELEEKLSALLEELEELFEA------------------LREELAELEAELAEIRNELEELKREIES----LEERLER 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2592 LAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDgpAAEAEPEHSFDGLRRKVSAQRLQEAGILSA 2671
Cdd:COG1196 416 LSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLK--ELERELAELQEELQRLEKELSSLEARLDRL 493
|
410 420
....*....|....*....|
gi 530389149 2672 EELQRLAQGHTTVDELARRE 2691
Cdd:COG1196 494 EAEQRASQGVRAVLEALESG 513
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
2283-2624 |
4.00e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2283 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2362
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2363 AEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQ 2437
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2438 TLEIQRQQSDHDAERLREAIAELEREKeKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQE 2517
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2518 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvasmEEARRRQHEAEEGVR-RKQEELQQLEQQRRQQEELLAEEN 2596
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL----EEEEESIELKQGKLTeEKEELEKQELKLLKDELELKKSED 472
|
330 340
....*....|....*....|....*...
gi 530389149 2597 QRLREQLQLLEEQHRAALAHSEEVTASQ 2624
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2771-2807 |
4.08e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.08e-05
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 2771 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 2807
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4141-4169 |
4.08e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.08e-05
10 20
....*....|....*....|....*....
gi 530389149 4141 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4169
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2276-2637 |
4.17e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2276 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQED 2354
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2355 keqmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2434
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2435 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqQEQLLQETQALQQSFLSEKDSLLQRERFI 2514
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-LEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2515 EQEKAKLEQL------FQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqqRRQQ 2588
Cdd:TIGR02169 395 EKLKREINELkreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-----------LAAD 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530389149 2589 EELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 2637
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2163-2469 |
4.30e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 50.02 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2163 RQKQAADAEMEKHKKFAeQTLRQKAQVEQELTTLRLQLEET-DHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQ 2241
Cdd:COG5281 294 RAGDTAAAAAAAAEAAA-AMDDRTARVKENMGTLETAWDALaDAAKKMWDAVLGIGREDKQAALLAAKLAAEKLARVTAQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2242 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARlsvaAQEAARLRQLAEEDLAQQRALAEKMLKEkm 2321
Cdd:COG5281 373 GALNARLKLAQDDLTQAELNYAAADQAANQEGALNAREDEAEVLST----QEERRDILKNLLADAEKRTARQEELNKA-- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2322 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEEtqgfQRTLEAERQRQLEMSA---EAERLKLRVAEMS 2398
Cdd:COG5281 447 LAKAKILQADKAAKAYQEDILQREAQSRGKTAAAERSQEQMTAA----LKALLAFQQQIADLSGakeKASDQKSLLWKAE 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530389149 2399 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ 2469
Cdd:COG5281 523 EQYALLKEEAKQRQLQEQKALLEHKKETLEYTS-----QLAELLDQQADRFELSAQAAGSQKERGSDLYRE 588
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1344-1432 |
4.39e-05 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 48.40 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQ---QRMQEEVVRREEAAVDAQQQK 1420
Cdd:pfam00769 34 ETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEMEAEEKEQLERELREAQeevARLEEESERKEEEAERLQEEL 113
|
90
....*....|..
gi 530389149 1421 RSIQEELQQLRQ 1432
Cdd:pfam00769 114 EEAREEEEEAKE 125
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1249-1522 |
4.44e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 49.64 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1249 VREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspAKKPKVQSGSESVIQEYVDLRThy 1328
Cdd:COG4372 79 IRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAAR-----QNLAKAQQELARLTKQAQDLQT-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1329 sELTTLTSQYIKFISETlrrmeeeerlaeQQRAEERERLAEVEAALEKQRQLAEAHAqakAQAEREAKELQQRMQ----- 1403
Cdd:COG4372 152 -RLKTLAEQRRQLEAQA------------QSLQASQKQLQASATQLKSQVLDLKLRS---AQIEQEAQNLATRANaaqar 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1404 -EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAege 1479
Cdd:COG4372 216 tEELARRAAAAQQTAQAIQQRDAQISQKAQQIAAraeQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQA--- 292
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 530389149 1480 LQALRARAEEAEAQkRQAQEEAERlRRQVQDESQRKRQAEVEL 1522
Cdd:COG4372 293 AATQRGQVLAGAAQ-RVAQAQAQA-QAQAQLLSSANRPAALRL 333
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1228-1488 |
4.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 49.34 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1228 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQ-------------YINA-IKDYELQLVT 1293
Cdd:COG4942 33 AAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIEtaddlkklrkqiaDLNArLNALEVQERE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1294 YKAQLEPVASPAKK-----PKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLA 1368
Cdd:COG4942 113 QRRRLAEQLAALQRsgrnpPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLLS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1369 EVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrreeaavdAQQQKRSIQEELQQLRQsSEAEIQAKARQAEAA 1448
Cdd:COG4942 193 EQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEE-----------LRANESRLKNEIASAEA-AAAKAREAAAAAEAA 260
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530389149 1449 ERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1488
Cdd:COG4942 261 AARARAAEAKRTGETYKPTAPEKMLISSTGGFGALRGQLA 300
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1232-1564 |
4.69e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 49.50 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1232 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGE---KVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAspAKKP 1308
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesRVAELKEELRQSREKVEELEEKYKELSRSGEELA--EEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1309 ---KVQSGSESVIQEYVDlrthysELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERER---LAEVEAALEKQRQLAE 1382
Cdd:pfam07888 119 allAQRAESEARIRELEE------DIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERkqlQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1383 AHAQAK-AQAEREAKELQqrMQEEVVRREEAAVDAQQQKRSIQEELQQLR------QSSEAEIQAKARQAEAAERSRLRI 1455
Cdd:pfam07888 193 EFQELRnSLAQRDTQVLQ--LQDTITTLTQKLTTAHRKEAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1456 EEEIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAR 1534
Cdd:pfam07888 271 QAELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR 350
|
330 340 350
....*....|....*....|....*....|
gi 530389149 1535 EKQRALQALEELRLQAEEAERRLRQAEVER 1564
Cdd:pfam07888 351 EKDCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1784-1950 |
4.72e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1784 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1862
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1863 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQR--RQVEEEILALKASFE 1940
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 530389149 1941 KAAAGKAELE 1950
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1491-1825 |
5.28e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 48.95 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1491 EAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQV 1570
Cdd:COG4942 37 DKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQRRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1571 ---ALETAQRSAEAE-----LQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeaerareeaerelerwqlk 1642
Cdd:COG4942 117 laeQLAALQRSGRNPppallVSPEDAQRSVRLAIYYGALNPA-------------------------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1643 anealRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkaeeQAVRQRELAEQElEKQRQLAEGTAQQRlaAEQELIR 1722
Cdd:COG4942 159 -----RAERIDALKATLKQL------------------------AAVRAEIAAEQA-ELTTLLSEQRAQQA--KLAQLLE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1723 LRAETEQG-EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvllasKARAEEESRSTSEKSKqrleaEAGRF 1801
Cdd:COG4942 207 ERKKTLAQlNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAA-----AAEAAAARARAAEAKR-----TGETY 276
|
330 340
....*....|....*....|....
gi 530389149 1802 RELAEEAARLRALAEEAKRQRQLA 1825
Cdd:COG4942 277 KPTAPEKMLISSTGGFGALRGQLA 300
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2243-2370 |
5.87e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 48.34 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2243 EELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQLAEEDLAQQRALAE--KMLKEK 2320
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEK 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 530389149 2321 MQavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQ 2370
Cdd:cd16269 246 ME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1534-1844 |
6.12e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 433539 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1534 REKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASfAEKTAQLERSLQEEHVAVAQLRE 1613
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKQYRQELEEQIEERE-QKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1614 EAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE 1693
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEDLRILEYLKEKAEREEEREAERREIKEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1694 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAatQKRQELEAELAKVRAEMEVLL 1773
Cdd:pfam13868 190 RAQQEKAQDEKAERDELRAKLYQEEQERKWRQKEREEAEKKARQRQELQQAREEQIE--LKERRLAEEAEREEEEFERML 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530389149 1774 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKL 1844
Cdd:pfam13868 268 RKQAEDEEIEQEEAEKRREKRLEHRRELEKQIEERERQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1108-1514 |
6.20e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 49.50 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1108 EVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRgAQEVGERLQQRHGERDVEVERWRERVA 1187
Cdd:COG3096 294 ELYTSRQQLAAEQYRHVDMSRELAELNGAEGDLEADYQAASDHLNLVQTALR-QQEKIERYQADLEELTIRLEEQNEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1188 QLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADplgAWLQDARRRQEQIQAMPLADSQAVREQLRQE--QALLEEIER 1265
Cdd:COG3096 373 EANERQEENEARAEAAELEVDELKSQLADYQQALD---VQQTRAIQYQQAIAALERAKELCHLPDLTADsaEEWLETFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1266 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSqyikfiset 1345
Cdd:COG3096 450 KEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVARELLREGPDQRHLAEQVQPLRM--------- 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1346 lRRMEEEERLAEQQRAEererlaeveaalekqRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI-- 1423
Cdd:COG3096 521 -RLSELEQRLRQQQSAE---------------RLLADFCKRQGKNLDAEELEALHQELEALIESLSDSVSNAREQRMAlr 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1424 --QEELQQLRQSSEAE----IQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelqALRARAEEAEAQKRQA 1497
Cdd:COG3096 585 qeQEQLQSRIQSLMQRapvwLAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLERER--------EATVERDELGARKNAL 656
|
410
....*....|....*..
gi 530389149 1498 QEEAERLRRQVQDESQR 1514
Cdd:COG3096 657 DEEIERLSQPGGSEDQR 673
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1488-1567 |
6.55e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 49.56 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1488 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL----ASRVKAE--AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1560
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqQELVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 530389149 1561 EVERARQ 1567
Cdd:PRK11448 218 RKEITDQ 224
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
41-145 |
6.58e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 45.34 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 41 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHR 118
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAK 84
|
90 100
....*....|....*....|....*..
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1351-2059 |
6.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1351 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1426
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1427 LQQLR-QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ-----LEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1500
Cdd:PRK04863 378 QEENEaRAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1501 AERLRRQVQDESQRKRQAEV--ELASRVKAEAEAAREKQRALQALEELRLQAEEAER----RLRQAEVERARQVQVALET 1574
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQayQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1575 AQRSAEaelqsKRASFAEKTAQLERSLQEEHVAvaqlreeaerrAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1654
Cdd:PRK04863 538 LLAEFC-----KRLGKNLDDEDELEQLQEELEA-----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1655 EVAQQKslaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRAETEqgEQQR 1734
Cdd:PRK04863 602 APAWLA-----------------------AQDALARLREQSGEEFEDSQDV-TEYMQQLLERERELTVERDELA--ARKQ 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1735 QLLEE----------ELARLQR------------------------------------------EAAAATQKRQELEAEL 1762
Cdd:PRK04863 656 ALDEEierlsqpggsEDPRLNAlaerfggvllseiyddvsledapyfsalygparhaivvpdlsDAAEQLAGLEDCPEDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1763 AKVRAEMEVLLASKARAEEESRSTSEKSKQRlEAEAGRFRE--LAEEAARlRALAEEAKRQRQLAEEDAARQRAE----- 1835
Cdd:PRK04863 736 YLIEGDPDSFDDSVFSVEELEKAVVVKIADR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDvqklq 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1836 -----AERVLAEKLA---------AIGEATRLKTEAEIALKEKEAENERLR--------------------RLAEDEAFQ 1881
Cdd:PRK04863 814 rlhqaFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHESQEQQQRsqleqakeglsalnrllprlNLLADETLA 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1882 RRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGRIR---- 1957
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQRRahfs 972
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1958 -SNAEDTLrSKEQAELEAARQRQLAAEEERRRREAE-----------ERVQKSLAAEEEAARQ-RKAALEEVE----RLK 2020
Cdd:PRK04863 973 yEDAAEML-AKNSDLNEKLRQRLEQAEQERTRAREQlrqaqaqlaqyNQVLASLKSSYDAKRQmLQELKQELQdlgvPAD 1051
|
810 820 830
....*....|....*....|....*....|....*....
gi 530389149 2021 AKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2059
Cdd:PRK04863 1052 SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1648-1830 |
7.15e-05 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 48.41 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1648 RLRLQAEEVaQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlaAEQELIRLRAET 1727
Cdd:COG3064 84 KEEQVAEEL-KPKQAAEQERLKQLEKERLKAQEQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKKK--AEAAKAKAAAEA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1728 EQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEvLLASKARAEEESRSTSEKSKQRL-EAEAGRFRELAE 1806
Cdd:COG3064 161 AKLKAAAE--AKKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAK-AAAEKAKAEAEAKAKAEKKAEAAaEEKAAAEKKKAA 237
|
170 180
....*....|....*....|....
gi 530389149 1807 EAARLRALAEEAKRQRQLAEEDAA 1830
Cdd:COG3064 238 AKAKADKAAAAAKAAERKAAAAAL 261
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1340-1591 |
7.45e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 47.31 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1340 KFISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAKELQQRMqEEVVRREEAAVDAQQQ 1419
Cdd:COG1842 13 ANINELLDKAEDPEKMLEQAIRDMESELAKAR------QALAQAIARQK-QLERKLEEAQARA-EKLEEKAELALQAGNE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1420 K--RSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvVRLQLEATERQRGGAEGELQALRARAEEAEAQkrqa 1497
Cdd:COG1842 85 DlaREALEEKQSLEDLAKALEAELQQAEEQVEK-----------LKKQLAALEQKIAELRAKKEALKARKAAAKAQ---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1498 qeeaERLRRQVQDesqrkrqaevelASRVKAEAEAAREKQRALQALEELRLQAEEAERRlrqaevERARQVQVALETAQR 1577
Cdd:COG1842 150 ----EKVNRSLGG------------GSSSSAMAAFERMEEKIEEREARAEAAAELAEGS------GDDLDKEFAQAGAQS 207
|
250
....*....|....
gi 530389149 1578 SAEAELQSKRASFA 1591
Cdd:COG1842 208 AVDSRLAALKARMK 221
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3802-3838 |
7.50e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.50e-05
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 3802 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3838
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2173-2651 |
7.62e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2173 EKHKKFAEQTLRQKAQVEQELTTLRLQL-EETDHQKNLLDEELQRLKAEATEAARQRSQV---EEELFSVRVQMEELSKL 2248
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2249 KARIEAENRAlilrdkdntQRFLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2328
Cdd:pfam12128 477 REEQEAANAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2329 RLKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA------ 2400
Cdd:pfam12128 539 FLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsare 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2401 -QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKS 2478
Cdd:pfam12128 619 kQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2479 EEMQTVQQEQLLQETQALQQSFL---SEKDSLLQR-----ERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQER 2550
Cdd:pfam12128 699 QAWLEEQKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREI 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2551 QRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE----VTASQVA 2626
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerkaSEKQQVR 857
|
490 500 510
....*....|....*....|....*....|...
gi 530389149 2627 ATKTLPNGRD--------ALDGPAAEAEPEHSF 2651
Cdd:pfam12128 858 LSENLRGLRCemsklatlKEDANSEQAQGSIGE 890
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2214-2427 |
7.69e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2214 LQRLKAEATEAARQRSQVEEElfsvrvQMEELSKLKARIEAENRALilrdkdnTQRFLQEEAEKmKQvAEEAARLSVAAQ 2293
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL-------EKERLAAQEQK-KQ-AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2294 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQGFQRT 2372
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 2373 LEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2427
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| DUF812 |
pfam05667 |
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ... |
1342-1599 |
7.76e-05 |
|
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.
Pssm-ID: 428574 [Multi-domain] Cd Length: 601 Bit Score: 48.85 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1342 ISETLR----RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQ 1417
Cdd:pfam05667 252 IAEQLRsaalASTEATSGASRSKQDLAELLSSFGGSSTTDTNLTKGSRFTHTEKLQFTNEEAPAATSSPPTKAETEEELQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1418 QQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEaterqrggaegELQALRARAEEAEAQKRQA 1497
Cdd:pfam05667 332 QQREEELEELQEQLEELESSIEELEKEIKKLESSIKQVEEELEELKEQNE-----------ELEKQYKVKKKTLDLLPDA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1498 QEEAERLRRQVQDESQRKrqaeVELASRVKAEAEAAREKQRALQalEELRLQAEEAERRLRQAEVERARQVQVAletaqr 1577
Cdd:pfam05667 401 EENIAKLQALVEASAQRL----VELAGQWEKHRVPLIEEYRALK--EAKSNKESESQRKLEEIKELREKIKEVA------ 468
|
250 260
....*....|....*....|..
gi 530389149 1578 saeAELQSKRASFAEKTAQLER 1599
Cdd:pfam05667 469 ---EEARSKEELYKQLVAEYER 487
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
2164-2428 |
7.89e-05 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227608 [Multi-domain] Cd Length: 1213 Bit Score: 49.16 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2164 QKQAADAEMEKHKKFAEqTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE-----------ATEAARQRSQVE 2232
Cdd:COG5283 80 VKEVNRATQASKKAYQE-YNAQYTQAENKLRSLSGQFGVASEQLMLQQKEIQRLQYAistlnksmaaqARLLEQTGNKFG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2233 EE-------LFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEeaarlsVAAQEAARLRQLAEED 2305
Cdd:COG5283 159 TAdakvvglRESFGRQTEALNKQLERTKKVADALTYVLDEAQQKLSQALSARLERLQE------SRTQMSQSSGQLGKRL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2306 LAQQRAL-AEKMLKEKMQ----AVQEATRLKAEAELLQQQKelaQEQARRLQEDKEQMAQQLAEETQGFQRTleaerQRQ 2380
Cdd:COG5283 233 ETDKAGAgALGLLGAALAgsfaAIGAAVRRTAQMNGELMDK---TKQVKGARDNLGKVTSQGEEMSDAIQET-----AEH 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 530389149 2381 LEMSAeaerLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2428
Cdd:COG5283 305 IKDSG----RELSKAAAIGAAAAMGVAAGKFPTGQEAKPTLKEMARVA 348
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1344-1539 |
7.90e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEER---LAEQQRAEererlaeveaaLEKQRQLAEAHAQAKAQAEREAKELQQRMQ----------EEVVRRE 1410
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE-----------LDASRALAEKQKHELDTEKRCAEELKEAMQmamegharmlEQYADLE 1120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1411 EAAVDAQQQKRSIQEELQQLRQsseAEIQAKARQAE-------AAERSRLRI--EEEIRVVRLQLEATERQ-RGGAE--- 1477
Cdd:PLN03188 1121 EKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVerEKERRYLRDENKSLQAQlRDTAEavq 1197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1478 --GELQALRARAEEA--EAQKR--QAQEEAERLRRQVqDESQRKRQAEVELASRVKAEAEAAREKQRA 1539
Cdd:PLN03188 1198 aaGELLVRLKEAEEAltVAQKRamDAEQEAAEAYKQI-DKLKRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
2332-2532 |
8.00e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 48.87 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2332 AEAELLQQQKELAQEQARRLQEDKEQMaqqlaeETQGFQRTLEAERQRQlemsaEAERLKLRVAEMSRAQARAEEDAQRF 2411
Cdd:COG4372 74 FQLDDIRPQLRALRTELGTAQGEKRAA------ETEREAARSELQKARQ-----EREAVRQELAAARQNLAKAQQELARL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2412 RKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllq 2491
Cdd:COG4372 143 TKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQ--------- 213
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 530389149 2492 etqALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 2532
Cdd:COG4372 214 ---ARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARA 251
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
44-156 |
8.51e-05 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 45.80 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 44 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDY 114
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNS 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530389149 115 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 156
Cdd:cd21323 104 ASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
1652-1827 |
8.58e-05 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 48.28 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1652 QAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1731
Cdd:COG4487 31 QIEQEDQSRILNTLEEFEKEANEKRAQYRSAKKKELSQLEEQLINQKKEQKNLFNEQIKQFELALQDEIAKLEALELLNL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1732 QQ---RQLLEEELARLQREAAAATQKRQELEaELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG----RFREL 1804
Cdd:COG4487 111 EKdkeLELLEKELDELSKELQKQLQNTAEII-EKKRENNKNEERLKFENEKKLEESLELEREKFEEQLHEAnldlEFKEN 189
|
170 180
....*....|....*....|...
gi 530389149 1805 AEEAARLRALAEEAKRQRQLAEE 1827
Cdd:COG4487 190 EEQRESKWAILKKLKRRAELGSQ 212
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1685-2318 |
8.62e-05 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 49.07 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1685 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAaeqELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR----QELEA 1760
Cdd:COG4717 212 ESRRAEHARLAELRSELRADRDHIRALRDAV---ELWPRLQEWKQLEQELTRRREELATFPRDGVLRLEKReahlQKTEA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1761 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1840
Cdd:COG4717 289 EIDALLVRLAELKDLASQLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGIEADLRDKEEAAGNGFEAERVHDLRSL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1841 AEKLAAIGEATRLKTEA--------EIALKEKEAENERLRRLAEDE----AFQRRRLEEQAA-QHKADIEERLAQLRKAS 1907
Cdd:COG4717 369 ECMLRYQSSQRELKQTEaayckrldEKRLFEDEAEEEARQRLADDEeevrAGDEAREEKIAAnSQVIDKEEVCNLYDRRD 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1908 DSELERQKGLVEDTLRQRRQVEEE--ILALKASFEKAAAGKAELELELGRIRSnaedtlrskeqaelEAARQRQLAAEEE 1985
Cdd:COG4717 449 TAWQKQRFLREKQTAFERQKTEHTkiIALRLAGMLLVALSRLLTSLIFQIIFA--------------VAQIVFLSAEIKS 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1986 RRRREAEERVQKSLAAEEEAarqRKAALEEVERLKAKVEEARRLRERAEQESAR--QLQLAQEAAQKRLQAEEKAHAfAV 2063
Cdd:COG4717 515 SSRAVREEKAAVTDIPEELA---RLLITDELPELAVDLLVQSRIRQHWQQLRKAldQLEAAYEALEGRFAAAEAAMA-EW 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2064 QQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQV----EEAERLKQSAEEQAQARAQAQAA 2139
Cdd:COG4717 591 QSEWEEALDELGLSRELSPEQQLDILSTMKDLKKLMQKKAELTHQVARLREEQaafeERVEGLLAVLEAQFIDLSTLFCV 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2140 AEKLRKEAEQEAARRAQAEQAALRQKQAAD---AEMEKHKKFAEQTL-----------RQKAQVEQELTTLRLQLEETDH 2205
Cdd:COG4717 671 QRLRVAAELQKEEARLALEGNIERTKELNDelrAELELHRKEILDLFdcgtadtedafREAAREEQQLTQRESRLESLEA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2206 QKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEE----AEKMKQV 2281
Cdd:COG4717 751 QLEGVAAEAYELSASLDQRELKEEELALLEEAIDALDEEVEELHAQVAALSRQIAQLEGGGTVAELRQRreslKEDLEEK 830
|
650 660 670
....*....|....*....|....*....|....*...
gi 530389149 2282 AEEAARLSVAAQEAAR-LRQLAEEDLAQQRALAEKMLK 2318
Cdd:COG4717 831 ARKWASLRLAVQVLEEaLRLFKERRLPAVIQEASEFFM 868
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2218-2408 |
8.83e-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: 47.92 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2218 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAAR 2297
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2298 LRQLAEEDLAQQrALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfQRTLEAER 2377
Cdd:TIGR02794 126 AKQAAEAKAKAE-AEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK-AKAEAAKA 203
|
170 180 190
....*....|....*....|....*....|.
gi 530389149 2378 QRQLEMSAEAERLKLRVAEMsRAQARAEEDA 2408
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAA-EAERKADEAE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1241-1505 |
8.86e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 48.18 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1241 MPLADSQAVREQLRQEQALLEEIERhgeKVEECQRFAKQYINAIKDYELQLVTYKAQLepVASPAKKPKVQSGSESVIQE 1320
Cdd:COG4942 28 AAAFSAAADDKQLKQIQKEIAALEK---KIREQQDQRAKLEKQLKSLETEIASLEAQL--IETADDLKKLRKQIADLNAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1321 YVDLRTHYSELTTLTSQYIkfisETLRRMEEEERLAE---QQRAEERERLAEVEAAL--EKQRQLAEAHAQAKAQAEREA 1395
Cdd:COG4942 103 LNALEVQEREQRRRLAEQL----AALQRSGRNPPPALlvsPEDAQRSVRLAIYYGALnpARAERIDALKATLKQLAAVRA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1396 KELQQRMQeevVRREEAAVDAQQQKRSI-QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvRLQLEATERQRG 1474
Cdd:COG4942 179 EIAAEQAE---LTTLLSEQRAQQAKLAQlLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIA--SAEAAAAKAREA 253
|
250 260 270
....*....|....*....|....*....|..
gi 530389149 1475 GAEGELQALRARAEEAE-AQKRQAQEEAERLR 1505
Cdd:COG4942 254 AAAAEAAAARARAAEAKrTGETYKPTAPEKML 285
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1697-2066 |
8.91e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 48.34 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1697 QELEKQRQLAEGTAQQRlaaEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1776
Cdd:pfam07888 41 QERAELLQAQEAANRQR---EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEELAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1777 ---ARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLAEKlaaigEATRL 1853
Cdd:pfam07888 118 dalLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRK--EEEAERKQLQAKLQQTEE-----ELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1854 KTEAEIALKEKEAENERLRRLAEDEAFQRRRLeEQAAQHKADIEERLAQLRkasdselerqkglvedTLRQRrqveeeil 1933
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKL-TTAHRKEAENEALLEELR----------------SLQER-------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1934 aLKASFEKAAAGKAELElelgrirsnAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAAL 2013
Cdd:pfam07888 246 -LNASERKVEGLGEELS---------SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530389149 2014 E---------EVERLKAKVEEARRLRERAEQESARQ--LQLAQEAAQKRLQAEEKAhAFAVQQK 2066
Cdd:pfam07888 316 DkdrieklsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1797-1916 |
9.01e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.79 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1797 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLAEKLAAIGEATRLKTEAEIA-LKEKEAE 1867
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1868 NERLRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA---SDSE-LERQKG 1916
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKAgweADSKtLRFSKG 261
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2212-2417 |
9.04e-05 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 48.41 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2212 EELQRLKAEATEAARQRsqvEEELFSVRVQMEELSKLKARIEAENRAL-ILRDKDNTQRFLQEEAEKMKQVAEEAARlSV 2290
Cdd:COG3064 62 QQYGRIQSQQSSAKKGE---QQRKKKEEQVAEELKPKQAAEQERLKQLeKERLKAQEQQKQAEEAEKQAQLEQKQQE-EQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2291 AAQEAARLRQLAEEDLAQQRALAEKMlkekmQAVQEAtrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQ 2370
Cdd:COG3064 138 ARKAAAEQKKKAEAAKAKAAAEAAKL-----KAAAEA---KKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530389149 2371 rtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2417
Cdd:COG3064 210 ---EAEAKAKAEKKAEAAAEEKAAAEKKKAAAKAKADKAAAAAKAAE 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2162-2393 |
9.58e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 48.18 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2162 LRQKQAADAEMEKH----KKFAEQTLRQKAQVEQELTTLRLQLEET----DHQKNLLDEELQRLKAEATEAARQRSQVEE 2233
Cdd:COG4942 40 LKQIQKEIAALEKKireqQDQRAKLEKQLKSLETEIASLEAQLIETaddlKKLRKQIADLNARLNALEVQEREQRRRLAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2234 ELFSVRvQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALA 2313
Cdd:COG4942 120 QLAALQ-RSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2314 EKM---LKEKMQAVQE-----ATRLKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMS 2384
Cdd:COG4942 199 AKLaqlLEERKKTLAQlnselSADQKKLEELRANESRLKNEIASaEAAAAKAREAAAAAEAAAARARAAEAKRTGETYKP 278
|
....*....
gi 530389149 2385 AEAERLKLR 2393
Cdd:COG4942 279 TAPEKMLIS 287
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1107-1823 |
9.58e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1107 EEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1185
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1186 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplGAWLQDARRRQEQIQAMpLADSQavrEQLRQEQALLEEIER 1265
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRKQ-LSKTQ---EELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1266 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTHYSELTTLTSQY 1338
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1339 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKeLQQRMQEEvvrreeaAVDAQ 1417
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDK-------AAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1418 QQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1497
Cdd:pfam07111 370 VERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1498 QEEAER--LRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEEL--RLQAEEAERRLRQAEVERARQVQVAle 1573
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVA-- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1574 taqRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1653
Cdd:pfam07111 527 ---QQLEQELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1654 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1728
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1729 QGEQQR-----QLLEEE----LARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1794
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 530389149 1795 EAEAGRFRELAEEAARLRALAEEAKRQRQ 1823
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1799-2045 |
9.62e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 48.34 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1799 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDE 1878
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1879 AFQRRRLEEQAAQHKADIEE------RLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELE 1952
Cdd:pfam07888 114 AEEKDALLAQRAESEARIREleedikTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1953 LGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2031
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 530389149 2032 RAEQESAR-QLQLAQ 2045
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1889-2124 |
9.91e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 48.18 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1889 AAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE 1968
Cdd:COG4942 29 AAFSAAADDKQLKQIQK----EIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1969 QAEL-EAARQRQLAAEEERRRREAEERVQKSLAAEEEAA----------------RQRKAALEEVERLKAKVEeARRLRE 2031
Cdd:COG4942 105 ALEVqEREQRRRLAEQLAALQRSGRNPPPALLVSPEDAQrsvrlaiyygalnparAERIDALKATLKQLAAVR-AEIAAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2032 RAEQESARQLQLAQEAAQKRLQAEEKahafavqQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEaeearvqAEREAAQ 2111
Cdd:COG4942 184 QAELTTLLSEQRAQQAKLAQLLEERK-------KTLAQLNSELSADQKKLEELRANESRLKNEIAS-------AEAAAAK 249
|
250
....*....|...
gi 530389149 2112 SRRQVEEAERLKQ 2124
Cdd:COG4942 250 AREAAAAAEAAAA 262
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
33-157 |
1.00e-04 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 45.43 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 33 AQDEQDERDRVQKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMR 101
Cdd:cd21325 14 SEGTQHSYSEEEKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTP 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 102 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 157
Cdd:cd21325 91 FIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3355-3389 |
1.04e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.04e-04
10 20 30
....*....|....*....|....*....|....*
gi 530389149 3355 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3389
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1813-2048 |
1.07e-04 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 48.02 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1813 ALAEEAKRQRQlaeedaarQRAEAERVLAEKLaaigeaTRLKTEAEIALKEKEAENERLRRLAEDeafqrrRLEEQAAQH 1892
Cdd:COG3064 59 AVVQQYGRIQS--------QQSSAKKGEQQRK------KKEEQVAEELKPKQAAEQERLKQLEKE------RLKAQEQQK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1893 KADIEERLAQLRKASDSELERQKGLvedtlRQRRQVEEEILALKASFEKAAAgKAELELELGRIRSNAEDTLRSKEQAEL 1972
Cdd:COG3064 119 QAEEAEKQAQLEQKQQEEQARKAAA-----EQKKKAEAAKAKAAAEAAKLKA-AAEAKKKAEEAAKAAEEAKAKAEAAAA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1973 EAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALeeverlKAKVEEARRLRERAEQESARqlQLAQEAA 2048
Cdd:COG3064 193 KKKAEAEAKAAAEKAKAEAEAKAKAEKKAEAAAEEKAAAEK------KKAAAKAKADKAAAAAKAAE--RKAAAAA 260
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4390-4427 |
1.16e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.16e-04
10 20 30
....*....|....*....|....*....|....*...
gi 530389149 4390 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 4427
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1067-1507 |
1.16e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 48.56 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1067 TLRSELEltlGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQL-----------KEAQAVPATLPE----LE 1131
Cdd:pfam15921 437 AMKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtlesseRTVSDLTASLQEkeraIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1132 ATKASLKKLRAQAEAQQPTFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVAQLLE-------RWQAVLAQTD 1201
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrTAGAMQVEKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1202 VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfaKQYI 1281
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELN 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1282 NAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTHYSELTTltsqyikfISETLRRMEEEERLAeqqra 1361
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQ--------TRNTLKSMEGSDGHA----- 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1362 eererlaeVEAALEKQRQLAEAHAQAKAqaereakelqqrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQssEAEIQAK 1441
Cdd:pfam15921 726 --------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ--ELSTVAT 783
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1442 ARQAEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQAlrarAEEAEAQKRQAQEEAeRLRRQ 1507
Cdd:pfam15921 784 EKNKMAGELEVLRSQER----RLKEKVANMEVALDKASLQF----AECQDIIQRQEQESV-RLKLQ 840
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2182-2414 |
1.21e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2182 TLRQKAQVEQELTTLRLQleetdhQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIL 2261
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2262 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2335
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 2336 LLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2414
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3971-4005 |
1.24e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.24e-04
10 20 30
....*....|....*....|....*....|....*
gi 530389149 3971 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4005
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1838-2609 |
1.29e-04 |
|
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: 48.53 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1838 RVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqHKADIEERLAQLRKASDSELERQKgl 1917
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGYELLKEK-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1918 vEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAED-TLRSKEQAELEAARQRQLAAEEERRRREAEERVQ 1996
Cdd:TIGR02169 233 -EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1997 KSLAAEEEAARQRKAALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFAVQQKE 2067
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2068 QELQQtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE-RLKQSAEEqaqaraqaqaaaeklrke 2146
Cdd:TIGR02169 389 DYREK--------LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEaKINELEEE------------------ 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2147 aeqeaarraqaeqaalrqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEA---TE 2223
Cdd:TIGR02169 443 ------------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQArasEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2224 AARQRSQVEEELFS----VRVQMEELSKLKAR------IEAENR--ALILRDKDNTQR---FLQEEA---------EKMK 2279
Cdd:TIGR02169 505 RVRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMR 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2280 QVAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAE 2333
Cdd:TIGR02169 585 DERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2334 AELLQQQKElaqEQARRLQEDKEQMAQQLAeetqGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK 2413
Cdd:TIGR02169 665 GILFSRSEP---AELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2414 QAEEIGEKLhrtelatqekvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-----EAKLLQLKSEEMQtvQQEQ 2488
Cdd:TIGR02169 738 RLEELEEDL--------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQ--AELS 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2489 LLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAE 2568
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 530389149 2569 E---GVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQ 2609
Cdd:TIGR02169 882 SrlgDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1486-1610 |
1.32e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1486 RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRalQALEELRL------QAEEAERRLRQ 1559
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQaalkqkQAEEAAAKAAA 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 530389149 1560 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ 1610
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2162-2464 |
1.35e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteristic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.75 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2162 LRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEEELFSVRVQ 2241
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2242 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2320
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2321 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAEETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEM 2397
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 2398 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLREaiaELEREK 2464
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1477-1604 |
1.48e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 430825 [Multi-domain] Cd Length: 305 Bit Score: 47.04 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1477 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERR 1556
Cdd:pfam09787 67 NQQIEQLRTELQELEAQ---QQEEAESSREQLQD---LEEQLATERQARREAEAELERLQEELRYLEEELRRTKATLQSR 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1557 LRQ--AEVERARQvQVALETAQRSAEAELQSK----RASFAEKTAQLErSLQEE 1604
Cdd:pfam09787 141 IKDreAEIEKLRN-QLTNKSQSSSSQSELENRlhqlTESLIQKQTMLE-ALSTE 192
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
2183-2406 |
1.60e-04 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 47.82 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2183 LRQKAQVEQELTTLRLQLEETDHQKN----LLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRA 2258
Cdd:COG3206 143 LLESLKVLRAGRSRVIELSYTSNDPKlaakLANALAQAYLADQLEAQLEAFRRASDSLDERLEELRARLQEAEAQVEDFR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2259 LILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE-----DLAQQRALAEKMLKEKMQAvQEATRLKAE 2333
Cdd:COG3206 223 AQHGLTDAARGQLLSEQQLSALNTQLQSARARLAQAEARLASLLQLlplgrEAAALREVLESPTIQDLRQ-QYAQVRQQI 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 2334 AELLQQQKEL---AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2406
Cdd:COG3206 302 ADLSTELGAKhpqLVALEAQLAELRQQIAAELRQILASLPNELALLEQQEAALEKELAQLKGRLSKLPKLQVQLRE 377
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1431-1584 |
1.64e-04 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.03 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1431 RQSSEAEIQAKARQAEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1508
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1509 QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQ 1584
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ... |
1448-1567 |
1.74e-04 |
|
MAP7 (E-MAP-115) family; The organisation 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-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 428577 [Multi-domain] Cd Length: 153 Bit Score: 45.01 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1448 AERSRLRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsrvK 1527
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQER-----LEKEEEERLRREELRRRAEEERARREEEARRLEEERKREEEERQR---K 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 530389149 1528 AEAEAAREKQRALQALEELRLQAEEAERRLRQaEVERARQ 1567
Cdd:pfam05672 81 AEEEAEEKEQREKEEQERLQKQKEEAEAKARE-EAERQRQ 119
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4280-4313 |
1.75e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.75e-04
10 20 30
....*....|....*....|....*....|....
gi 530389149 4280 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4313
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1546-1860 |
1.83e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 47.52 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1546 LRLQAEEAERRlRQAEVERARQVQVALETAQRsaEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEA 1625
Cdd:COG2268 213 RRRIAQVLQDA-EIAENEAEKETEIAIAEANR--DAKLVELEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAETRREA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1626 ERAreeaerelerwqlkanealrlRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQL 1705
Cdd:COG2268 290 EQA---------------------EILAEQAIQEEKAQAEQEVQHAKALEAREMRVGLIERQ--KETELEPQERSYFINA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1706 AEGTAQ-QRLAAEQELIRLRAETEQGEQ-QRQLLEEELArlqrEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1783
Cdd:COG2268 347 AQRQAQeEAKAAANIAEAIGAQAEAAVEtARETEEAERA----EQAALVAAAEAAEQEQVEIAVRAEAAKAEAEAQAAEI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1784 RSTSEKSKQRLEAEAGRFRELAeEAARLRALAEEAKRQRQL--AEEDAARQRAEAERVL-AEKLAAIGEATRLKTEAEIA 1860
Cdd:COG2268 423 KAEAEAIREKGKAEAEAKRALA-EAIQVLGDAAAAELFKALvqALPEVAEEAAQPMKNIdSEKVRVIGGANGGSTAGKVN 501
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2172-2484 |
1.88e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 47.52 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2172 MEKHKKFAEQTLRQkaqVEQELTTLRLQLE------------ETDHQKNLLDEELQRLKAEATEAARQrsqVEEELfsvr 2239
Cdd:COG2268 161 NEDRLGFAQVVQEV---VGDDLSKMGLVLDslaindindtskENQDPNNYLDALGRRRIAQVLQDAEI---AENEA---- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2240 VQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQ---EAARLRQLAEEDLAQQRALAEK- 2315
Cdd:COG2268 231 EKETEIAIAEANRDAKLVELEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAEtrrEAEQAEILAEQAIQEEKAQAEQe 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2316 -----MLKEKMQAVQEATRLKaEAELLQQQKEL--------AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLE 2382
Cdd:COG2268 311 vqhakALEAREMRVGLIERQK-ETELEPQERSYfinaaqrqAQEEAKAAANIAEAIGAQAEAAVETARETEEAERAEQAA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2383 MSAEAERLKLRVAEMsraQARAEEDAQRFRKQAEEIgeklhRTELATQEKVTLVQtLEIQRQQSdhDAERLREAIAELER 2462
Cdd:COG2268 390 LVAAAEAAEQEQVEI---AVRAEAAKAEAEAQAAEI-----KAEAEAIREKGKAE-AEAKRALA--EAIQVLGDAAAAEL 458
|
330 340
....*....|....*....|..
gi 530389149 2463 EKEKLQQEAKLLQLKSEEMQTV 2484
Cdd:COG2268 459 FKALVQALPEVAEEAAQPMKNI 480
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3355-3389 |
1.90e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 41.55 E-value: 1.90e-04
10 20 30
....*....|....*....|....*....|....*
gi 530389149 3355 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3389
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPET 35
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1687-2057 |
2.13e-04 |
|
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: 428594 [Multi-domain] Cd Length: 562 Bit Score: 47.33 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1687 QAVRQRELAEQELEKQRQ-------LAEGTAQQRLAAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQkrqelE 1759
Cdd:pfam05701 32 QTVERRKLVELELEKVQEeipeykkQSEAAEAAKAQVLEELESTKRLIEE-------LKLNLERAQTEEAQAKQ-----D 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1760 AELAKVRA-EMEVLLASKARAeeESRSTSEKSKQRLEAEAGRFRELAEEaarLRALAEEakRQRQLAEEDAARQRAEaER 1838
Cdd:pfam05701 100 SELAKLRVeEMEQGIADEASV--AAKAQLEVAKARHAAAVAELKSVKEE---LESLRKE--YASLVSERDIAIKRAE-EA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1839 VLAEKlaAIGEATRLKTEAEIALKEK---------EAENERLR----------------RLAEDEAfqrRRLEEQAA--- 1890
Cdd:pfam05701 172 VSASK--EIEKTVEELTIELIATKESlesahaahlEAEEHRIGaalareqdklnwekelKQAEEEL---QRLNQQLLsak 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1891 --QHKADIEERLAQLRKAS-----DSELERQKGLVEDTLRQRRQVEEEILALKASFE--KAAAGKAELELELGRIrsnAE 1961
Cdd:pfam05701 247 dlKSKLETASALLLDLKAElaaymESKLKEEADGEGNEKKTSTSIQAALASAKKELEevKANIEKAKDEVNCLRV---AA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1962 DTLRS---KEQAELEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAArqrKAALEEVERLKAKVEEARRLRERAE--- 2034
Cdd:pfam05701 324 ASLRSeleKEKAELASLRQREgMASIAVSSLEAELNRTKSEIALVQAKE---KEAREKMVELPKQLQQAAQEAEEAKsla 400
|
410 420 430
....*....|....*....|....*....|...
gi 530389149 2035 ----------QESARQLQLAQEAAQKRLQAEEK 2057
Cdd:pfam05701 401 qaareelrkaKEEAEQAKAAASTVESRLEAVLK 433
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
2277-2626 |
2.19e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2277 KMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALaekmLKEKMQAvqeatrlKAEAELLQQQKELAQEQARRLQEDKE 2356
Cdd:pfam02463 166 RLKRKKKEALK--KLIEETENLAELIIDLEELKLQE----LKLKEQA-------KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2357 QMAQQLAEEtqgFQRTLEAERQRQLEMSAEAErlklrvaemsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlV 2436
Cdd:pfam02463 233 KLNEERIDL---LQELLRDEQEEIESSKQEIE-----------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE---E 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2437 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqlLQETQALQQSFLSEKDSLLQRERFIEQ 2516
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE-----LKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2517 EKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEA-----EEGVRRKQEELQQLEQQRRQQEEL 2591
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeekkEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350
....*....|....*....|....*....|....*
gi 530389149 2592 LAEENQRLREQLQLLEEQHRAALAHSEEVTASQVA 2626
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1353-1517 |
2.23e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1353 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQ 1432
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1433 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1512
Cdd:PRK12678 158 ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
....*
gi 530389149 1513 QRKRQ 1517
Cdd:PRK12678 237 DARGD 241
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
39-152 |
2.24e-04 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 43.82 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 39 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQ 109
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCN 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530389149 110 IALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21329 73 YAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
2144-2395 |
2.25e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 47.33 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2144 RKeaeqeaarraqaeqaalrqkqAADAEMEKhkkfaeqTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATE 2223
Cdd:COG4372 104 RE---------------------AARSELQK-------ARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2224 AARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQ--RFLQEEAEKMKQVAEEAARLSVAAQE-AARLRQ 2300
Cdd:COG4372 156 LAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQeaQNLATRANAAQARTEELARRAAAAQQtAQAIQQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2301 LAEEdlAQQRALAekmLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2380
Cdd:COG4372 236 RDAQ--ISQKAQQ---IAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQQAAATQRGQVLAGAAQRVAQ 310
|
250
....*....|....*
gi 530389149 2381 LEMSAEAERLKLRVA 2395
Cdd:COG4372 311 AQAQAQAQAQLLSSA 325
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
1682-1898 |
2.29e-04 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 47.12 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1682 GKAEEQAVRQRELAEQELEkQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1761
Cdd:COG4487 29 YKQIEQEDQSRILNTLEEF-EKEANEKRAQYRSAKKKELSQLEEQLINQKKEQKNLFNEQIKQFELALQDEIAKLEALEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1762 LAKVR-AEMEVLLASKARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAEEAKrqrqlaEEDAARQRAEAERVL 1840
Cdd:COG4487 108 LNLEKdKELELLEKELDELSKELQKQLQNTAEIIEKK----RENNKNEERLKFENEKKL------EESLELEREKFEEQL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1841 AEKLAAIGEAtrlktEAEIALKEKEAENERLRRLAE--DEAFQRRRLEEQAAQHKADIEE 1898
Cdd:COG4487 178 HEANLDLEFK-----ENEEQRESKWAILKKLKRRAElgSQQVQGEALELPNESFIRSKFP 232
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1353-1604 |
2.32e-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: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1353 ERLAEQQRAEERERLAEVEaalekqrqlaeahaqakaQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQE---E 1426
Cdd:pfam10174 453 ERLKEQREREDRERLEELE------------------SLKKENKDLKEKvsaLQPELTEKESSLIDLKEHASSLASsglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1427 LQQLRQSSEAEIQA-------------KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1493
Cdd:pfam10174 515 KDSKLKSLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1494 K---------------RQAQEEAERLR--RQVQDESQRKRQAEVELASRVK-AEAEAAREKQRA--LQALEELRLQAEEA 1553
Cdd:pfam10174 595 KndkdkkiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDAT 674
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1554 ERRLRQAEV--------------ERARQVQVALETAQRSAEAELQSKRASFA--EKTAQLERSLQEE 1604
Cdd:pfam10174 675 KARLSSTQQslaekdghltnlraERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE 741
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1344-1592 |
2.37e-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: 434789 [Multi-domain] Cd Length: 374 Bit Score: 46.96 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERERL--AEVEAALEKQRQ---LAEAHAQAKAQAEREAKELQQRMqeevvrrEEAAVDAQQ 1418
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLerAAQEAEQRKQCQeqnLKEKEEELQALREQNGLQLQERL-------EQACHKRQL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1419 QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSrlriEEEIRvvRLQLE-----ATERQRGGAEGELQALRARAEEAEAQ 1493
Cdd:pfam15558 161 KELEEQKKVQENNLSELLNHQARKVLVDCQAKA----EELLR--RLSLEqslqrSQENYEQLVEERHRELREKAQKEEEQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1494 KRQAQEEAERLRRQvQDESQRKRQAEVELASRvKAEAEAAREKQRALQALEELRLQAEEAERRLRQ----AEVERARQVQ 1569
Cdd:pfam15558 235 FQRAKLRAEEKEEE-QQEHKEALAELADQKIQ-QARSVAHKTVQDKAQRARELNLEREKNHHLLKLkvekEEECHREGIK 312
|
250 260
....*....|....*....|...
gi 530389149 1570 VALETAQRSAEAELQSKRASFAE 1592
Cdd:pfam15558 313 EAIKKKEQRSEQISREKEATLEE 335
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2180-2483 |
2.39e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 47.40 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2180 EQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE--------------LFSVRVQMEEL 2245
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDR 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2246 SKLKARIEAENRALILRDKDNTQR---FLQEEAEKMKQVAEEAARLSVAAQeaaRLRQLAEEDLAQQRALAEK------- 2315
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERqmaAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTAKKMTLESSertvsdl 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2316 --MLKEKMQAVQ----EATRLKAEAEL-LQQQKELAQE--QARRLQEDKEQMAQQLAEEtqgfQRTLEAERQRQLEMSAE 2386
Cdd:pfam15921 502 taSLQEKERAIEatnaEITKLRSRVDLkLQELQHLKNEgdHLRNVQTECEALKLQMAEK----DKVIEILRQQIENMTQL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2387 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQR-QQSDHDAERLReAIAELEREKE 2465
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvKLVNAGSERLR-AVKDIKQERD 656
|
330 340 350
....*....|....*....|....*....|....*.
gi 530389149 2466 KLQQEAKL------------------LQLKSEEMQT 2483
Cdd:pfam15921 657 QLLNEVKTsrnelnslsedyevlkrnFRNKSEEMET 692
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
186-263 |
2.42e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 43.06 E-value: 2.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 186 DNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 263
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2174-2470 |
2.62e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 435008 [Multi-domain] Cd Length: 329 Bit Score: 46.35 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2174 KHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIE 2253
Cdd:pfam15905 64 KSQKDLKESKDQKEL-EKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2254 AENRAlilrdkDNTQRflqeeaekmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQAVQeaTRLKAE 2333
Cdd:pfam15905 143 AKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQVTQ--KNLEHS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2334 AELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK 2413
Cdd:pfam15905 197 KGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 2414 QAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQE 2470
Cdd:pfam15905 276 QIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2289-2567 |
2.62e-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: 380155 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2289 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAEeTQG 2368
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLAA-ISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2369 FQRTLEAERQRQLEMSAEAERlklrvaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2448
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2449 DAE---RLREAIAE--LEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSllqrerfiEQEKAKLEQ 2523
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 530389149 2524 LFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRR-QHEA 2567
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1064-1930 |
2.78e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1064 AAPTLRsELELTLGKLEQVRSLSAIYLEKLKTISLVIRGT--------QGAEEVLRAHE-------EQLKEAQAVPATLP 1128
Cdd:TIGR00606 187 ALETLR-QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYEneldplkNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1129 ELEATKASLKKLRAQAEAQQPTFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRERVaqllerwqavlaqtdvrQREL 1207
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDC-----------------QREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1208 EQLGRQLRYYRESADPL----GAWLQDARRRQEQIQAMplaDSQAVREQLRQEQALLEE---IER-----HGEKVEECQR 1275
Cdd:TIGR00606 329 EKLNKERRLLNQEKTELlveqGRLQLQADRHQEHIRAR---DSLIQSLATRLELDGFERgpfSERqiknfHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1276 FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTHYSELTTLT--SQYIKFISETLRRMEE 1351
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLEgsSDRILELDQELRKAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1352 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKELQQRMQEEVVRREEAAVDAQQQK---RSIQEELQ 1428
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKiksRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1429 QLRQSSEAEIQAKARQAEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-----AQKRQAQE-EAE 1502
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTR--DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdVCGSQDEEsDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1503 RLRRQVqdESQRKRQAEVELASRVKAE--AEAAREKQ-------RALQALEELRLQAEEAERRLRQA------------E 1561
Cdd:TIGR00606 643 RLKEEI--EKSSKQRAMLAGATAVYSQfiTQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLApdklksteselkK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1562 VERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQL 1641
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1642 KANEALRlrlqaeEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLaaeQELI 1721
Cdd:TIGR00606 800 ELKDVER------KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT---NELK 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1722 RLRAETEQGEQQRQLLEEELARLQREA----AAATQKRQE---LEAELAKVRAEMEVLLASK----ARAEEESRSTSEKS 1790
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISSKetsnKKAQDKVNDIKEKV 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1791 KQRLEAEAGRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE------AERVLAEKLaaigeaTRL 1853
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNL------TLR 1024
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1854 KTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEE 1930
Cdd:TIGR00606 1025 KRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3690-3725 |
2.80e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.80e-04
10 20 30
....*....|....*....|....*....|....*.
gi 530389149 3690 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 3725
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3430-3461 |
2.88e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.88e-04
10 20 30
....*....|....*....|....*....|..
gi 530389149 3430 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 3461
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2197-2482 |
3.06e-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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 46.44 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2197 RLQLEETDHQKNLLDE-ELQRLKAEATEAARQRSQVEEEL---FSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQ 2272
Cdd:pfam13868 33 RIKAEEKEEERRLDEMmEEERERALEEEEEKEEERKEERKqyrQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2273 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKELAQEQARRLQ 2352
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEDLRILEYLKEKAE--REEEREAERREIKEEKEREIARLR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2353 EDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2432
Cdd:pfam13868 191 AQQEKAQDEKAERDELRAKLYQEEQERKWRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQ 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530389149 2433 VTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2482
Cdd:pfam13868 271 AEDEEIEQEEAEKRREKRLEHRRELEKQIEERERQRAAEREEELEEGERL 320
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1360-1886 |
3.08e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 47.03 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1360 RAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVD---------AQQQKRSIQEELQQL 1430
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELERKASALARQLERESDRNQELQKRirllekreaEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1431 RQSSEAEIQAKARQAEA----AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1506
Cdd:pfam05557 81 KKKNLEALNKKLNEKESqladAREVISCLKNELSELRRQIQRQELELSSTNSELEELQERLDLQKAKAQEAEQLRQNLEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1507 QVQ---DESQRKRQAEVELASRV-------KAEAEAAR--EKQRALQALEE--------------LRLQAEEAERRLRQa 1560
Cdd:pfam05557 161 QQSslaEAEQRIKELEFEIQSQEqdseivkNSKSELARipELERELERLREhnkhlnenienkllLKEEVEDLKRKLER- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1561 eVERARQVQVALETAQRSAEAELQSkrasfAEKTAQ---------------LERSLQEEHVAVAQLREEAERRAQQQAEA 1625
Cdd:pfam05557 240 -EEGYREELATLELEKEKLEQELKS-----WEKLAQdtglnlrspedlsrrIEQLQQREITLKEENSSLTSSARQLEKAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1626 ERAREEAEREL-----ERWQLKANEALRLRLQAEEVAQQKS-------LAQAEAEKQKEEAEREARRRGKAEEQAVRQRE 1693
Cdd:pfam05557 314 RELEQELAQYLkniedLNKKLKRHKALVRRLQRRVLLLTKErdgmraiLESYDKELTPSNYSPQLLERIEEAEDMTQDMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1694 LAEQELEKQRQLAEGTA----QQRLAAEQELIRLRAETEQGEQQRQllEEELARLQREAaaatqkrQELEAELAKVRAEM 1769
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELggykQQATTLERELQALRQQESLADPSYS--KEEVDSLRRKL-------ETLEAERQRLREQK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1770 EVLLASKARAEEESRSTSEKSK---QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervlAEKLAA 1846
Cdd:pfam05557 465 NELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQRANDLEKLQAEIERLKRRLKKLEDD------------LEQVGS 532
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 530389149 1847 IGEATRLKTEAEIA--LKEKEAENERLRRLaeDEAFQRRRLE 1886
Cdd:pfam05557 533 LPETTSTMNFKEVLelRKELESAELKNQRL--KEVFQAKIQE 572
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1696-1927 |
3.12e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1696 EQELeKQRQLAEGTAQ----QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAaaatqkRQELEAELAKVRA---- 1767
Cdd:PRK10929 29 TQEL-EQAKAAKTPAQaeivEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAEL------RQQLNNERDEPRSvppn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1768 ------EMEVLLAS-------------KARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAE----EAKRQRQL 1824
Cdd:PRK10929 102 mstdalEQEILQVSsqlleksrqaqqeQDRAREISDSLSQLPQQQTEAR----RQLNEIERRLQTLGTpntpLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1825 AEEDAARQRAEAERVLAEKLAAIG--EATRLKteAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1902
Cdd:PRK10929 178 LQAESAALKALVDELELAQLSANNrqELARLR--SELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGD 255
|
250 260
....*....|....*....|....*
gi 530389149 1903 LRKASDSELERQKGLvEDTLRQRRQ 1927
Cdd:PRK10929 256 LPKSIVAQFKINREL-SQALNQQAQ 279
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2212-2420 |
3.30e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2212 EELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKM-----KQVAEEAA 2286
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2287 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLA 2363
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 2364 EETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2420
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1946-2625 |
3.30e-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: 46.89 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1946 KAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE 2025
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2026 ARRLRERAEQESARQLQLAQEAAQ-KRLQAEEKAHAFAV----QQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEE 2100
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLEETQerinRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2101 ARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAE 2180
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2181 QTLRQKAQVEQELTTLRlqleetdhqknllDEELQRLKAEATEAARQRSQVEEELFSvrvqMEELSKLKARIEAENRAli 2260
Cdd:TIGR00618 404 ILQREQATIDTRTSAFR-------------DLQGQLAHAKKQQELQQRYAELCAAAI----TCTAQCEKLEKIHLQES-- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2261 lrdkdntQRFLQEEAEKMKQVA----EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2336
Cdd:TIGR00618 465 -------AQSLKEREQQLQTKEqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2337 LQQQKELAQEQARrLQEDKEQmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAE 2416
Cdd:TIGR00618 538 AQLETSEEDVYHQ-LTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ---NITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2417 EigekLHRTELATQEKVTLVQTLEIQRQQSdhdaERLREAIAELEREKEKL----QQEAKLLQLKSEEMQTVQQEQLLQE 2492
Cdd:TIGR00618 613 E----QHALLRKLQPEQDLQDVRLHLQQCS----QELALKLTALHALQLTLtqerVREHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2493 TQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVR 2572
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 2573 RKQEELQQLEQQRRQQEELLAEENQRLRE------QLQLLEEQHRAALAHSEEVTASQV 2625
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLreedthLLKTLEAEIGQEIPSDEDILNLQC 823
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1719-2032 |
3.41e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 46.65 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1719 ELIRLRAETEQGEQQ--RQLLEEELARLQREAAAATQKRQeLEAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR 1793
Cdd:pfam05557 3 ELIESKARLSQLQNEkkQMELEHKRARIELERKASALARQ-LERESDRNQElqkRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1794 LEAEAGRFRELAEEAARLRALAE----------EAKRQRQLAEEDAARQRAEAERV---LAEKLAAIGEATRLKTEAEIA 1860
Cdd:pfam05557 82 KKNLEALNKKLNEKESQLADAREvisclknelsELRRQIQRQELELSSTNSELEELqerLDLQKAKAQEAEQLRQNLEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1861 LKEKEAENERLRRLAedeafQRRRLEEQAAQHKADIEERLAQLRKAsDSELERQKGLVE---DTLRQRRQVEEEILALKA 1937
Cdd:pfam05557 162 QSSLAEAEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPEL-ERELERLREHNKhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1938 S---FEKAAAGKAELELELGRIRS----------NAEDTLRSKE--QAELEAARQRQLAAEEE----RRRREAEERVQKS 1998
Cdd:pfam05557 236 KlerEEGYREELATLELEKEKLEQelksweklaqDTGLNLRSPEdlSRRIEQLQQREITLKEEnsslTSSARQLEKAQRE 315
|
330 340 350
....*....|....*....|....*....|....
gi 530389149 1999 LaaEEEAARQRKAALEEVERLKAKVEEARRLRER 2032
Cdd:pfam05557 316 L--EQELAQYLKNIEDLNKKLKRHKALVRRLQRR 347
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1915-2125 |
3.66e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 46.56 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1915 KGLVEdTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEER 1994
Cdd:COG4372 67 RNLRS-GVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1995 VQ------KSLAAE-EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA-VQQK 2066
Cdd:COG4372 146 AQdlqtrlKTLAEQrRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEELArRAAA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 2067 EQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQS 2125
Cdd:COG4372 226 AQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQA 284
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2246-2480 |
4.00e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2246 SKLKARIEAENRALILRdkdntQRFlqeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQ 2325
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAK-----ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2326 EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV 2394
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2395 -AEMSRAQAR---AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREK-EKLQQ 2469
Cdd:PRK05035 583 aAAIARAKAKkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKaRKAAQ 662
|
250
....*....|.
gi 530389149 2470 EAKLLQLKSEE 2480
Cdd:PRK05035 663 QQANAEPEEAE 673
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1373-1544 |
4.14e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1373 ALEKQRQLA--------EAHAQAKAQA-EREAKEL--QQRMQEEVvrreeaavDAQQQKRsiqeELQQLRQSSEAEIQAK 1441
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARGRleRQKMHDKA--------KAEEQRT----KLLELQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1442 ARQAEA-AERSRLRIEEEirvvrlqleaterqrggAEGELQALRARAEEAEAQKrqaqeEAERLR-RQVQDESQRKRQAE 1519
Cdd:PTZ00491 716 QSRAEAlAEAEARLIEAE-----------------AEVEQAELRAKALRIEAEA-----ELEKLRkRQELELEYEQAQNE 773
|
170 180
....*....|....*....|....*
gi 530389149 1520 VELasrvkaeaeaarEKQRALQALE 1544
Cdd:PTZ00491 774 LEI------------AKAKELADIE 786
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2734-2767 |
4.48e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.48e-04
10 20 30
....*....|....*....|....*....|....
gi 530389149 2734 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2767
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2180-2437 |
4.54e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2180 EQTLR---QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRS------QVEEELFSVRVQmeeLSKLKA 2250
Cdd:PRK11281 66 EQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQ---LQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2251 RIEAENRALIlrdkdnTQRFLQEEAEkmkqvaeeaARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQEATrl 2330
Cdd:PRK11281 143 DLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALRPS-QRVLLQAEQALL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2331 kaEAELLQQQKELA-----QE--QARRlqEDKEQMAQQLAEETQGFQrtlEAERQRQLEMSAEAerlklrVAEMSRAQAR 2403
Cdd:PRK11281 205 --NAQNDLQRKSLEgntqlQDllQKQR--DYLTARIQRLEHQLQLLQ---EAINSKRLTLSEKT------VQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*
gi 530389149 2404 AEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVQ 2437
Cdd:PRK11281 272 ARIQANPLVAQELEINLQLSQRLLkATEKLNTLTQ 306
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1802-2062 |
4.57e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 46.17 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1802 RELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1881
Cdd:COG4372 70 RSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1882 RRRLEEQAAQHKADIEErlAQLRKASDSELERQKglvedtlrqrRQVEEEILALKASFEKAAAGKAELELELGRIRSnae 1961
Cdd:COG4372 150 QTRLKTLAEQRRQLEAQ--AQSLQASQKQLQASA----------TQLKSQVLDLKLRSAQIEQEAQNLATRANAAQA--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1962 dtlRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVE--RLKAKVEEARRL----RERAEQ 2035
Cdd:COG4372 215 ---RTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAqaRLEQEVAQLEAYyqayVRLRQQ 291
|
250 260
....*....|....*....|....*...
gi 530389149 2036 ESARQL-QLAQEAAQKRLQAEEKAHAFA 2062
Cdd:COG4372 292 AAATQRgQVLAGAAQRVAQAQAQAQAQA 319
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1341-1403 |
4.62e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.40 E-value: 4.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1341 FISETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAEREAKELQQRMQ 1403
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1361-1603 |
4.74e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1361 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLRQSSEAEIQA 1440
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1441 KARqaeaaersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEV 1520
Cdd:pfam12795 74 ILA-------------------SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1521 ELASRVKAEAEAAREKQRALQA--------LEELRLQAEEAERR--LRQAEVERARQVQVALETAQRSAEAELQSKRASF 1590
Cdd:pfam12795 135 RLNGPAPPGEPLSEAQRWALQAelaalkaqIDMLEQELLSNNNRqdLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQE 214
|
250
....*....|....
gi 530389149 1591 AEKT-AQLERSLQE 1603
Cdd:pfam12795 215 AEQAvAQTEQLAEE 228
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1690-1907 |
4.82e-04 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 45.90 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1690 RQRELAEQELEKQRQLAEGTAQQRLAAEQelirlraeteqgeQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEM 1769
Cdd:COG3206 203 RLEELRARLQEAEAQVEDFRAQHGLTDAA-------------RGQLLSEQQLSALNTQLQSARARLAQAEARLASLLQLL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1770 EVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAeklAAIGE 1849
Cdd:COG3206 270 PLGREAAALREVLESPTIQDLRQQYAQVR---QQIADLSTELGAKHPQLVALEAQLAELRQQIAAELRQILA---SLPNE 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1850 ATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKAS 1907
Cdd:COG3206 344 LALLEQQEAALEKELAQLKGRLSKLPKLQV-QLRELEREAEAARSLYETLLQRYQELS 400
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2211-2431 |
5.18e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.74 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2211 DEELQRLKAEATEAARQRSQveEELfsVRVQMEELSKLKARIEAENRALILRDKDNTqrflqEEAEKMKQVAEEAARLSV 2290
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEAR--KRL--VAKHGAEISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2291 AAQEAARLRQLAEEDLAQQRALAekmlkekmqavqeATRLKAEAELLQQQKELAQEQARrlQEDKEQMAQQLAEETQGfq 2370
Cdd:PRK07735 75 AKQKREGTEEVTEEEKAKAKAKA-------------AAAAKAKAAALAKQKREGTEEVT--EEEKAAAKAKAAAAAKA-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530389149 2371 RTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2431
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE 198
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
32-156 |
5.45e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 43.46 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 32 WAQDEQDERdrvQKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRM 100
Cdd:cd21324 16 GTQHSYSEE---EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLT 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 101 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 156
Cdd:cd21324 90 PFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3765-3801 |
5.62e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.62e-04
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 3765 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 3801
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
1026-1569 |
5.77e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1026 QRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQG 1105
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1106 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQE-------VGERLQQRHGERDVE 1178
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRI 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1179 VERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQA 1258
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1259 LLEEIERHGEKVEECQR---FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLT 1335
Cdd:pfam02463 605 LAQLDKATLEADEDDKRakvVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1336 SQYIKFISETLRRMEEEERlaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEA--- 1412
Cdd:pfam02463 685 AESELAKEEILRRQLEIKK--KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeek 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1413 ---AVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEE 1489
Cdd:pfam02463 763 eeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1490 AEAQKRQ--AQEEAERLrrqvQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1567
Cdd:pfam02463 843 KEEQKLEklAEEELERL----EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
..
gi 530389149 1568 VQ 1569
Cdd:pfam02463 919 IE 920
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1106-1601 |
5.90e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 46.42 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1106 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1185
Cdd:COG3096 552 AEELEALHQELEALIESLSDSVSNAREQRMALRQEQEQLQSRIQSLMQRAPVWLAAQNALEQLSEQSGEEFTDSQDVTEY 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1186 VAQLLERWQAVLAQTD---VRQRELEQLGRQLRYYRESADP--------LGAWLQDARRRQEQIQAMP------------ 1242
Cdd:COG3096 632 MQQLLEREREATVERDelgARKNALDEEIERLSQPGGSEDQrlnalaerFGGVLLSEIYDDVTIEDAPyfsalygpsrha 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1243 --LADSQAVREQLRQEQALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQlePVASPAKKPK---- 1309
Cdd:COG3096 712 ivVPDLSQVKEHLEGLTDCPEDLyliegdpQSFDDSVFSVDELEKAVVVKIADRQWRYSRFPEI--PLFGRAAREQrles 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1310 VQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAH 1384
Cdd:COG3096 790 LHAERDVLSERHATLSFDVQKTQRLHQAFSRFIGSHLAVAfeadpEAEIRQLNSRRNELERALSNHENDNQQQRIQFDQA 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1385 AQAKAQAEREAKELQQRMQEEVVRR----EEAAVDAQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERSRLRIEEE 1458
Cdd:COG3096 870 KEGVTALNRLIPQLNLLADESLADRveeiRERLDEAQEAARFIQQHGNTLSKLEPiaSVLQSDPEQFEQLKEDYAQAQQM 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1459 IRVVRLQL----EATER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEVELA 1523
Cdd:COG3096 950 QRQARQQAfaltEVVQRrahfsysdsaEMLSENSDLnEKLRQRLEQAEAERTRAREQL----RQHQAQLSQYNQVLASLK 1025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1524 SRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERA----RQVQVALETAQRSAEAELQS--KRASFAEKTAQL 1597
Cdd:COG3096 1026 SSYDTKKELLNELQQELQDIGVRADSGAEERARIRRDELHAQlstnRSRRNQLEKQLTFCEAEMDNltRKLRKLERDYFE 1105
|
....
gi 530389149 1598 ERSL 1601
Cdd:COG3096 1106 MREQ 1109
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1685-1782 |
5.95e-04 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 44.93 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1685 EEQAVRQRELAEQE-----LEKQRQLAEGTA----QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1755
Cdd:pfam00769 20 EETRKAQEELEESEetaelLEEKLRVAEEEAelleQKAQEAEEEKERLEESAEMEAEEKEQLERELREAQEEVARLEEES 99
|
90 100
....*....|....*....|....*..
gi 530389149 1756 QELEAELAKVRAEMEvllasKARAEEE 1782
Cdd:pfam00769 100 ERKEEEAERLQEELE-----EAREEEE 121
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1357-1473 |
6.05e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 397124 [Multi-domain] Cd Length: 297 Bit Score: 45.36 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1357 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAqAEREAKELQQRMQEEVVRREeaavdaqQQKRSIQEELQQLRQSSEA 1436
Cdd:pfam02841 183 KSKEAVEEAILQTDQALTAKEKAIEAERAKAEA-AEAEQELLREKQKEEEQMME-------AQERSYQEHVKQLIEKMEA 254
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 1437 EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1473
Cdd:pfam02841 255 EREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| YloA |
COG1293 |
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ... |
1812-2039 |
6.37e-04 |
|
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224212 [Multi-domain] Cd Length: 564 Bit Score: 45.85 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1812 RALAEEAKRQRQLAEEDAARqrAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAE---------DEAFQR 1882
Cdd:COG1293 200 GLLAEELLSRAGLDKKVPAK--DLFEEEIKKVREALEELLNPLKPNYYYKDEKYLDVVPLKAYADleklfnealDEKFER 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1883 RRLEEQAAQHKADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEILALKASFEkaaagKAELELELGRIRSNAED 1962
Cdd:COG1293 278 DKIKQLASELEKKLEKELKKLENKLE-KQEDELEELEKAAEELRQKGELLYANLQLIE-----EGLKSVRLADFYGNEEI 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1963 TLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEA-ARQRKAALEEVERLKAkVEEARRLRERAEQESAR 2039
Cdd:COG1293 352 KIELDKSKTPSENAQRYFKKYKKLKGAKVNLDRQLSELKEAIAyYESAKTALEKAEGKKA-IEEIREELIEEGLLKSK 428
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2104-2470 |
6.53e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 45.65 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2104 QAEREAAQSRRQVEEAERLKQSAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAEQtL 2183
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKVEELEE---------------------------KYKELSRSGEELAEEKDAL-L 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2184 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRAL--IL 2261
Cdd:pfam07888 122 AQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2262 RDKDNTQRFLQEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQ 2339
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2340 QKELAQ------EQARRLQEDKEQMAQqlaeETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrk 2413
Cdd:pfam07888 278 RLQAAQltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER--- 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 2414 qaeeigEKLhRTELATQEKVTLVQTLEIQRQQSDhdaerLREAIAELEREKEKLQQE 2470
Cdd:pfam07888 342 ------EKL-EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3136-3172 |
6.71e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 6.71e-04
10 20 30
....*....|....*....|....*....|....*..
gi 530389149 3136 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 3172
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3062-3096 |
6.77e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 6.77e-04
10 20 30
....*....|....*....|....*....|....*
gi 530389149 3062 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 3096
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1717-1977 |
6.85e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 45.59 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1717 EQELIRLRAETEQGEQQRQlleeelARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRlEA 1796
Cdd:COG2268 215 RIAQVLQDAEIAENEAEKE------TEIAIAEANRDAKLVELEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAET-RR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1797 EAGRFRELAEEAARLralaEEAKRQRQLAEEDAARQRaeaervlaekLAAIGEATRLKtEAEIALKEKEAENERLRRLAE 1876
Cdd:COG2268 288 EAEQAEILAEQAIQE----EKAQAEQEVQHAKALEAR----------EMRVGLIERQK-ETELEPQERSYFINAAQRQAQ 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1877 DEAFQRRRLEE-----QAAQHKADIEERLAQLRKASDSELERQKGLVEdtlrQRRQVEEEILALKASFEKAAAGKAELEL 1951
Cdd:COG2268 353 EEAKAAANIAEaigaqAEAAVETARETEEAERAEQAALVAAAEAAEQE----QVEIAVRAEAAKAEAEAQAAEIKAEAEA 428
|
250 260
....*....|....*....|....*.
gi 530389149 1952 ElgrirsnaedtlRSKEQAELEAARQ 1977
Cdd:COG2268 429 I------------REKGKAEAEAKRA 442
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1478-1610 |
6.89e-04 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 45.32 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1478 GELQALRARAEEAEAQK-RQAQEEAERLRRQVQDESQRKRQAEVELAsrvkAEAEAAREKQRALQALEELRLQAEEAERR 1556
Cdd:COG3064 65 GRIQSQQSSAKKGEQQRkKKEEQVAEELKPKQAAEQERLKQLEKERL----KAQEQQKQAEEAEKQAQLEQKQQEEQARK 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1557 LrQAEveraRQVQVALETAQRSAEAElQSKRASFAEKTAQLERSLQEEHVAVAQ 1610
Cdd:COG3064 141 A-AAE----QKKKAEAAKAKAAAEAA-KLKAAAEAKKKAEEAAKAAEEAKAKAE 188
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1386-1601 |
6.93e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1386 QAKAQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQEELQQLRQ------SSEAEIQAK--------ARQAEAA 1448
Cdd:PRK11637 54 QDIAAKEKSVRQQQQQrasLLAQLKKQEEAISQASRKLRETQNTLNQLNKqidelnASIAKLEQQqaaqerllAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1449 ERsrlriEEEIRVVRLQLEATERQRG------------GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1516
Cdd:PRK11637 134 FR-----QGEHTGLQLILSGEESQRGerilayfgylnqARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1517 QAEVELASRVK--AEAEAAREKQRalQALEELRLQaeeaERRLR----QAEVE-RARQVQVALEtAQRSAEAELQSKRAS 1589
Cdd:PRK11637 209 KLEQARNERKKtlTGLESSLQKDQ--QQLSELRAN----ESRLRdsiaRAEREaKARAEREARE-AARVRDKQKQAKRKG 281
|
250
....*....|..
gi 530389149 1590 FAEKTAQLERSL 1601
Cdd:PRK11637 282 STYKPTESERSL 293
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1824-2057 |
7.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 45.48 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1824 LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEEQAAQHKADIEERLAQL 1903
Cdd:COG4942 31 FSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEA-------QLIETADDLKKLRKQIADLNARL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1904 RKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELE-------LGRIRSNAEDT---LRSKEQAELE 1973
Cdd:COG4942 104 NALEVQEREQRRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYgalnparAERIDALKATLkqlAAVRAEIAAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1974 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR---QLQLAQEAAQK 2050
Cdd:COG4942 184 QAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKareAAAAAEAAAAR 263
|
....*..
gi 530389149 2051 RLQAEEK 2057
Cdd:COG4942 264 ARAAEAK 270
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2164-2364 |
7.55e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2164 QKQAADAEMEKHKKFAEQT--LRQKAQVEQElttlRLQLEEtdhQKNLLDEELQRLKAEATEAARQRSQVEEElfsVRVQ 2241
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLE---KERLAAQEQKKQAEEAAKQAALKQKQAEE---AAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2242 MEELSKLKAriEAENRALilrdkdntqrflqeeAEKMKQVAEEAARLSVAAQEAarlrQLAEEdlAQQRALAEkmlkEKM 2321
Cdd:PRK09510 141 AAAAAKAKA--EAEAKRA---------------AAAAKKAAAEAKKKAEAEAAK----KAAAE--AKKKAEAE----AAA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530389149 2322 QAVQEAtRLKAEAELLQQQKELAQEQARRlqEDKEQMAQQLAE 2364
Cdd:PRK09510 194 KAAAEA-KKKAEAEAKKKAAAEAKKKAAA--EAKAAAAKAAAE 233
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1700-1975 |
7.58e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilisation of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 427167 [Multi-domain] Cd Length: 383 Bit Score: 45.22 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1700 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1776
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELERELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1777 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1836
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1837 ErvLAEKLAAIG---EATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLRKASDS 1909
Cdd:pfam03148 159 D--LSDKKEALEideKCLSLNnTSPNISYKPGPTRIPPNSSTPETwEEFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1910 ELERQKGLVEDTLRQRrqVEEeilalkasFEKAaagKAELELELGRIRSNAEDTlrSKEQAELEAA 1975
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEM--EKNIEALEKA 287
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1433-1567 |
7.63e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1433 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDES 1512
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 1513 QRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1567
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1731-2572 |
7.91e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 45.92 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1731 EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE------- 1803
Cdd:pfam01576 4 EEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLCEE-KNILAEQLQAETELFAEAEEMRARLAARKQELEEilhelea 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1804 -LAEEAARLRALAEEAKR--------QRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEIAL-KEKEAENERLR 1872
Cdd:pfam01576 83 rLEEEEERSQQLQNEKKKmqqhiqdlEEQLEEEEAARQKLQLEKVTTEaKIKKMEEDILLLEDQNNKLqKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1873 ----RLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKglvedtlrQRRQVEEEILALKASFEKAAAGKAE 1948
Cdd:pfam01576 163 eftsNLAEEEE-KSKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEK--------AKRKLEGESSDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1949 LELELgrirsnaedtlrSKEQAELEAARQRqlaaeeerrrreaeervqkslaAEEEAArQRKAALEEVERLKAKVEEarr 2028
Cdd:pfam01576 234 LRAQL------------AKKEEELQAALAR----------------------LEEETA-QKNAALKKLRELEAQLSE--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2029 LRERAEQESArqlQLAQEAAQKRLQAEEkahafavqqkeqelqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAERE 2108
Cdd:pfam01576 276 LQEDLESERA---ARAKAEKQRRDLGEE------------------------LEALKTELEDTLDTTAAQQELRSKREQE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2109 AAQSRRQVEEAERLKQSAEEqaqaraqaqaaaeKLRKEAEQEAARRAQAeqaaLRQKQAADAEMEKHKKFAEQtlrQKAQ 2188
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQ-------------EMRQKHTQALEELTEQ----LEQAKRNKASLEKAKQALES---ENAE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2189 VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIlRDKDNTQ 2268
Cdd:pfam01576 389 LQAELRSLQQAKQDSEHKRKKLEGQLQELQSRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS-KDVSSLE 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2269 RFLQEEAEKMKQvaEEAARLSVAAqeaaRLRQLAEEdlaqqRALAEKMLKEKMQAVQEATRlkaEAELLQQQkelAQEQA 2348
Cdd:pfam01576 468 SQLQDTQELLQE--ETRQKLNLSS----RLRQLEDE-----KNSLQEQLEEEEEAKRNVER---QLQTLQAQ---LSDLK 530
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2349 RRLQEDKEqMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLklrvaemsraqaraeeDAQRFRKQAEeigekLHRTELA 2428
Cdd:pfam01576 531 KKLEEDAG-AVEALEEGRKRLQRELEALTQRLEEKAAAYDKL----------------EKTKNRLQQE-----LDDLLVD 588
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2429 TQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKllqlkseemqtvqqeqllqetqalqqsflsEKDS-L 2507
Cdd:pfam01576 589 LDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAR------------------------------EKETkA 638
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 2508 LQRERFIEQEKAKLEqlfqdevakaqqlreEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVR 2572
Cdd:pfam01576 639 LSLARALEEALDAKE---------------ELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKR 688
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3690-3728 |
7.96e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 39.63 E-value: 7.96e-04
10 20 30
....*....|....*....|....*....|....*....
gi 530389149 3690 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 3728
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
2169-2440 |
8.12e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 46.03 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2169 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRsqVEEelfsVRVQMEELSKL 2248
Cdd:COG3096 835 EAEIRQLNSRRNELERALSNHENDNQQQRIQFDQAKEGVTALNRLIPQLNLLADESLADR--VEE----IRERLDEAQEA 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2249 KARIEAENRALILRDKdnTQRFLQEEAEKMKQVAEEAArLSVAAQEAARLRQLAEEDLAQQRAlaEKMLKEKMQAVQEAT 2328
Cdd:COG3096 909 ARFIQQHGNTLSKLEP--IASVLQSDPEQFEQLKEDYA-QAQQMQRQARQQAFALTEVVQRRA--HFSYSDSAEMLSENS 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2329 ----RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEetqgFQRTLEAERQRQLEMSAEAERLKLRVAE--MSRAQA 2402
Cdd:COG3096 984 dlneKLRQRLEQAEAERTRAREQLRQHQAQLSQYNQVLAS----LKSSYDTKKELLNELQQELQDIGVRADSgaEERARI 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530389149 2403 RAEEDAQRF---RKQAEEIGEKLHRTELATQEKVTLVQTLE 2440
Cdd:COG3096 1060 RRDELHAQLstnRSRRNQLEKQLTFCEAEMDNLTRKLRKLE 1100
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1101-1552 |
8.26e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1101 RGTQGAEEVLRAHEEQLKEAQAVPA----------------TLPELEATKASLKKLRAQAEAQQP-------TFDALrdE 1157
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqladvkTICEQEARIKDLEAQRAQLQAGQPcplcgstSHPAV--E 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1158 LRGAQEVGERlQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQ 1237
Cdd:PRK10246 519 AYQALEPGVN-QSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDD 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1238 IQamPLADSQAVRE----QLRQEQALLEEIERHGEKVEEcqrfakqyinaikdYELQLVTYKAQLEPVASPAKKPKVQSG 1313
Cdd:PRK10246 598 IQ--PWLDAQEEHErqlrLLSQRHELQGQIAAHNQQIIQ--------------YQQQIEQRQQQLLTALAGYALTLPQED 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1314 SESviqeyvdlrthySELTTltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1393
Cdd:PRK10246 662 EEA------------SWLAT----------------RQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEET 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1394 EAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1473
Cdd:PRK10246 714 VALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1474 GGAegelQALRARAEEAEAQKRQAQEE-------AERLRRQVQDESQRKRQ---AEVELASRVKAEAEAAREKQRALQAL 1543
Cdd:PRK10246 794 QQA----QTLVTQTAQALAQHQQHRPDgldltvtVEQIQQELAQLAQQLREnttRQGEIRQQLKQDADNRQQQQALMQQI 869
|
....*....
gi 530389149 1544 EELRLQAEE 1552
Cdd:PRK10246 870 AQATQQVED 878
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2166-2419 |
8.32e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2166 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA-----EATEAARQRSQVEEELFSVRV 2240
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2241 QMEELSKLKARI-EAENRaliLRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2319
Cdd:PRK04863 511 LAEQLQQLRMRLsELEQR---LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2320 KMQAVQEATRLKAEAELLQQqkelAQEQARRLQE---DKEQMAQQLaeeTQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2396
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLA----AQDALARLREqsgEEFEDSQDV---TEYMQQLLERERELTVERDELAARKQALDEE 660
|
250 260
....*....|....*....|...
gi 530389149 2397 MSRAQARAEEDAQRFRKQAEEIG 2419
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAERFG 683
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1444-1610 |
8.34e-04 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 45.32 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1444 QAEAAERSRLRIEEEiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDEsqrkRQAEVELA 1523
Cdd:COG3064 58 GAVVQQYGRIQSQQS-SAKKGEQQRKKKEEQVAEELKPKQAAEQERLKQLEKERLKAQEQQKQAEEAE----KQAQLEQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1524 SRVKAEAEAAREKQRalQALEELRLQAEEAERRLRQAEVER-ARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQ 1602
Cdd:COG3064 133 QQEEQARKAAAEQKK--KAEAAKAKAAAEAAKLKAAAEAKKkAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKAE 210
|
....*...
gi 530389149 1603 EEHVAVAQ 1610
Cdd:COG3064 211 AEAKAKAE 218
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
1363-1540 |
8.62e-04 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225803 [Multi-domain] Cd Length: 835 Bit Score: 45.45 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1363 ERERLAEVEAALEKQRQLAEAHAQAKAQAEreakelqQRMQEEVvrreeaavdAQQQKRSIQEELQQLRQSSEAEIQAkA 1442
Cdd:COG3264 16 RRELLTAESAQLEAALQLLQEAVNSKRQEE-------AEPAAEE---------AELQAELIQQELAINDQLSQALNQQ-T 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1443 RQAEAAERSRLRIEEeirvVRLQLEATERQrggAEGELQALRARAEEAEAQ-----------KRQAQEEAERLRRQVQDE 1511
Cdd:COG3264 79 ERLNALASDDRQLAN----LLLQLLQSSRT---IREQIAVLRGSLLLSRILlqqlgplpeagQPQEQFEVTQERDALQAE 151
|
170 180 190
....*....|....*....|....*....|..
gi 530389149 1512 SQRKRQAE---VELASRVKAEAEAAREKQRAL 1540
Cdd:COG3264 152 KAYINALEgqaEQLTAEVRDILDQILDTRREL 183
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1490-1938 |
8.80e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.52 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1490 AEAQKRQAQEEAERLRRQVQDES-QRKRQAEVElASRVKAEAEAAREKQRALQALEElrlqAEEAERRLRQAEVERA-RQ 1567
Cdd:pfam09731 73 SAVTGESKEPKEEKKQVKIPRQSgVSSEVAEEE-KEATKDAAEAKAQLPKSEQEKEK----ALEEVLKEAISKAESAtAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1568 VQVALETAQRSAEAELQSKRASFA-EKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1646
Cdd:pfam09731 148 AKEAKDDAIQAVKAHTDSLKEASDtAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1647 LRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQqrLAAEQELIRLRAE 1726
Cdd:pfam09731 228 LDNVEEKVEKAQSLAKLVDQYKEL------------VASERIVFQQELVSIFPDIIPVLKEDNLL--SNDDLNSLIAHAH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1727 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASkaraeeesrstsEKSKQRLEAEagrfrelae 1806
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAA------------DEAQLRLEFE--------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1807 eaarlRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR-RRL 1885
Cdd:pfam09731 353 -----REREEIRESYEEKLRTELERQAEAHEEHLKDVLVE--QEIELQREFLQDIKEKVEEERAGRLLKLNELLANlKGL 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530389149 1886 EEQAAQHKADIEERLA--QLRKASDSelerqkglVEDTLR------QRRQVEEEILALKAS 1938
Cdd:pfam09731 426 EKATSSHSEVEDENRKaqQLWLAVEA--------LRSTLEdgsadsRPRPLVRELKALKEL 478
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1259-1752 |
8.96e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1259 LLEEIERHGEKVEECQRFAKQYI---NAIKDY---ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELT 1332
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLkelIEKKDHltkELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1333 TLTSQYIKFISE---TLRRMEEEERlAEQQRAEERE-RLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvr 1408
Cdd:pfam05483 342 KAKAAHSFVVTEfeaTTCSLEELLR-TEQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED--- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1409 reEAAVDAQQQKRSIQEELQQ-------LRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-------------- 1467
Cdd:pfam05483 418 --EKLLDEKKQFEKIAEELKGkeqelifLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcd 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1468 --ATERQRGGAEGELQALRARAEEAEAQKRQAQEEA--------ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1537
Cdd:pfam05483 496 klLLENKELTQEASDMTLELKKHQEDIINCKKQEERmlkqienlEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1538 RALQ---------------ALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSA--------EAELQSKRASFAEK 1593
Cdd:pfam05483 576 RSIEyevlkkekqmkilenKCNNLKKQIENKNKNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEI 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1594 TAQLERSLQEEHVAVAQLREEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKslaqaeaekqkEE 1673
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEE---------------------VEKAKAIADEAVKLQKEIDKRCQHK-----------IA 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1674 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1752
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2296-2471 |
9.18e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.38 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2296 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLAEETQG 2368
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2369 FQRTLEAERQRQLemsaeAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2448
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 530389149 2449 DAERLREAIAELEREKEKLQQEA 2471
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| DUF4207 |
pfam13904 |
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several ... |
1344-1448 |
9.25e-04 |
|
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 433570 [Multi-domain] Cd Length: 223 Bit Score: 43.93 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQ-------AEREAKELQQRMQEEVVRREEA-- 1412
Cdd:pfam13904 71 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKqkaaesaSKSLAKPERKVSQEEAKEVLQEwe 150
|
90 100 110
....*....|....*....|....*....|....*..
gi 530389149 1413 -AVDAQQQKRsiQEELQQLRQSSEAEIQAKARQAEAA 1448
Cdd:pfam13904 151 lKKLEQQQRK--REEEQREQLKKEEEEQERKQLAEKA 185
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1797-1976 |
9.25e-04 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 44.94 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1797 EAGRFRELAEEAARlrALAEEAKRQRQLAEEDAARQRAEAERV--LAEKLAAIGEATRLKTEAE--IALKEKEAENERLR 1872
Cdd:COG3064 63 QYGRIQSQQSSAKK--GEQQRKKKEEQVAEELKPKQAAEQERLkqLEKERLKAQEQQKQAEEAEkqAQLEQKQQEEQARK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1873 RLAE----DEAFQRRRLEEqAAQHKADiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAE 1948
Cdd:COG3064 141 AAAEqkkkAEAAKAKAAAE-AAKLKAA-AEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKAEAEAKAKAE 218
|
170 180
....*....|....*....|....*...
gi 530389149 1949 LELELGRIRSNAEDTLRSKEQAELEAAR 1976
Cdd:COG3064 219 KKAEAAAEEKAAAEKKKAAAKAKADKAA 246
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1381-1562 |
9.61e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 226055 [Multi-domain] Cd Length: 372 Bit Score: 44.82 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1381 AEAHAQAKA---QAEREAKELQQRMQEEVVRREEAAVDAQQQKrsIQEELQQLR--QSSEAEIQAKArQAEAAERSRLRI 1455
Cdd:COG3524 152 KEAQKIAQAilkQSEKLINQLSERARRDTVRFAEEEVQKAEER--VKKASNDLTdyRIKNGVFDPKA-QAEVQMSLVSKL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1456 EEEIRVVRLQLEATERQRGGAEGELQALRARaeeAEAQKRQAQEEAERLRRQVQDESQRKRQAEVElasRVKAEAE-AAR 1534
Cdd:COG3524 229 EDELIVIQAQLDTVKSVMNPENPQIPGLKAR---IESLRKQLLQEKQAISAGGSSQSLSNQAAEFQ---RLYLENTfAEK 302
|
170 180
....*....|....*....|....*...
gi 530389149 1535 EKQRALQALEELRLqaeEAERRLRQAEV 1562
Cdd:COG3524 303 AYAAALTSLESARI---EADRQQLYLEI 327
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2265-2434 |
9.66e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2265 DNTQRFLQEEAEKMKQVAEEAarlSVAAQEAARLRQlaEEDLAQqrALAEKMLKEKMQAVQEATRLKAEAElLQQQKEla 2344
Cdd:pfam05262 202 DLKERESQEDAKRAQQLKEEL---DKKQIDADKAQQ--KADFAQ--DNADKQRDEVRQKQQEAKNLPKPAD-TSSPKE-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2345 qeqARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRkqaEEIGEKLHR 2424
Cdd:pfam05262 272 ---DKQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR---EPVAEDLQK 339
|
170
....*....|
gi 530389149 2425 TELATQEKVT 2434
Cdd:pfam05262 340 TKPQVEAQPT 349
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
2235-2519 |
1.00e-03 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 45.60 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2235 LFSVRVQMEELSKLKARIEAENRALILRDKDNTQrfLQEEAEKMKQvaeEAARLSVAAQEAARLRQLAEEDLAQQRALAE 2314
Cdd:COG4717 149 LFSGTSGSPASTKLLEVLNKEADSLYKPSGRNPQ--INQLLEKLKQ---ERNEIDEAEKEYATYHKLLESRRAEHARLAE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2315 KM--LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED--------------KEQMAQQLAEETQGFQRTLEAERQ 2378
Cdd:COG4717 224 LRseLRADRDHIRALRDAVELWPRLQEWKQLEQELTRRREELatfprdgvlrlekrEAHLQKTEAEIDALLVRLAELKDL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2379 RQLEMSAEAERLKLRVAeMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAT-----QEKVTLVQTLEIQRQQSDHDAERL 2453
Cdd:COG4717 304 ASQLIPAKEAVLQALVR-LHQQLSEIKASAFELTETLAGIEADLRDKEEAAgngfeAERVHDLRSLECMLRYQSSQRELK 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2454 REAIAELEREKEKLQ------QEAKLLQLKSEEMQTVQQEQLLQETQALQQ--------SFLSEKDSLLQRERF-IEQEK 2518
Cdd:COG4717 383 QTEAAYCKRLDEKRLfedeaeEEARQRLADDEEEVRAGDEAREEKIAANSQvidkeevcNLYDRRDTAWQKQRFlREKQT 462
|
.
gi 530389149 2519 A 2519
Cdd:COG4717 463 A 463
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1342-1447 |
1.07e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 44.21 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1342 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAK------AQ--AEREAKELQQRMQEEV-V 1407
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEvakiqmQQkiMEKEAEKKISEIEDEMhL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530389149 1408 RREEAAVDAQQQKRSIQEELQQLRQSSE----AEIQAKARQAEA 1447
Cdd:cd03406 237 AREKARADAEYYRALREAEANKLKLTPEylelKKYQAIANNTKI 280
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1364-1569 |
1.09e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1364 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEelqQLRQSSEAEIQAKAR 1443
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAE---AASAPEAAQARERRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1444 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqaLRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAEVELA 1523
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEE-----EERDERRRRGDREDRQAEAERGERG--RREERGRDGDDRDR 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530389149 1524 SRVKAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEVERARQVQ 1569
Cdd:PRK12678 206 RDRREQGDRREERGRRDGGDRrGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2273-2464 |
1.13e-03 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 44.55 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2273 EEAEKMKQVAEEAARlsvAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqavQEATRLKAeAELLQQQKELAQEQARRLQ 2352
Cdd:COG3064 62 QQYGRIQSQQSSAKK---GEQQRKKKEEQVAEELKPKQAAEQERLKQ-----LEKERLKA-QEQQKQAEEAEKQAQLEQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2353 EDKEQMAQQLAEEtqgfQRTLEAERQRQLemsAEAERLKLR--VAEMSRAQARAEEDAQrfrKQAEEIGEKLHRtELATQ 2430
Cdd:COG3064 133 QQEEQARKAAAEQ----KKKAEAAKAKAA---AEAAKLKAAaeAKKKAEEAAKAAEEAK---AKAEAAAAKKKA-EAEAK 201
|
170 180 190
....*....|....*....|....*....|....
gi 530389149 2431 EKVTLVQTLEIQRQQSDHDAERLREAIAELEREK 2464
Cdd:COG3064 202 AAAEKAKAEAEAKAKAEKKAEAAAEEKAAAEKKK 235
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1750-1910 |
1.19e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 43.77 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1750 AATQKRQELEAELAKVRAEMEvllaskaRAEEESRStSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDA 1829
Cdd:pfam00769 3 EAEREKQELEERLKQYEEETR-------KAQEELEE-SEETAELLEEKL---RVAEEEAELLEQKAQEAEEEKERLEESA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1830 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDS 1909
Cdd:pfam00769 72 EMEAEEKEQLERELREAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAKEKLLAASTSPSHHHSEESENEDDEEEE 151
|
.
gi 530389149 1910 E 1910
Cdd:pfam00769 152 E 152
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
1396-1591 |
1.21e-03 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 44.81 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1396 KELQQRM--QEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1473
Cdd:COG4487 34 QEDQSRIlnTLEEFEKEANEKRAQYRSAKKKELSQLEEQLINQKKEQKNLFNEQIKQFELALQDEIAKLEALELLNLEKD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1474 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREkqralqaleelrlQAEEA 1553
Cdd:COG4487 114 KELELLEKELDELSKELQKQLQNTAEIIEKKRENNKNEERLKFENEKKLEESLELEREKFEE-------------QLHEA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530389149 1554 ERRLRQAEVERARQ-VQVALETAQRSAEAE---LQSKRASFA 1591
Cdd:COG4487 181 NLDLEFKENEEQREsKWAILKKLKRRAELGsqqVQGEALELP 222
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2269-2481 |
1.24e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2269 RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2344
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2345 QEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARA----EEDAQRFRKQAEEIG 2419
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530389149 2420 EKLHRTELATQEKVTLVQTLEIQRQQ------SDHDAERLREAIAELErEKEKLQQ------EAKLLQLKSEEM 2481
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldtemaQLRVQRLRYEDL 355
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2274-2409 |
1.27e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2274 EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2349
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530389149 2350 RLQEDKEQmaQQLAEetqgfqrtLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2409
Cdd:PTZ00491 761 QELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1374-1584 |
1.33e-03 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 44.47 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1374 LEKQRQLAEAHAQAKAqAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKaRQAEAAERSRL 1453
Cdd:pfam08017 31 LERRQRDAENRSQGNV-LERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER-RQRDAENRSQG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1454 RIEEEIR---VVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEA 1530
Cdd:pfam08017 109 NVLERRQrdaENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1531 EAAREKQRAlqalEELRLQAEEAERRLRQAEVERARQVqvaLETAQRSAEAELQ 1584
Cdd:pfam08017 189 NVLERRQRD----AENRSQGNVLERRQRDAENRSQGNV---LERRQRDAENRSQ 235
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1686-1829 |
1.34e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1686 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1765
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1766 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1829
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1349-1603 |
1.39e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227608 [Multi-domain] Cd Length: 1213 Bit Score: 44.92 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1349 MEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAKA------QAEREAKEL-QQRMQEEVVRReeaAVDAQQQK 1420
Cdd:COG5283 41 LEKQQKLTKDGLSASKGKYEGLSEAMEKQkKAYEDLKQEVKEvnratqASKKAYQEYnAQYTQAENKLR---SLSGQFGV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1421 RSIQEELQQLR-QSSEAEIQAKAR----QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ-------ALRARAE 1488
Cdd:COG5283 118 ASEQLMLQQKEiQRLQYAISTLNKsmaaQARLLEQTGNKFGTADAKVVGLRESFGRQTEALNKQLErtkkvadALTYVLD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1489 EAEAQKRQAQEEA-ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQrALQALEELRLQAEEAERRLRQAEVERARQ 1567
Cdd:COG5283 198 EAQQKLSQALSARlERLQESRTQMSQSSGQLGKRLETDKAGAGALGLLGA-ALAGSFAAIGAAVRRTAQMNGELMDKTKQ 276
|
250 260 270
....*....|....*....|....*....|....*...
gi 530389149 1568 VQVALETAQR--SAEAELQSKRASFAEKTAQLERSLQE 1603
Cdd:COG5283 277 VKGARDNLGKvtSQGEEMSDAIQETAEHIKDSGRELSK 314
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1436-1745 |
1.46e-03 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 44.36 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1436 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRA--RAEEAEAQKRQAQEEAERLRRQVQDESQ 1513
Cdd:COG3206 130 DPTIFEISYRLDDLLESLKVLRAGRSRVIELSYTSNDPKLAAKLANALAQayLADQLEAQLEAFRRASDSLDERLEELRA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1514 RKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAElqskRASFAEK 1593
Cdd:COG3206 210 RLQEAEAQVEDFRAQHGLTDAARGQLLSEQQLSALNTQLQSARARLAQAEARLASLLQLLPLGREAAAL----REVLESP 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1594 TAQlerSLQEEHVAVAQLREEAERraqqqaeaerareeaerelerwQLKAN--EALRLRLQAEEVAQQkslaqaeaekqK 1671
Cdd:COG3206 286 TIQ---DLRQQYAQVRQQIADLST----------------------ELGAKhpQLVALEAQLAELRQQ-----------I 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1672 EEAEREARRRGKAEEQAVRQRelaEQELEKQRQLAEGTAQQRLAAEQELIRLraeTEQGEQQRQLLEEELARLQ 1745
Cdd:COG3206 330 AAELRQILASLPNELALLEQQ---EAALEKELAQLKGRLSKLPKLQVQLREL---EREAEAARSLYETLLQRYQ 397
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
2185-2378 |
1.53e-03 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 44.36 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2185 QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIlrdk 2264
Cdd:COG3206 212 QEAEAQVEDFRAQHGLTDAARGQLLSEQQLSALNTQLQSARARLAQAEARLASLLQLLPLGREAAALREVLESPTI---- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2265 dntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAlaekmlkekmQAVQEATRLKAEAELLQQQKELA 2344
Cdd:COG3206 288 ---QDLRQQYAQVRQQIADLSTELGAKHPQLVALEAQLAELRQQIAA----------ELRQILASLPNELALLEQQEAAL 354
|
170 180 190
....*....|....*....|....*....|....
gi 530389149 2345 QEQARRLQEDKEQMAQQLAEETQgFQRTLEAERQ 2378
Cdd:COG3206 355 EKELAQLKGRLSKLPKLQVQLRE-LEREAEAARS 387
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1356-1549 |
1.54e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1356 AEQQRAEERERlaEVEAALEKQRqlaeahAQAKAQAEREAKELQQrmqeevVRREEAAVDAQQQKRsiqeelqqlrqsSE 1435
Cdd:PTZ00491 667 AARHQAELLEQ--EARGRLERQK------MHDKAKAEEQRTKLLE------LQAESAAVESSGQSR------------AE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1436 AEIQAKARQAEAaersrlriEEEIRVVRLQLEAterQRGGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDESQr 1514
Cdd:PTZ00491 721 ALAEAEARLIEA--------EAEVEQAELRAKA---LRIEAEAELEKLRKRQElELEYEQAQNELEIAKAKELADIEAT- 788
|
170 180 190
....*....|....*....|....*....|....*..
gi 530389149 1515 KRQAEVELASR--VKAEAEAAREKQRALqaLEELRLQ 1549
Cdd:PTZ00491 789 KFERIVEALGRetLIAIARAGPELQAKL--LGGLGLK 823
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2197-2415 |
1.57e-03 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 44.17 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2197 RLQLEETDHQKNllDEELQRLKAEATEAARQRSQVEEELFSV--RVQMEELSKLKARIEAENRALiLRDKDNTQRFLQEE 2274
Cdd:COG3064 66 RIQSQQSSAKKG--EQQRKKKEEQVAEELKPKQAAEQERLKQleKERLKAQEQQKQAEEAEKQAQ-LEQKQQEEQARKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2275 AEKMKQVAEEAARlsvAAQEAARLRQLAEedlAQQRALAEKMLKEKMQAVQEATRLKAEAEllqQQKELAQEQARRLQED 2354
Cdd:COG3064 143 AEQKKKAEAAKAK---AAAEAAKLKAAAE---AKKKAEEAAKAAEEAKAKAEAAAAKKKAE---AEAKAAAEKAKAEAEA 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530389149 2355 KEQMaqqlaeetqgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQA 2415
Cdd:COG3064 214 KAKA---------------EKKAEAAAEEKAAAEKKKAAAKAKADKAAAAAKAAERKAAAA 259
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1159-1459 |
1.58e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 44.88 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1159 RGAQEvgERLQQRHGERDVEVERWRERV--AQLLERWQAVLAQ------TDVRQRELEQLGRQLRYYRESAD-PLGAWLQ 1229
Cdd:COG3096 780 RAARE--QRLESLHAERDVLSERHATLSfdVQKTQRLHQAFSRfigshlAVAFEADPEAEIRQLNSRRNELErALSNHEN 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1230 DARRRQEQI----QAMPLADSQAVREQLRQEQAL---LEEIERHGEKVEECQRFAKQYINAIkdyelqlvtykAQLEPVA 1302
Cdd:COG3096 858 DNQQQRIQFdqakEGVTALNRLIPQLNLLADESLadrVEEIRERLDEAQEAARFIQQHGNTL-----------SKLEPIA 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1303 S-----PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAE----ERERLAEVEA 1372
Cdd:COG3096 927 SvlqsdPEQFEQLKEDYAQAQQMQRQARQQAFALTEVVQRRAHFsYSDSAEMLSENSDLNEKLRQRleqaEAERTRAREQ 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1373 ALEKQRQLAE-----AHAQAKAQAEREA-KELQQRMQEEVVRREEAAVD-AQQQKRSIQEELQQLRQ----------SSE 1435
Cdd:COG3096 1007 LRQHQAQLSQynqvlASLKSSYDTKKELlNELQQELQDIGVRADSGAEErARIRRDELHAQLSTNRSrrnqlekqltFCE 1086
|
330 340
....*....|....*....|....
gi 530389149 1436 AEIQAKARQAEAAERSRLRIEEEI 1459
Cdd:COG3096 1087 AEMDNLTRKLRKLERDYFEMREQV 1110
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1691-2376 |
1.63e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1691 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR---QLLEEELARLQREAAAATQKRQELEAELAKVR- 1766
Cdd:PRK10246 232 EKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpQLAALSLAQPARQLRPHWERIQEQSAALAHTRq 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1767 --AEMEVLLASKARAEEESRSTSEKSKQRLEAEAG----------RFRELAEEAARLRALAEEAKRQRQlaEEDAARQRA 1834
Cdd:PRK10246 312 qiEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslntwlaehdRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1835 EAERvlaEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLaedeafqRRRLEEQAAQHkADIEERLAQLrKASDSELERQ 1914
Cdd:PRK10246 390 THAE---QKLNALPAITLTLTADEVA--AALAQHAEQRPL-------RQRLVALHGQI-VPQQKRLAQL-QVAIQNVTQE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1915 KGLVEDTLRQRRQveeeilALKASFEKAAAGKAELELElGRIRSNAEdtlrskEQAELEAARQRQLAAEEERRRreaeer 1994
Cdd:PRK10246 456 QTQRNAALNEMRQ------RYKEKTQQLADVKTICEQE-ARIKDLEA------QRAQLQAGQPCPLCGSTSHPA------ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1995 VQKSLAAEEEAARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQT 2073
Cdd:PRK10246 517 VEAYQALEPGVNQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2074 LQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQsrRQVEEAErlKQSAEEQAQARAQAQAAAEKLRKEAEQEAAR 2153
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHN--QQIIQYQ--QQIEQRQQQLLTALAGYALTLPQEDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2154 RAqaeqaalrqkQAADAEMEKHKKFAEQTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--ATEAARQRSQ 2230
Cdd:PRK10246 668 AT----------RQQEAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQclSLHSQLQTLQ 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2231 VEEELFSVRVQmeelsKLKARIEAENRALILRDKDNTQRFLQEEaEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2310
Cdd:PRK10246 738 QQDVLEAQRLQ-----KAQAQFDTALQASVFDDQQAFLAALLDE-ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 2311 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2376
Cdd:PRK10246 812 QHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2260-2467 |
1.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2260 ILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2333
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2334 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQR 2410
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 2411 FRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL 2467
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1691-2469 |
1.71e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1691 QRELAEQE-----LEKQRQLAE---GTAQQRLAAEQELIRLRAE----TEQGEQQRQLLE---EELARLQREAAAATQKR 1755
Cdd:PRK04863 313 ARELAELNeaesdLEQDYQAASdhlNLVQTALRQQEKIERYQADleelEERLEEQNEVVEeadEQQEENEARAEAAEEEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1756 QELEAELAKVRAEMEVLlASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ-----RQLAEEDAA 1830
Cdd:PRK04863 393 DELKSQLADYQQALDVQ-QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEllsleQKLSVAQAA 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1831 RQRAEAERVLAEKLAaiGEATRlkTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASD 1908
Cdd:PRK04863 472 HSQFEQAYQLVRKIA--GEVSR--SEAWDVARELLRRLREQRHLAEQLQQLRMRLSelEQRLRQQQRAERLLAEFCKRLG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1909 SELERqkglvEDTLRQ-RRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdTLRSKEQAELEA----ARQRQLAAE 1983
Cdd:PRK04863 548 KNLDD-----EDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ-RLAARAPAWLAAqdalARLREQSGE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1984 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKakvEEARRLRERAEQESARQLQLA-----------------QE 2046
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLERERELTVERDELAARKQALD---EEIERLSQPGGSEDPRLNALAerfggvllseiyddvslED 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2047 AAQKRLQAEEKAHAFAVQQKEQELQQTLQqeqsvLDQLRGEAEAARRAAEEAEEARVQA-EREAAQSRRQVEEAERLKQS 2125
Cdd:PRK04863 699 APYFSALYGPARHAIVVPDLSDAAEQLAG-----LEDCPEDLYLIEGDPDSFDDSVFSVeELEKAVVVKIADRQWRYSRF 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2126 AEEQAQARAQAQAAAEKLRKEAEQEAARRAQAE---QAALRQKQAADAEMEKHKKFAEQtlrqkAQVEQELTTLRLQLEE 2202
Cdd:PRK04863 774 PEVPLFGRAAREKRIEQLRAEREELAERYATLSfdvQKLQRLHQAFSRFIGSHLAVAFE-----ADPEAELRQLNRRRVE 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2203 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEElsKLKARIEaENRALILRDKDNtQRFLQEEAEKMKQVA 2282
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE--TLADRVE-EIREQLDEAEEA-KRFVQQHGNALAQLE 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2283 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQ-----AVQEATRLKAEA----ELLQQQKELAQEQARRL 2351
Cdd:PRK04863 925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfaLTEVVQrrahfSYEDAAEMLAKNsdlnEKLRQRLEQAEQERTRA 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2352 QEDKEQMAQQLAEETQgFQRTLEAERQRQLEMSAEAERlklrvaEMSRAQARAEEDA-QRFRKQAEEIGEKLHRTELATQ 2430
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQ-VLASLKSSYDAKRQMLQELKQ------ELQDLGVPADSGAeERARARRDELHARLSANRSRRN 1077
|
810 820 830
....*....|....*....|....*....|....*....
gi 530389149 2431 EkvtLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ 2469
Cdd:PRK04863 1078 Q---LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2376-2700 |
1.74e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2376 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2436
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2437 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEKDSLLQRERFIEQ 2516
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2517 EKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqQRRQQEELLAEEN 2596
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----------LRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2597 QrLREQLQLLEEQ-HRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQ 2675
Cdd:TIGR02168 397 S-LNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*
gi 530389149 2676 RLAQGHTTVDELARREDVRHYLQGR 2700
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQEN 500
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1476-1585 |
1.76e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1476 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEElRLQA 1550
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE-ELEK 114
|
90 100 110
....*....|....*....|....*....|....*
gi 530389149 1551 EEAERRLRQAEVERARQVqvaLETAQRSAEAELQS 1585
Cdd:PRK12704 115 KEKELEQKQQELEKKEEE---LEELIEEQLQELER 146
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1347-1559 |
1.77e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 43.39 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1347 RRMEEEERLaeQQRAEERERlaeVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrreeaavdAQQQKrsiqEE 1426
Cdd:pfam00769 7 EKQELEERL--KQYEEETRK---AQEELEESEETAELLEEKLRVAEEEAELLEQKAQE-----------AEEEK----ER 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1427 LQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAERLRR 1506
Cdd:pfam00769 67 LEESAEMEAEEKEQLERELREAQEEVARLEEESE--RKEEEAERLQE-------ELEEAREEEEEAKEKLLAASTSPSHH 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1507 QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1559
Cdd:pfam00769 138 HSEESENEDDEEEEESYEGGSAELSNDGDMDQLSDRIEEERVTEAEKNERLQK 190
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1693-1867 |
1.78e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1693 ELAEQELEKQRQLAEGTAqqrLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE-LAKVRAEMEV 1771
Cdd:PHA03247 1552 ERVDQSPVKDTAYAEYVA---FVARRDLAEAKDALVRAKQQRAEATDRVTAALREALAAHERRAQSEAEsLANLKTLLRV 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1772 --LLASKARAEEESRSTSEKSKQrLEAeagrFRELAEEAARLRALA----EEAKRQRQLAEEDAARQRAEAERV-LAEKL 1844
Cdd:PHA03247 1629 aaIPATAAKTLDQARSVAEIVDQ-IEL----LLEQTEKAAELDVAAvdwlEHARRVFEAHPLTAARGGGPDPLArLHARL 1703
|
170 180
....*....|....*....|...
gi 530389149 1845 AAIGEATRLKTEAEIALKEKEAE 1867
Cdd:PHA03247 1704 DALGETRRRTEALRRSLEAAEAE 1726
|
|
| DivIVA |
COG3599 |
Cell division septum initiation DivIVA, interacts with FtsZ, MinD and other proteins [Cell ... |
1369-1604 |
1.92e-03 |
|
Cell division septum initiation DivIVA, interacts with FtsZ, MinD and other proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226127 [Multi-domain] Cd Length: 212 Bit Score: 42.81 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1369 EVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDaqqqkrSIQEELQQLRQSSEAEIQAKARQAEAA 1448
Cdd:COG3599 27 EVDEFLDDVIDDYEQLLDENEDLEDEIDELKEELKEAADAEDSQAIQ------QAETEAEELKQAAEAEADDILKRASAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1449 ERsrlrieeeiRVVRLQLEATERQRGGAegelqalrARAEEAEAQKRQAQEEAERLRRQVqdesqrkrqaevelasrvka 1528
Cdd:COG3599 101 AQ---------RVFGKAQYKADRYLEDA--------KIAQELEDLKRQAQVERQRLRSDI-------------------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1529 eaEAAREKQRALQALEELRLQAEEAERRLRQAeverarqvQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEE 1604
Cdd:COG3599 144 --EAQLASAKQEDWDEILRSTVDEVEAANEEA--------ERLADAAQADADRLRDECDIYVDTKLAELETRLSGT 209
|
|
| YloA |
COG1293 |
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ... |
1690-1837 |
1.93e-03 |
|
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224212 [Multi-domain] Cd Length: 564 Bit Score: 44.31 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1690 RQRELAEQELEKQRQLaegtaqqrlaaEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEM 1769
Cdd:COG1293 276 ERDKIKQLASELEKKL-----------EKELKKLENKLEKQEDELEELEKAAEELRQKGELLYANLQLIEEGLKSVRLAD 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1770 EVLLASKARAEEESRS---------TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAE 1837
Cdd:COG1293 345 FYGNEEIKIELDKSKTpsenaqryfKKYKKLKGAKVNLDRQLSELKEAIAYYESAKTALEKaeGKKAIEEIREELIEEG 423
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1347-1603 |
1.93e-03 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 43.75 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1347 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREakelqqrmqeevvrREEAAVDAQQQKRSIQE 1425
Cdd:pfam00038 28 KDLETKISELRQKKGAEPSRLYSLyEREIRELRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1426 ELQqLRQSSEAEIQAKARQAEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQAQEEAERLR 1505
Cdd:pfam00038 94 ELN-LRQSAEADIVGLRKDLDEATLARVDLEMKI---------------------ESLK---EELAFLKKNHEEEVRELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1506 RQVQDESqrkRQAEV------ELAS-----RVKAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEVERA---RQ 1567
Cdd:pfam00038 149 SQVSDTQ---VNVEMdaarklDLTSalaeiRAQYEEIAEKNREEAeewyQSKLEELQQAAARNGDALRSAKEEITelrRQ 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 530389149 1568 VQ-------------VALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1603
Cdd:pfam00038 226 IQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQQ 274
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2243-2371 |
1.96e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2243 EELSKLKARIEAENRALILRDKDNTQrfLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2322
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530389149 2323 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAEETQGFQR 2371
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
71-146 |
1.98e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.28 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 71 LYEDLRDGHNLISLLEvlsgDSLP-------------REKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 137
Cdd:cd21294 38 LFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113
|
....*....
gi 530389149 138 TLGLIWTII 146
Cdd:cd21294 114 ILGLIWQII 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2185-2527 |
2.08e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2185 QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENralilrDK 2264
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI------DK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2265 DNTQRFLQEEaekmkqvaeeaaRLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ-K 2341
Cdd:TIGR04523 192 IKNKLLKLEL------------LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2342 ELAQEQarrlQEDKEQMAQQLAEETQGFQRTLEAERQRQlEMSAEAERLKlrvaemsraqaraeedaqrfrKQAEEIGEK 2421
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN---------------------NQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2422 LHRTELATQEKVtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvqqeqllqetqaLQQSFL 2501
Cdd:TIGR04523 311 ELKSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN------------EIEKLK 376
|
330 340
....*....|....*....|....*.
gi 530389149 2502 SEKDSLLQRERFIEQEKAKLEQLFQD 2527
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN 402
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1420-1566 |
2.09e-03 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 43.12 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1420 KRSIQEELQQLRQSSEA---EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQALRARA 1487
Cdd:COG1579 26 IKEIRKALKKAKAELEAlnkALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAVkderelralNIEIQIAKERI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1488 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELA---SRVKAEAEAAREKQRALQAlEELRLQAEEAERRLrqAEVER 1564
Cdd:COG1579 106 NSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAeaeARLEEEVAEIREEGQELSS-KREELKEKLDPELL--SEYER 182
|
..
gi 530389149 1565 AR 1566
Cdd:COG1579 183 IR 184
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1377-1539 |
2.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1377 QRQLAEAHAQAK---AQAEREAKELQQRM----QEEVVR-REEAAVDAQQQKRSIQEELQQLRQSSEAEiqakARQAEAA 1448
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAIKKEAlleaKEEIHKlRNEFEKELRERRNELQKLEKRLLQKEENL----DRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1449 ERSrlriEEEIRVVRLQLEATERqrggaegELQALRARAEEAEAQKRQA--------QEEA-ERLRRQVQDESQRkrqae 1519
Cdd:PRK12704 106 EKR----EEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEEARH----- 169
|
170 180
....*....|....*....|..
gi 530389149 1520 vELASRVKAEAEAARE--KQRA 1539
Cdd:PRK12704 170 -EAAVLIKEIEEEAKEeaDKKA 190
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
44-146 |
2.27e-03 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 41.50 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 44 QKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALD 113
Cdd:cd21292 25 EKVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALN 102
|
90 100 110
....*....|....*....|....*....|...
gi 530389149 114 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 146
Cdd:cd21292 103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2338-2619 |
2.30e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2338 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2417
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRK----LEEAEKARQ----AEMDRQAAIYAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2418 I-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDhdaERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQA 2495
Cdd:pfam17380 360 ReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2496 LQQsflsekdslLQRERFIEQEKAKLEQLFQDEvakaqqlREEQQRQQQQMEQERQRlvaSMEEARRRQHEAEEgVRRKQ 2575
Cdd:pfam17380 437 VRR---------LEEERAREMERVRLEEQERQQ-------QVERLRQQEEERKRKKL---ELEKEKRDRKRAEE-QRRKI 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 530389149 2576 EELQQLEQQRRQQeellaeENQRLREQLQLLEEQHRAALAHSEE 2619
Cdd:pfam17380 497 LEKELEERKQAMI------EEERKRKLLEKEMEERQKAIYEEER 534
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2162-2383 |
2.50e-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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 43.36 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2162 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQ-VEEELFSVRV 2240
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEDLRILEYLKEKAEREEEREAERREIKEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2241 QMEELSKLKARIEAENRALILRDKdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--- 2317
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKWRQK---EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEdee 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 2318 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEM 2383
Cdd:pfam13868 276 IEQEEAEKRREKRLEHRRELEKQIEERERQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1476-1559 |
2.59e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1476 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVElasrvKAEAEAAREKQralQALEELRLQAEEAER 1555
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-----EAKEEAERILE---QAKAEIEQEKEKALA 113
|
....
gi 530389149 1556 RLRQ 1559
Cdd:cd06503 114 ELRK 117
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1374-1552 |
2.76e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1374 LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrl 1453
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1454 rieeeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEVELASRVKAEAEaa 1533
Cdd:PRK12705 100 ------------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180
....*....|....*....|
gi 530389149 1534 REK-QRALQALEELRLQAEE 1552
Cdd:PRK12705 157 EEKaQRVKKIEEEADLEAER 176
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1480-1604 |
2.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1480 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELasrvKAEAEaarekQRALQALEELRLQAEEAERRLRQ 1559
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530389149 1560 AEVERARQVqvaletaqrsAEAELQSKRASFAEKTAQLERSLQEE 1604
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1808-1952 |
2.96e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1808 AARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 1887
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1888 QAAQ------HKADIEERLAQLRKASDSELERQKGLVEDTLRQR--RQVEEEILALKASFEKAAAGKAELELE 1952
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1414-1560 |
3.15e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1414 VDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvvrlqleaterqrggAEGELQALRARAEEAEAQ 1493
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530389149 1494 KRQAQEEAERLRRQVQDESQRKRQaevelasrvkaeaeaaREKQRALQALEELRLqaEEAERR------LRQA 1560
Cdd:PRK11448 193 QQELEAQLEQLQEKAAETSQERKQ----------------KRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1347-1436 |
3.22e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1347 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAH-------AQAKAQAEREAKE-LQQRMQEEVVRREEAAVDAQ 1417
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARkqaqaviAEAEAEADKLAAEaLAEAQAEAQASKEKARREIE 111
|
90
....*....|....*....
gi 530389149 1418 QQKrsiQEELQQLRQSSEA 1436
Cdd:PRK07353 112 QQK---QAALAQLEQQVDA 127
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2694-2731 |
3.30e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.30e-03
10 20 30
....*....|....*....|....*....|....*...
gi 530389149 2694 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 2731
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump [Defense mechanisms]; |
1354-1470 |
3.50e-03 |
|
Multidrug resistance efflux pump [Defense mechanisms];
Pssm-ID: 224482 [Multi-domain] Cd Length: 352 Bit Score: 43.09 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1354 RLA-EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQE----EVVRREEAAvDAQQQKRSIQEELQ 1428
Cdd:COG1566 90 RAAlEQAEAALAAAEAQLRNLRAQLASAQALIAQAEAQDLDQAQNELERRAElaqrGVVSREELD-RARAALQAAEAALA 168
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530389149 1429 QLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE 1470
Cdd:COG1566 169 AAQAAQKQNLALLESEVSGAQAQVASAEAALDQAKLDLERTV 210
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1683-1932 |
3.54e-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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1683 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAaaatqkRQELEAEL 1762
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEE------DLRILEYL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1763 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELaeEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1842
Cdd:pfam13868 162 KEKAEREEEREAERREIKEEKEREIARLRAQQEKAQDEKAER--DELRAKLYQEEQERKWRQKEREEAEKKARQRQELQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1843 KLAAIGEATRLKTEAEIALKEKEAEN--ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLA---QLRKASDSELERQKGL 1917
Cdd:pfam13868 240 AREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRREKRLEHRRELEKQIEereRQRAAEREEELEEGER 319
|
250
....*....|....*
gi 530389149 1918 VEDTLRQRRQVEEEI 1932
Cdd:pfam13868 320 LREEEAERRERIEEE 334
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1107-1603 |
3.58e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1107 EEVLRAHEEQLKEAQAVPATL-PELEATKASL-------KKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVE 1178
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLtKELEDIKMSLqrsmstqKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1179 VERWRERVAQLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQA 1258
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKN---EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1259 LLEEIErhgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqEYVDLRTHYSELTTLTSQY 1338
Cdd:pfam05483 430 IAEELK---GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL--KNIELTAHCDKLLLENKEL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1339 IKFISE-TLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRM---QEEVVRREEAAV 1414
Cdd:pfam05483 505 TQEASDmTLELKKHQEDIINCKKQEER-MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLdksEENARSIEYEVL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1415 DAQQQKRSIQEELQQLRQS--------SEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-ATERQRGG-------AEG 1478
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQienknkniEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKFEeiidnyqKEI 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1479 ELQALRARAEEAEAQKRQA-QEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERrl 1557
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAiADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK-- 741
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 530389149 1558 rqaeverarqvqVALETAQRSAEAELQSKRASFA---EKTAQLERSLQE 1603
Cdd:pfam05483 742 ------------AALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKE 778
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1341-1557 |
3.62e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 281941 [Multi-domain] Cd Length: 218 Bit Score: 41.98 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1341 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAKELQQRMQEEVVRREEAAVDAQQQ- 1419
Cdd:pfam04012 13 NIHEGLDKAEDPEKMLEQAIRDMQSELGKAR------QALAQVIARQK-QLERKLEEQKEQAKKLENKARAALTKGNEEl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1420 KRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1499
Cdd:pfam04012 86 AREALAEIATLEKLAEALETQLTQQRSAVEQ-----------LRKQLAALETKIQQLKAKKTALKARLKAAKAQEAVNTS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1500 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRaLQALEELRLQAEEAERRL 1557
Cdd:pfam04012 155 LGSASTESATDSFERIEEKIEEREARADAAAELASAQDL-DAKLEAAGIQMEVSEDVL 211
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2164-2532 |
3.76e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2164 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKnlldEELQRLKAEATEAARQrsQVEEELFSVRVQME 2243
Cdd:pfam09731 98 SSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKA----ESATAVAKEAKDDAIQ--AVKAHTDSLKEASD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2244 --ELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA------LAEK 2315
Cdd:pfam09731 172 taEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLaklvdqYKEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2316 MLKEKMQAVQEATRLkaEAELLQQQKELAQEQARRL-------QEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEA 2387
Cdd:pfam09731 252 VASERIVFQQELVSI--FPDIIPVLKEDNLLSNDDLnsliahaHREIDQLSKKLAElKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2388 ERLKLR---VAEMSRAQARAEEDAQRFRkQAEEIGEKLhRTELATQEKV---TLVQTLEIQRQQSDHDAERLREAIAELE 2461
Cdd:pfam09731 330 EELSARleeVRAADEAQLRLEFEREREE-IRESYEEKL-RTELERQAEAheeHLKDVLVEQEIELQREFLQDIKEKVEEE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2462 REKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQ---------SFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 2532
Cdd:pfam09731 408 RAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQlwlavealrSTLEDGSADSRPRPLVRELKALKELASDDEVVKA 487
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
1348-1518 |
3.79e-03 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 43.15 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1348 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1427
Cdd:COG1322 14 LVNLAFIRQLLLRLGRLEQMLGELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLELIQELNELKARLQQQLLQSREQL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1428 QQLRQSSEAEIQAKARQAEaaersRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK-RQAQEEAERLRR 1506
Cdd:COG1322 94 QLLIESLAQLSSEFQELAN-----EIFEELNRRLAELNQQNLKQLLKPLREVLEKFREQLEQRIHESaEERSTLLEEIDR 168
|
170
....*....|..
gi 530389149 1507 QVQDESQRKRQA 1518
Cdd:COG1322 169 LLGEIQQLAQEA 180
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1349-1429 |
3.79e-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: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1349 MEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAH-------AQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQ 1419
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEyEEKLAEARaeaqeiiEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQE 107
|
90
....*....|
gi 530389149 1420 KRSIQEELQQ 1429
Cdd:cd06503 108 KEKALAELRK 117
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2171-2518 |
3.97e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 434900 [Multi-domain] Cd Length: 384 Bit Score: 43.13 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2171 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNL--------LDEELQRLKAEATEAARQRSQVEEELFSVRVQM 2242
Cdd:pfam15742 6 KLKYQQQEEVQQLRQDLQRLQILCTSAERELRYEREKNLdlkqhnslLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2243 EElSKLKARiEAENRALILRDKDNTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDlaqQRALAEKMLKEKM 2321
Cdd:pfam15742 86 EH-CQQKIR-ELELEVLKQAQSIKSQNSLQEKLAQEKsKVADAEKKILELQQKLEHAHKVCLTE---TCILEKKQLEEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2322 QAVQEatrlkAEAELLQQQKElaQEQARRLQEDKEQMAQQlaeetqgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQ 2401
Cdd:pfam15742 161 KEAQE-----NEAKLKQQYQE--EQQKRKLLDQNVNELQQ--------QVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2402 ARAE-EDAQRFRKQAEEIGEKLHRTElatQEKVTLVQTLEIQRQQSDHDAERLREAI----AELEREKEKLQQEAKLL-- 2474
Cdd:pfam15742 226 LENEkRKSDEHLKSNQELSEKLSSLQ---QEKEALQEELQQVLKQLDVHVRKYNEKHhhhkAKLRRAKDRLVHEVEQRde 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530389149 2475 QLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQ-----RERFIEQEK 2518
Cdd:pfam15742 303 RIKQLENEIRILRQQIEKEKAFQKQVTAENDTLLLekrklLEQLTEQEE 351
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1231-1567 |
3.99e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1231 ARRRQEQIQAMpLADSQAVREQLRQE-QALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVaspakkpk 1309
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDEL-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1310 vqsgsESVIQEYVDLRTHYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1388
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1389 AQ--------AEREAKELQQRMQEEVVRREEAAVD-AQQQKRSIQEELQQLRQSSEAEIQAKArqaeaaersrlRIEEEI 1459
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKK-----------YVEKNL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1460 RVVRLQLEATERQRGGAEGELQALRAR---AEEAEAQKRQAQEEAERLRRQVQDESQR---KRQAEVELASRVKaeaeaa 1533
Cdd:pfam06160 294 PEIEDYLEHAEEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDEIVERleeKEVAYSELQEELE------ 367
|
330 340 350
....*....|....*....|....*....|....
gi 530389149 1534 rEKQRALQALEELRLQAEEAERRLRQAEvERARQ 1567
Cdd:pfam06160 368 -EILEQLEEIEEEQEEFKESLQSLRKDE-LEARE 399
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1350-1533 |
4.08e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1350 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAV-DAQQQKRSIQEELQ 1428
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIaRAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1429 QLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQAQEEAErlrrqv 1508
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*.
gi 530389149 1509 QDESQRKrqAEVELA-SRVKAEAEAA 1533
Cdd:PRK05035 671 EAEDPKK--AAVAAAiARAKAKKAAQ 694
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2183-2480 |
4.30e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2183 LRQKAQVEQ-ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFsvrvQMEELSKLKARIEAEnraliL 2261
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2262 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2341
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2342 ELAQEQARRLQEDKEQMAQQLAEET--QGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2419
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2420 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2467
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 530389149 2468 QQEAKllQLKSEE 2480
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2213-2474 |
4.34e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.36 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2213 ELQRLKAEATEAARQRSQVEEElfsvrvqmEELSKLKARIEAEN-RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVA 2291
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEE--------ANFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2292 AQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQgf 2369
Cdd:pfam15964 397 EREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH-- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2370 qRTLEAERQRQLEMS-AEAERLKL-------RVAEMSRAQARAEEDAQRFrkqAEEIGEKLHRTELATQEKVTLVQTL-- 2439
Cdd:pfam15964 473 -REYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREECLKL---TELLGESEHQLHLTRLEKESIQQSFsn 548
|
250 260 270
....*....|....*....|....*....|....*..
gi 530389149 2440 --EIQRQQSDHDAERLREAIAELEREKEKLQQEAKLL 2474
Cdd:pfam15964 549 eaKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSL 585
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2276-2370 |
4.35e-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: 397124 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2276 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2349
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 530389149 2350 RLQEDKEQMAQQLAEETQGFQ 2370
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
1343-1526 |
4.38e-03 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 42.88 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1343 SETLRRMEEEERLAEQQRAEERERLAEVEAalEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRS 1422
Cdd:COG4487 38 SRILNTLEEFEKEANEKRAQYRSAKKKELS--QLEEQLINQKKEQKNLFNEQIKQFELALQDEIAKLEALELLNLEKDKE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1423 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1502
Cdd:COG4487 116 LELLEKELDELSKELQKQLQNTAEIIEKKRENNKNE---ERLKFENEKKLEESLELEREKFEEQLHEANLDLEFKENEEQ 192
|
170 180
....*....|....*....|....*.
gi 530389149 1503 R--LRRQVQDESQRKRQAEVELASRV 1526
Cdd:COG4487 193 ResKWAILKKLKRRAELGSQQVQGEA 218
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1551-1887 |
4.43e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1551 EEAERRLRQAEVERARqvqvaLETAQRSAEAELQSKRASFAE----KTAQLERS---LQEEHVAVAQLREEAERRAQQQA 1623
Cdd:pfam03528 4 EDLQQRVAELEKENAE-----FYRLKQQLEAEFNQKRAKFKElylaKEEDLKRQnavLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1624 EAERAREEAerelERWQLKANEALRLRLQaEEVAqqkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL-EKQ 1702
Cdd:pfam03528 79 NIKAVATVS----ENTKQEAIDEVKSQWQ-EEVA---SLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIaDLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1703 RQLAEGTAQQRLaaEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAelAKVRAEMEVLLASKA-RAEE 1781
Cdd:pfam03528 151 RRLSEGQEEENL--EDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEA--SKMKELNHYLEAEKScRTDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1782 ESR-STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL---AEKLAAIGEATRLKTEA 1857
Cdd:pfam03528 227 EMYvAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLmrdMQRMESVLTSEQLRQVE 306
|
330 340 350
....*....|....*....|....*....|
gi 530389149 1858 EIALKEKEaENERLRRLAEDEAFQRRRLEE 1887
Cdd:pfam03528 307 EIKKKDQE-EHKRARTHKEKETLKSDREHT 335
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1113-1611 |
4.44e-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: 43.27 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1113 HEEQLKEAQAVPATLPELEatkaslkklrAQAEAQQPTFDAlRDElrGAQEVGERLQQRHGERDVEVERWrERVAQLLEr 1192
Cdd:pfam10174 125 HERQAKELFLLRKTLEEME----------LRIETQKQTLGA-RDE--SIKKLLEMLQSKGLPKKSGEEDW-ERTRRIAE- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1193 WQAVLAQTDVrqrELEQLGRQLRYYRESAdplgawlqdarRRQEQIQAMPlADSQAVREQLRQEQALLEEIERHGEKVEE 1272
Cdd:pfam10174 190 AEMQLGHLEV---LLDQKEKENIHLREEL-----------HRRNQLQPDP-AKTKALQTVIEMKDTKISSLERNIRDLED 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1273 CQRFAKQyiNAIKDYELQLVTYKaQLEPVASPAK--KPKVQSGSESVIQEYVDLRTHYSELTTLTS------QYIKFISE 1344
Cdd:pfam10174 255 EVQMLKT--NGLLHTEDREEEIK-QMEVYKSHSKfmKNKIDQLKQELSKKESELLALQTKLETLTNqnsdckQHIEVLKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1345 TLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQA-------------EREAKELQQRMQ--EEVVR 1408
Cdd:pfam10174 332 SLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEKSTLAgeirdlkdmldvkERKINVLQKKIEnlQEQLR 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1409 reeaavDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEA-------AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ 1481
Cdd:pfam10174 412 ------DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAlsekeriIERLKEQREREDRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1482 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAER-RLRQA 1560
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQ 565
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1561 EV----ERARQVQVALE---TAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1611
Cdd:pfam10174 566 EVarykEESGKAQAEVErllGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI 623
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
2247-2527 |
4.45e-03 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 43.05 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2247 KLKARIEAENRaLILRDKDNtqrfLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAlAEKMLKEKMQAVQE 2326
Cdd:COG5185 257 ELKLGFEKFVH-IINTDIAN----LKTQNDNLYEKIQEAMKISQKIKTLREKWRALKSDSNKYEN-YVNAMKQKSQEWPG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2327 A-TRLKAEAELLQQQKELAQEQARRLQEDKEQmaQQLAEETQGFQRTLEAERQRQLE-MSAEAERLKLRVAEMSR-AQAR 2403
Cdd:COG5185 331 KlEKLKSEIELKEEEIKALQSNIDELHKQLRK--QGISTEQFELMNQEREKLTRELDkINIQSDKLTKSVKSRKLeAQGI 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2404 AEEDAQRFRK-----------------------------QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDH-----D 2449
Cdd:COG5185 409 FKSLEKTLRQydsliqnitrsrsqighnvndsslkinieQLFPKGSGINESIKKSILELNDEIQERIKTEENKSitleeD 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2450 AERLREAIAELEREKEKLQ-------QEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLE 2522
Cdd:COG5185 489 IKNLKHDINELTQILEKLElelseanSKFELSKEENERELVAQRIEIEKLEKELNDLNLLSKTSILDAEQLVQSTEIKLD 568
|
....*
gi 530389149 2523 QLFQD 2527
Cdd:COG5185 569 ELKVD 573
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1377-1542 |
4.49e-03 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1377 QRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAER-SRLRI 1455
Cdd:pfam00529 53 PTDYQAALDSAEAQL-AKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDlARRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1456 EEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqAEVElASRVKAEAEAAR 1534
Cdd:pfam00529 132 LAPIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQI-AEAE-AELKLAKLDLER 209
|
....*...
gi 530389149 1535 EKQRALQA 1542
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1412-1850 |
4.52e-03 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 43.09 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1412 AAVDAQQQKRSIQEEL---QQLRQSSEAEIQAKARQAEAAERSRlrieeeirVVRLQLEATERQRGGAEGELQALRARAE 1488
Cdd:COG5281 175 AWYAGAQETEAFNKVLiltGEYAGTTAAQLRAGAAAGITQHQAA--------EVLAQLVAAGVATAEQLGDVAQAAARFA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1489 EAEAQKrqaQEEAERLRRQVQDESQRKRQAEVELASRVKAEA-EAAREKQRALQALEELRLQAEEAERRLRQAEveRARQ 1567
Cdd:COG5281 247 SASGES---IDKTIKAFSKLTDDPVNGAKALNRQFHYLTAAQlEQIAALQRAGDTAAAAAAAAEAAAAMDDRTA--RVKE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1568 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERA---REEAERELERWQLKAN 1644
Cdd:COG5281 322 NMGTLETAWDALADAAKKMWDAVLGIGREDKQAALLAAKLAAEKLARVTAQGALNARLKLAqddLTQAELNYAAADQAAN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1645 EAlRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE-LAEQELEKQRQLAEGTAQQRLAAEQELIRL 1723
Cdd:COG5281 402 QE-GALNAREDEAEVLSTQEERRDILKNLLADAEKRTARQEELNKALAKaKILQADKAAKAYQEDILQREAQSRGKTAAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1724 RAETEQGEQQRQLLEEELARLQrEAAAATQKRQELEAELAKVRAEMEVL-LASKARAEEESRSTSEKSKQRLEAEagrfR 1802
Cdd:COG5281 481 ERSQEQMTAALKALLAFQQQIA-DLSGAKEKASDQKSLLWKAEEQYALLkEEAKQRQLQEQKALLEHKKETLEYT----S 555
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 530389149 1803 ELAEEAArlralaeEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1850
Cdd:COG5281 556 QLAELLD-------QQADRFELSAQAAGSQKERGSDLYREALAQNAAA 596
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2272-2465 |
4.73e-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: 434873 [Multi-domain] Cd Length: 521 Bit Score: 43.01 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2272 QEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKE---LAQEQA 2348
Cdd:pfam15709 326 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEeerQRQEEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2349 RRLQEDKEQMAQQLAEETQ-GFQRTL-EAERQRQLEmsaEAErlklrvaemsraqaRAEEDAQRFRKQAEEIGEKLHR-T 2425
Cdd:pfam15709 406 ERKQRLQLQAAQERARQQQeEFRRKLqELQRKKQQE---EAE--------------RAEAEKQRQKELEMQLAEEQKRlM 468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530389149 2426 ELATQEKvtlvqtLEIQRQQSDHDAERLREAIAELEREKE 2465
Cdd:pfam15709 469 EMAEEER------LEYQRQKQEAEEKARLEAEERRQKEEE 502
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1479-1826 |
4.88e-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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 42.59 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1479 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKA----EAEAAREKQRALQALEELRLQAEEAE 1554
Cdd:pfam13868 7 ELRELNSKLLAAKCNKERDAQIEEKKRIKAEEKEEERRLDEMMEEERERAleeeEEKEEERKEERKQYRQELEEQIEERE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1555 RRLRQAEVERARQVQVALETAQRSAEAELQSkrasfAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAER 1634
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAE-----AEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEDLRILEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1635 ELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRL 1714
Cdd:pfam13868 162 KEKAEREEEREAERREIKEEKEREIARLRAQQEKAQDE----------KAERDELRAKLYQEEQERKWRQKEREEAEKKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1715 AAEQELIRLRAEteQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL 1794
Cdd:pfam13868 232 RQRQELQQAREE--QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRREKRLEHRRELEKQIEERERQRAAE 309
|
330 340 350
....*....|....*....|....*....|..
gi 530389149 1795 EAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1826
Cdd:pfam13868 310 REEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1230-1426 |
5.10e-03 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 42.63 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1230 DARRRQEQIQAMPladsQAVREQLRQEQALLEEIERHGEKVE-ECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKp 1308
Cdd:COG3064 73 SAKKGEQQRKKKE----EQVAEELKPKQAAEQERLKQLEKERlKAQEQQKQAEEAEKQAQLEQKQQEEQARKAAAEQKK- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1309 kvqsgsesviQEYVDLRTHYSELTTLTSQY-IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1387
Cdd:COG3064 148 ----------KAEAAKAKAAAEAAKLKAAAeAKKKAEEAAKAAEEAKAKAEAAAAKKKAEAEAKAAAEKAKAEAEAKAKA 217
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530389149 1388 KAQAEREAKE---LQQRMQEEVVRREEAAVDAQQQKRSIQEE 1426
Cdd:COG3064 218 EKKAEAAAEEkaaAEKKKAAAKAKADKAAAAAKAAERKAAAA 259
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1694-1979 |
5.12e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1694 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1773
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1774 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAIGEAtRL 1853
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1854 KTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrqveeeil 1933
Cdd:PRK11637 170 ETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT--------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 530389149 1934 ALKASFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-------ARQRQ 1979
Cdd:PRK11637 223 GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1489-1588 |
5.39e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1489 EAEAQKRQAQEEAERLR--RQVQDESQRK-------RQAEVELASRVKAEAEA-AREKQRALQA-LEELRLQAeEAERRL 1557
Cdd:PTZ00491 671 QAELLEQEARGRLERQKmhDKAKAEEQRTkllelqaESAAVESSGQSRAEALAeAEARLIEAEAeVEQAELRA-KALRIE 749
|
90 100 110
....*....|....*....|....*....|..
gi 530389149 1558 RQAEVERARQVQVA-LETAQRSAEAELQSKRA 1588
Cdd:PTZ00491 750 AEAELEKLRKRQELeLEYEQAQNELEIAKAKE 781
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1316-1566 |
5.44e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 224455 [Multi-domain] Cd Length: 457 Bit Score: 42.85 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1316 SVIQEYVDLRTHYSELTTL--TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQ------ 1386
Cdd:COG1538 155 EVATAYFDLLAAQEQLALAeeTLAAAEEQLELAEKRYDAGLATRLDVLQAEAQLASARAQLAAaQAQLAQARNAlarllg 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1387 AKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKA------------RQAEAAERSRLR 1454
Cdd:COG1538 235 LEPGELLDAPEPEALPALPPVLPDGLPSEALARRPDILAAEAQLAAANANIGAARAaflptlsltasyGRSSTNLSGLFG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1455 IEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAR 1534
Cdd:COG1538 315 SSSRSWSVGPGLSLPIFDGGRLRARVRQAEAQYDAALAQYEQTVLTARQEVADALAALEAALEQLQALRQAVEAAQEALE 394
|
250 260 270
....*....|....*....|....*....|..
gi 530389149 1535 EKQRALQALEELRLQAEEAERRLRQAEVERAR 1566
Cdd:COG1538 395 LARERYQAGVRTLLDVLDAQRTLLQARQALLQ 426
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1351-1611 |
5.71e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1351 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRR-----------EEAAVDAQQQ 1419
Cdd:PRK10811 514 SEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAAAPKAAAATPPA-QPGLLSRffgalkalfsgGEETKPQEQP 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1420 KRSIQE--ELQQLRQSSeaeiqakaRQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1497
Cdd:PRK10811 593 APKAEAkpERQQDRRKP--------RQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEK 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1498 QEEAERLRRQVQDESQRKRQAEVELASrvkAEAEAarekqralQALEELRLQAEEAERRLRQAEVERA-RQV--QVALET 1574
Cdd:PRK10811 665 ARTQDEQQQAPRRERQRRRNDEKRQAQ---QEAKA--------LNVEEQSVQETEQEERVQQVQPRRKqRQLnqKVRIEQ 733
|
250 260 270
....*....|....*....|....*....|....*..
gi 530389149 1575 AQrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1611
Cdd:PRK10811 734 SV-AEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPL 769
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
2271-2424 |
5.76e-03 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 42.76 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2271 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAeedlaqqRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2350
Cdd:COG1322 30 LEQMLGELAAVLEQLLLLLAFRAEAEQLRTFA-------RSLQALNLELIQELNELKARLQQQLLQSREQLQLLIESLAQ 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 2351 LQEDKEQMAQQLAEETQGFQRTLEAER-QRQLEMSAEaerlklrvaEMSRAQARAEedaQRFRKQAEEIGEKLHR 2424
Cdd:COG1322 103 LSSEFQELANEIFEELNRRLAELNQQNlKQLLKPLRE---------VLEKFREQLE---QRIHESAEERSTLLEE 165
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1684-1784 |
5.92e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1684 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1763
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 530389149 1764 KvRAEMEVLLaskarAEEESR 1784
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| COG4913 |
COG4913 |
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown]; |
1155-1538 |
5.98e-03 |
|
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 227250 [Multi-domain] Cd Length: 1104 Bit Score: 43.09 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1155 RDELRGAQEVGERLQQRHG-ERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQL-------RYYRESAD--PL 1224
Cdd:COG4913 593 RWEKDDRRKLGDRSTYRLGsTNDAKVETLRETVKAMLSREDFYMIKIMRQQGEYIKLQEQAnalahiqALNFASIDlpSA 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1225 GAWLQDARRRQEQIQAMPlADSQAVREQLRQEQALLEEIER-HGEKVEEC------QRFAKQYINAIKDYELQLVTYKAQ 1297
Cdd:COG4913 673 QRQIAELQARLERLTHTQ-SDIAIAKAALDAAQTRQKVLERqYQQEVTECaglkkdLKRAAMLSRKVHSIAKQGMTGALQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1298 LEPVASpakKPKVQSGSESVIQEYVDLrthysELTTLTSQYIKFISETLRRMEEE-----ERLAEQQRAEERERLAEVEA 1372
Cdd:COG4913 752 ALGAAH---FPQVAPEQHDDIVDIERI-----EHRRQLQKRIDAVNARLRRLREEiigrmSDAKKEDTAALSEVGAELDD 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1373 ALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDaqQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSR 1452
Cdd:COG4913 824 IPEYLARLQTLTEDALPEFLARFQELLNRSSDDGVTQLLSHLD--HERALIEERIEAINDSLRRVDFNSGRYLHIDIAKQ 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1453 LRIEEEIR-VVRLQLEATERQRGGAEGELQ--ALRARAEEAEAQKRQAQEEAERLRRQVQDE--------SQRKRQAEVE 1521
Cdd:COG4913 902 PVPHDSMRtFQQALRALTSGRFVGDDGESQykALQALVGLIIDACERHDSADTRWARAVLDPrfrlefavSEREREDGSV 981
|
410
....*....|....*..
gi 530389149 1522 LASRVKAEAEAAREKQR 1538
Cdd:COG4913 982 IETYTDSQGGSGGQKEK 998
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1344-1501 |
6.00e-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: 434873 [Multi-domain] Cd Length: 521 Bit Score: 42.63 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1423
Cdd:pfam15709 368 ERAEKMREELEL-EQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQ--LQAAQERARQQQEEFRRKLQELQRKKQQEEAE 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 1424 QEELQQLRQsSEAEIQAKARQAEAAERSRlriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA-EAQKRQAQEEA 1501
Cdd:pfam15709 445 RAEAEKQRQ-KELEMQLAEEQKRLMEMAE---EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLAlEEAMKQAQEQA 519
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1386-1888 |
6.01e-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: 411407 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1386 QAKAQAEREAKELQQRMQEEVvrREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ 1465
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEI--QKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1466 LEATERQRGGAEgelqalrARAEEAEAQKRqAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEE 1545
Cdd:NF033838 132 KDTLEPGKKVAE-------ATKKVEEAEKK-AKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1546 LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAqlERSLQEEhvavaqlreeaerraqqqaEA 1625
Cdd:NF033838 204 EKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNV--ATSEQDK-------------------PK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1626 ERAREEAERELERWQLKANEAlrlrlqaeevaqqkslaqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQL 1705
Cdd:NF033838 263 RRAKRGVLGEPATPDKKENDA------------------------------------KSSDSSVGEETLPSPSLKPEKKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1706 AEgtAQQRLAAEQElirlRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevllasKARAEEESRS 1785
Cdd:NF033838 307 AE--AEKKVEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAK-------EPRNEEKIKQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1786 TSEKSKQRLeAEAGRFrelaeeaarlralaEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE 1865
Cdd:NF033838 374 AKAKVESKK-AEATRL--------------EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKP 438
|
490 500
....*....|....*....|....*
gi 530389149 1866 AENERLRRLAEDEAFQ--RRRLEEQ 1888
Cdd:NF033838 439 AEQPKAEKPADQQAEEdyARRSEEE 463
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
50-145 |
6.44e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 39.59 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 50 KWVNKHLikhWRAEAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN- 124
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYf 91
|
90 100
....*....|....*....|.
gi 530389149 125 IRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21218 92 LTPEDIVSGNPRLNLAFVATL 112
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1344-1511 |
6.60e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRA---EERERLAEVEAALEKQRQLAEAHAQ----AKAQAEREAKELqqrmqeevvrreeaavda 1416
Cdd:PRK00409 492 EIAKRLGLPENIIEEAKKligEDKEKLNELIASLEELERELEQKAEeaeaLLKEAEKLKEEL------------------ 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1417 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAersrlrIEEEIRVVRL--QLEATERQRGGAEGELQALRARAEEAEAQK 1494
Cdd:PRK00409 554 EEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE------ADEIIKELRQlqKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
170
....*....|....*..
gi 530389149 1495 RQAQEEAERLrrQVQDE 1511
Cdd:PRK00409 628 KKQKEKQEEL--KVGDE 642
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1465-1590 |
6.75e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1465 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQAL 1543
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 530389149 1544 EELR---------LQAEEAERRLRQAEVER-ARQVQVALetAQRSaeAELQSKRASF 1590
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKIADlGRRLNVAL--AQRV--QELNRYRSEF 199
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1239-1517 |
6.84e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1239 QAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpkvqsgsesvi 1318
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET---------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1319 qeyvdlRTHYSELttltsqyikfiseTLRRMEE--EERLAEQQRAeererlaeveaalekQRQLAEAHAQ---AKAQAER 1393
Cdd:PRK11281 115 ------RETLSTL-------------SLRQLESrlAQTLDQLQNA---------------QNDLAEYNSQlvsLQTQPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1394 EAKEL---QQRMQEevVRREEAAVDAQQqkRSIQEELQQLRQSSEAEIQAKA--RQAEAAERSRLrieeeIRVVRLQLEA 1468
Cdd:PRK11281 161 AQAALyanSQRLQQ--IRNLLKGGKVGG--KALRPSQRVLLQAEQALLNAQNdlQRKSLEGNTQL-----QDLLQKQRDY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530389149 1469 TERQRGGAEGELQALRA-----RAEEAEAQKRQAQEEAERLRRQ----VQDESQRKRQ 1517
Cdd:PRK11281 232 LTARIQRLEHQLQLLQEainskRLTLSEKTVQEAQSQDEAARIQanplVAQELEINLQ 289
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1414-1593 |
6.85e-03 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 41.58 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1414 VDAQQQKRSIQEELQQLrQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1493
Cdd:COG1579 3 NNNLKSLLAIQKLDLEK-DRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1494 KRQA--QEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRqAEVERARQVQVA 1571
Cdd:COG1579 82 LSAVkdERELRALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLE-EEVAEIREEGQE 160
|
170 180
....*....|....*....|..
gi 530389149 1572 LETAQRSAEAELQSKRASFAEK 1593
Cdd:COG1579 161 LSSKREELKEKLDPELLSEYER 182
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1789-1936 |
7.19e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1789 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAigEATRLKTE 1856
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1857 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALK 1936
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4286-4316 |
7.29e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 425816 Cd Length: 39 Bit Score: 36.93 E-value: 7.29e-03
10 20 30
....*....|....*....|....*....|.
gi 530389149 4286 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4316
Cdd:pfam00681 9 GGIIDPVTGERLSVEEALKRGLIDPETAQKL 39
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1692-1859 |
7.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1692 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtqkRQELEAELAKVRAEmev 1771
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKE--- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1772 llaskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1851
Cdd:PRK00409 582 -----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNK-ANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL 655
|
....*...
gi 530389149 1852 RLKTEAEI 1859
Cdd:PRK00409 656 SIPDDKEA 663
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2325-2403 |
7.57e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 42.01 E-value: 7.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530389149 2325 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAEETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2403
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
43-149 |
7.68e-03 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 39.32 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 43 VQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHR 118
Cdd:cd21306 16 VVKKSLITFVNKHLNK-----LNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDA 90
|
90 100 110
....*....|....*....|....*....|.
gi 530389149 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21306 91 GLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1344-1445 |
7.69e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1344 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAKELQQrmqeevvRREEAAVDAQQQKRSI 1423
Cdd:PRK11448 152 LTLKQQLELQAREKAQSQALAEAQQQELVALEG---LAAELEEKQQELEAQLEQLQE-------KAAETSQERKQKRKEI 221
|
90 100
....*....|....*....|....*.
gi 530389149 1424 QEELQQLRQSSEAE----IQAKARQA 1445
Cdd:PRK11448 222 TDQAAKRLELSEEEtrilIDQQLRKA 247
|
|
| PRK01294 |
PRK01294 |
lipase secretion chaperone; |
1398-1571 |
7.77e-03 |
|
lipase secretion chaperone;
Pssm-ID: 234937 [Multi-domain] Cd Length: 336 Bit Score: 41.97 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1398 LQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaersrlrieeeirvvrLQLEATERQRGGAE 1477
Cdd:PRK01294 187 YQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQAL----------------LQQLAQLQASGASP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1478 GELQALRARAEEAEAqkrqaqeeAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1557
Cdd:PRK01294 251 QELRLMRAQLVGPEA--------AQRLEQLDQQRAAWQQRYDDYLAQRAQILNAAGLSPQDRQAQIAQLRQQRFSPQEAL 322
|
170
....*....|....
gi 530389149 1558 RQAEVERARQVQVA 1571
Cdd:PRK01294 323 RLAALERIHDAGQT 336
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1427-1602 |
7.82e-03 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 41.82 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1427 LQQLRQSSEAEIQAKaRQAEAAERSRLR--IEEEIRVVRLQLEATERQRGGAEGELQALRARAE------EAEAQKRQAQ 1498
Cdd:pfam00038 23 LEQQNKDLETKISEL-RQKKGAEPSRLYslYEREIRELRRQLDTLTVERARLQLELDNLRLAAEdfrqkyEDELNLRQSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1499 E-EAERLRRQVQDESQRKRQAEV-------ELASRVKAEAEAAREKQRALQ------------------ALEELRLQAEE 1552
Cdd:pfam00038 102 EaDIVGLRKDLDEATLARVDLEMkieslkeELAFLKKNHEEEVRELQSQVSdtqvnvemdaarkldltsALAEIRAQYEE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530389149 1553 -AERRLRQAEVERARQVQVALETAQRSAEAELQSKrasfaEKTAQLERSLQ 1602
Cdd:pfam00038 182 iAEKNREEAEEWYQSKLEELQQAAARNGDALRSAK-----EEITELRRQIQ 227
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1533-1587 |
8.03e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1533 AREKQRALQaleelRLQAEEAERRlRQAEVERARQVQVALETAQRS-AEAELQSKR 1587
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| YloA |
COG1293 |
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ... |
2176-2341 |
8.11e-03 |
|
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224212 [Multi-domain] Cd Length: 564 Bit Score: 42.38 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2176 KKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRV-QMEELSKLKARIEa 2254
Cdd:COG1293 278 DKIKQLASELEKKLEKELKKLENKLEKQEDELEELEKAAEELRQKGELLYANLQLIEEGLKSVRLaDFYGNEEIKIELD- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2255 enraLILRDKDNTQRFLQEEAeKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQralaekmlkEKMQAVQEATRLKAEA 2334
Cdd:COG1293 357 ----KSKTPSENAQRYFKKYK-KLKGAKVNLDRQLSELKEAIAYYESAKTALEKA---------EGKKAIEEIREELIEE 422
|
....*..
gi 530389149 2335 ELLQQQK 2341
Cdd:COG1293 423 GLLKSKK 429
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
2299-2479 |
8.11e-03 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 42.11 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2299 RQLAEEDLAQQRALAEKMLKEKMQAVQEATrlkaeaELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQ 2378
Cdd:COG4487 28 RYKQIEQEDQSRILNTLEEFEKEANEKRAQ------YRSAKKKELSQLEEQLINQKKEQKNLFNEQIKQFELALQDEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2379 RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTE----LATQEKVTLVQTLEIQRQQSDHDAERLR 2454
Cdd:COG4487 102 LEALELLNLEKDKELELLEKELDELSKELQKQLQNTAEIIEKKRENNKneerLKFENEKKLEESLELEREKFEEQLHEAN 181
|
170 180
....*....|....*....|....*..
gi 530389149 2455 EAIAELEREK--EKLQQEAKLLQLKSE 2479
Cdd:COG4487 182 LDLEFKENEEqrESKWAILKKLKRRAE 208
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1549-1946 |
8.12e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 42.18 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1549 QAEEAERRLRQAEVERARQVQvALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEA 1625
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQ-AQEAANRQREKEKErykRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1626 ERAREEaerelerwqLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE--EQAVRQRELAEQELEKQR 1703
Cdd:pfam07888 107 SRSGEE---------LAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKErvKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1704 QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1783
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1784 RSTSEKSKQR--LEAEAGRFR-ELAEEAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLkteaE 1858
Cdd:pfam07888 258 EELSSMAAQRdrTQAELHQARlQAAQLTLQLAdaSLALREGRARWAQERETLQQSAEADKDRIEKLSA--ELQRL----E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1859 IALKEKEAENERLR-RLAEDEAFQRRRLEEQaaqhkadieERLAQLRKASDSELERQKglvEDTLRQRRQVEEEILALKA 1937
Cdd:pfam07888 332 ERLQEERMEREKLEvELGREKDCNRVQLSES---------RRELQELKASLRVAQKEK---EQLQAEKQELLEYIRQLEQ 399
|
....*....
gi 530389149 1938 SFEKAAAGK 1946
Cdd:pfam07888 400 RLETVADAK 408
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1436-1603 |
8.26e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1436 AEIQAKARQAEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1515
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA-AAATPAAPAAAARRAARAAAAARQAEQPAAEAAAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1516 RQAEVELASRVKAEAEAAREKQRALQALEelRLQAEEAERRLRQAEVERARQVQVALE---TAQRSAEAELQSKRASFAE 1592
Cdd:PRK12678 101 KAEAAPAARAAAAAAAEAASAPEAAQARE--RRERGEAARRGAARKAGEGGEQPATEAradAAERTEEEERDERRRRGDR 178
|
170
....*....|.
gi 530389149 1593 KTAQLERSLQE 1603
Cdd:PRK12678 179 EDRQAEAERGE 189
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2338-2472 |
8.38e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 2338 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSR------AQARAEEDAQRF 2411
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530389149 2412 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLQQEAK 2472
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1357-1604 |
8.94e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 41.59 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1357 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQK---RSIQEELQQLRQ- 1432
Cdd:COG1340 12 ELKRKQLKEEIEELKEKRDELRKEASELAEKRDELNAKVRELREKAQELREERDEINEEVQELKekrDEINAKLQELRKe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1433 ------------SSEAEIQAKARQAEAAER----SRLRIEEEIRVV------RLQLEATERQRGGAEgELQALRARAEEA 1490
Cdd:COG1340 92 yrelkekrnefnLGGRSIKSLEREIERLEKkqqtSVLTPEEERELVqkikelRKELEDAKKALEENE-KLKELKAEIDEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1491 EAQKRQAQEEAERLRRQVQDESQRKRQAeVELASRVKAEAEAAREK-QRALQALEELRLQAEEAERRLRQAEVERARQVQ 1569
Cdd:COG1340 171 KKKAREIHEKIQELANEAQEYHEEMIKL-FEEADELRKEADELHEEfVELSKKIDELHEEFRNLQNELRELEKKIKALRA 249
|
250 260 270
....*....|....*....|....*....|....*
gi 530389149 1570 VALETAQRSAEAELQSKRASFAEKTAQLERSLQEE 1604
Cdd:COG1340 250 KEKAAKRREKREELKERAEEIYEKFKRGEKLTTEE 284
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1350-1537 |
9.11e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.29 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1350 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER----------EAKELQQRMQEEVVRRE-----EAAV 1414
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegeiEAKEADHKGETEAEEVEhegetEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1415 DAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1491
Cdd:TIGR00927 726 TEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530389149 1492 AQKRQAQEEAERlRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1537
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1183-1564 |
9.53e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 433472 [Multi-domain] Cd Length: 817 Bit Score: 42.26 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1183 RERVAQLLERWQAvlaqtdvrQRELEQLGRQLR-----YYRESAdplgawlQDARRRQEQIQAMPLADSQAVREQlrQEQ 1257
Cdd:pfam13779 477 QERLSEALERGAS--------DEEIARLMQELRaalddYMQALA-------EQAQRNPQAQQARPGDNAQQMTQQ--DLQ 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1258 ALLEEIE---RHGEKVEecqrfAKQYINaikdyELQLVTYKAQlepvasPAKKPKVQSGSESVIQEYVDlrthysELTTL 1334
Cdd:pfam13779 540 RMMDRIEelaRSGRRAE-----AQQMLS-----QLQQMMENLQ------AAQPQQGQQQAQGEMQQAMD------ELGDL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1335 TSQYIKFISETLRRMEEEERLAEQQRAEERErlaeveaaleKQRQLAEahaqakaQAEREAKELQQRMQEEVVRREEAAV 1414
Cdd:pfam13779 598 LREQQQLLDETFRQLQEQRRGQQGQQGGGQP----------GQPQQGQ-------QGQQLGGQQGQGGPGEGQGGPDGGG 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1415 DAQQQK---RSIQEELQQLRQSSEAEIQA--KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEE 1489
Cdd:pfam13779 661 LAQRQQalrRRLEELQDELKGQGQEPGDAlgDAGRAMGDAEDALGQGDGAEAVDAQGRALEALRQGAQQMAEQMQGQGQG 740
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530389149 1490 aEAQKRQAQEEAERLRRQVQDESQRK-RQAEVELASRVKAEAEAARekQRALQALEELRLQAEEAERrlrqAEVER 1564
Cdd:pfam13779 741 -QGGGQGGQGGQGGRGRGDRDPLGRPlGGQGPGDDDDVKVPDEIDV--QRAREILEELRRRLGDPTR----PEEEL 809
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump [Defense mechanisms]; |
1463-1573 |
9.64e-03 |
|
Multidrug resistance efflux pump [Defense mechanisms];
Pssm-ID: 224482 [Multi-domain] Cd Length: 352 Bit Score: 41.55 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530389149 1463 RLQLEATERQRGGAEGELQALRARAEEAEAQK--------RQAQEEAERLRRQVQDE--SQRKRQ-AEVELAsrvKAEAE 1531
Cdd:COG1566 90 RAALEQAEAALAAAEAQLRNLRAQLASAQALIaqaeaqdlDQAQNELERRAELAQRGvvSREELDrARAALQ---AAEAA 166
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530389149 1532 AAREKQRALQALEELRLQAEEAERRLRQAEVERArQVQVALE 1573
Cdd:COG1566 167 LAAAQAAQKQNLALLESEVSGAQAQVASAEAALD-QAKLDLE 207
|
|
|