|
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 |
4.25e-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: 242.31 E-value: 4.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 41 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQV 120
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKI 75
|
90 100 110
....*....|....*....|....*....|
gi 254675119 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 |
8.95e-72 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 236.07 E-value: 8.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 254675119 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 |
4.15e-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: 234.53 E-value: 4.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 38 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 254675119 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 |
3.59e-69 |
|
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: 229.49 E-value: 3.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 37 QDERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLR 116
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLK 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 254675119 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 |
1.09e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 254675119 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 |
9.10e-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: 204.88 E-value: 9.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 38 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 254675119 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 |
9.57e-58 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.59 E-value: 9.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 254675119 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 |
5.04e-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: 176.77 E-value: 5.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 162 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 241
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 254675119 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 |
1.09e-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: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 43 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 122
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77
|
90 100
....*....|....*....|....*....
gi 254675119 123 VNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21186 78 VNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
164-264 |
2.47e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 254675119 244 EDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
37-147 |
6.09e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 162.54 E-value: 6.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 37 QDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYL 115
Cdd:cd21246 10 ADEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFL 84
|
90 100 110
....*....|....*....|....*....|..
gi 254675119 116 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21246 85 KEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
36-375 |
8.91e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 174.74 E-value: 8.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 36 EQDERDRVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALD 113
Cdd:COG5069 2 EAKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 114 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSW 192
Cdd:COG5069 78 FIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 193 RDGRLFNAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SL 263
Cdd:COG5069 155 RDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 264 YD----AMPRVPGAQDGVRANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE--LPAK 337
Cdd:COG5069 235 LEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLE 312
|
330 340 350
....*....|....*....|....*....|....*....
gi 254675119 338 EAD-KNRSKVIYQSLEgAVQAGQLKIPPGYHPLDVEKEW 375
Cdd:COG5069 313 TTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
164-264 |
1.82e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 157.94 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 254675119 244 EDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
39-151 |
3.87e-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: 157.15 E-value: 3.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 39 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 116
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*
gi 254675119 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 |
8.75e-44 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 156.19 E-value: 8.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 39 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 116
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 254675119 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
37-147 |
2.00e-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: 152.45 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 37 QDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYL 115
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL 84
|
90 100 110
....*....|....*....|....*....|..
gi 254675119 116 rHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21193 85 -KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
151-266 |
2.99e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 149.05 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
163-268 |
6.98e-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: 147.85 E-value: 6.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 254675119 243 PEDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
39-151 |
4.31e-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: 142.66 E-value: 4.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 39 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNK 77
|
90 100 110
....*....|....*....|....*....|...
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21242 78 SIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
160-264 |
1.61e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 141.35 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 160 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 239
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 254675119 240 LLDPEDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1353-1975 |
1.97e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 158.95 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1353 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAElEAQELQRRMQEevarreeaavdaqqqkRSIQEELQHLRQSs 1431
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAE-RYRELKEELKE----------------LEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1432 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1511
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1512 KRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVELQSKRASFAEKT 1591
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1592 AQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA 1671
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1672 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQHEATAA 1748
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1749 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA-----LAEEAKRQRQLAE 1823
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtlLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1824 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA 1903
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1904 SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRsnaedtmrsKEQAELEAARQR 1975
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE---------RELERLEREIEA 778
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
160-264 |
2.74e-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: 140.53 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 160 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 239
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 254675119 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 |
5.12e-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: 140.55 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 38 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 116
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
34-147 |
9.07e-38 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 139.80 E-value: 9.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 34 KDEQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIAL 112
Cdd:cd21317 22 KALADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 254675119 113 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21317 97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
163-264 |
6.71e-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: 136.15 E-value: 6.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 254675119 243 PEDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
43-149 |
2.29e-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: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 43 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 120
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGV 78
|
90 100
....*....|....*....|....*....
gi 254675119 121 KLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21215 79 KLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1348-2053 |
2.30e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 153.37 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1348 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSiqEELQHL 1427
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1428 RQSSEAEIQAKAQQVEAAERSRmRIEEEIRVVRLQlETTERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1507
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1508 ESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASF 1587
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1588 AEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRlqAEEVaqqkslAQADAEKQ 1667
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--AEEK------KKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1668 KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATA 1747
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1748 ATQKRQeleAELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAA 1827
Cdd:PTZ00121 1479 AEEAKK---ADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1828 RQRAEAERvlTEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE 1907
Cdd:PTZ00121 1546 KKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1908 L--------ERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDtMRSKEQAELEAARQRQLAA 1979
Cdd:PTZ00121 1620 IkaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDEKKAAEALKKEA 1698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1980 EEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2053
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1451-2051 |
3.24e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 151.63 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1451 RIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1530
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1531 REKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLre 1610
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1611 eaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1690
Cdd:COG1196 347 ---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1691 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL 1770
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1771 ASKARAEEESRST---SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEA 1847
Cdd:COG1196 498 EAEADYEGFLEGVkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1848 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQkglVEDTLRQRRQVEE 1927
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT---LAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1928 EIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRK 2007
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 254675119 2008 VALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2051
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
41-147 |
3.32e-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: 134.05 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 41 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQ 119
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKG 77
|
90 100
....*....|....*....|....*...
gi 254675119 120 VKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21214 78 VKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
167-268 |
4.80e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 133.71 E-value: 4.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 167 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 254675119 246 VDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
38-151 |
1.22e-35 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 132.74 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 38 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQK 76
|
90 100 110
....*....|....*....|....*....|....
gi 254675119 118 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21231 77 NNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
148-264 |
2.00e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.87 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 148 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 227
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 228 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1480-2080 |
9.27e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.01 E-value: 9.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1480 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQRKRqaeaelalrVKAEAEAA------------REKQRALQALDELR 1544
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAeryrelkeelkeLEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1545 LQAEEAERRLRQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAER 1624
Cdd:COG1196 239 AELEELEAELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1625 AREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAE 1704
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1705 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS 1784
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1785 EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLA----AISEATRLKTEAEIALKE 1860
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1861 KEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAA 1940
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1941 AGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKV 2020
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2021 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDR 2080
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1682-2244 |
1.64e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 146.24 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1682 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK 1761
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1762 VRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKL 1841
Cdd:COG1196 300 LEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1842 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLvEDTLRQ 1921
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1922 RRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEE 2001
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2002 AARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRL 2081
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2082 RSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ 2161
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2162 KQAADAEMEKHKKFAE-QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQME 2240
Cdd:COG1196 698 ALLAEEEEERELAEAEeERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
....
gi 254675119 2241 ELGK 2244
Cdd:COG1196 778 ALGP 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1316-1903 |
2.24e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 142.38 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1316 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-------LAEAHAQAKAQ 1387
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1388 AELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTE 1467
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1468 RQRGGAEGELQALRARAE------------------EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1529
Cdd:COG1196 373 ELAEAEEELEELAEELLEalraaaelaaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1530 AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLR 1609
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1610 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQ 1684
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1685 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRA 1764
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1765 EMEVLLASKARAEEESRSTSEKSKQRleaeagrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI 1844
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1845 SEATRLKTEAEIALKEKEAENerLRRLAEDEAFQRRR--LEEQaalhKADIEERLAQLRKA 1903
Cdd:COG1196 763 EELERELERLEREIEALGPVN--LLAIEEYEELEERYdfLSEQ----REDLEEARETLEEA 817
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
164-264 |
5.36e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.21 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 254675119 244 EDVDVPQPDEKSIITYVSSLY 264
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1341-1962 |
5.64e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 139.12 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAELEAQELQR----RMQEEVARREEAAVDAQ 1414
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedaKKAEAVKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1415 QQKRSIQE-------ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRlQLETTERQRGGAEGELQALRAR-AEE 1486
Cdd:PTZ00121 1241 EAKKAEEErnneeirKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1487 AEAQKRQAQEEAERLRRQVQdESQRKRQAEAELALRVKAEAEAAREKQRALQ--------ALDELRLQAEE---AERRLR 1555
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkeeakkKADAAKKKAEEkkkADEAKK 1398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1556 QAEAERARQVQVALETAQRSAEVELQsKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELER 1635
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1636 WQLKANEALRLRLQAEEVAQqkslaQADAEKQKEEAEREARRRGKAEEqAVRQRELAEQELEKQRQLAEGTAQQRLAAE- 1714
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKK-----KADEAKKAAEAKKKADEAKKAEE-AKKADEAKKAEEAKKADEAKKAEEKKKADEl 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1715 --QELIRLRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRlE 1792
Cdd:PTZ00121 1552 kkAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-E 1629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1793 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAA--RQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 1870
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1871 LAEDEAFQRRRLEEQAALHKADIEE--RLAQLRKASESELERQKGlvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELEL 1948
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEakKEAEEDKKKAEEAKKDEE--EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
650
....*....|....
gi 254675119 1949 ELGRIRSNAEDTMR 1962
Cdd:PTZ00121 1788 EDEKRRMEVDKKIK 1801
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
163-261 |
6.75e-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: 121.76 E-value: 6.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 254675119 243 PEDVDVPQPDEKSIITYVS 261
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
151-266 |
9.33e-32 |
|
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: 121.87 E-value: 9.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 151 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 231 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 266
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
43-151 |
9.50e-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: 9.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 43 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 122
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVEL 77
|
90 100
....*....|....*....|....*....
gi 254675119 123 VNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21232 78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
167-268 |
1.17e-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: 121.22 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 167 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 254675119 246 VDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
42-152 |
2.65e-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: 121.02 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 42 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ 119
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDE 88
|
90 100 110
....*....|....*....|....*....|....
gi 254675119 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 |
3.20e-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: 120.08 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 43 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 120
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGI 78
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 121 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21227 79 KLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
169-264 |
1.27e-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: 118.22 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 169 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 247
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 254675119 248 VPQPDEKSIITYVSSLY 264
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
167-269 |
2.67e-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: 117.72 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 167 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 244
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 254675119 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 |
3.01e-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: 117.24 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 254675119 243 PEDVDVPQPDEKSIITYVS 261
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
149-276 |
3.63e-30 |
|
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: 117.88 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 149 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 228
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 254675119 229 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQDG 276
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF---SGAQKA 123
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
38-147 |
3.84e-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: 118.61 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 38 DERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 116
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 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 |
5.84e-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: 116.52 E-value: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 39 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLR 116
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 153
Cdd:cd21191 78 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
896-973 |
1.41e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 114.24 E-value: 1.41e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 896 LAWQSLSRDIQLIRSWSLVTFRTLKPEEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLVAEREYGSCSRHYQQLLQS 973
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1724-2571 |
2.99e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 129.88 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1724 TEQGEQQRQLLEEELARLQHEATAATqkRQELEAELAKVR------AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR 1797
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEglkpsyKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGK 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1798 FRElAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeaf 1877
Cdd:PTZ00121 1111 AEE-ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE---- 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1878 QRRRLEEqaaLHKADIEERLAQLRKASEselerqkglvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNA 1957
Cdd:PTZ00121 1186 EVRKAEE---LRKAEDARKAEAARKAEE----------ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1958 EdtMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKValEEVERLKAKVEEARRLRERAEQesarq 2037
Cdd:PTZ00121 1253 E--IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK--KKADEAKKKAEEAKKADEAKKK----- 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2038 lqlAQEAAQKRLQAEEKAHafvvqqreeelqqtlqqeqnmldrlrseaeaarraaeeaeeareqaereaaqSRKQVEEAE 2117
Cdd:PTZ00121 1324 ---AEEAKKKADAAKKKAE----------------------------------------------------EAKKAAEAA 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2118 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQL 2197
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKA 1427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2198 EETDHQksildEELQRLKAEVTEAARQRSQVEEelfsvRVQMEELGKlkaRIEAENRALILRDKDNTQRFLEE---EAEK 2274
Cdd:PTZ00121 1428 EEKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEE 1494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2275 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE 2350
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2351 DKeQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKV 2430
Cdd:PTZ00121 1575 DK-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2431 TLVQTL-------EIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ-----EQILQETQALQKSFL 2498
Cdd:PTZ00121 1647 KKAEELkkaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAEELKKAEE 1726
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2499 SEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRK 2571
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1112-1818 |
6.86e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.13 E-value: 6.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1112 EQLKEAQAVPATLQELEATKASLKKLRAQAEAQQpvfntLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQ 1191
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEE-----LEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1192 AVLAQTDVRQRELEQLGRQLRYYRESadplsawLQDAKRRQEQIQAvpiancqaareqlrQEKALLEEIERHGEKVEECQ 1271
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEER-------RRELEERLEELEE--------------ELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1272 kfakqyinaikdyelqlitykaqlepvaspakkpkvqsgsesviqeyvdlrtryselttltsqyikfisETLRRMEEEER 1351
Cdd:COG1196 344 ---------------------------------------------------------------------EELEEAEEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1352 LAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmQEEVARREEAAVDAQQQKRSIQEELQHLRQSS 1431
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAEL 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1432 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA--------EAQKRQAQEEAERLRR 1503
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAaarlllllEAEADYEGFLEGVKAA 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1504 QVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1581
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1582 SKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQ 1661
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1662 ADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1741
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER--LEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1742 QHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLralaEEAKRQ 1818
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEALGPVNLLAIEE-----------YEELEERYDFLSEQREDL----EEARET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1785-2468 |
1.31e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.98 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1785 EKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedaaRQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1864
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1865 NERLRRLAEDEAFQRRRLEEQAAlhkadiEERLAQLRKASESELERQkglvEDTLRQRRQVEEEIMALKVSFEKAAAGKA 1944
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYEL------LAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1945 ELELELgrirSNAEDTMRSKEQAELEAARQRQlaaeeeqrrrEAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEAR 2024
Cdd:COG1196 341 ELEEEL----EEAEEELEEAEAELAEAEEALL----------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2025 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAER 2104
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2105 EAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE--MEKHKKFAEQTLRQ 2182
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2183 KAQVEQELTTLRLqleETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2262
Cdd:COG1196 567 KAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2263 NTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2342
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2343 EQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQL----EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgek 2418
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL--- 800
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 254675119 2419 lhrtelaTQEKVTLVQTLeiqrqqsdhdaERLREAIAELEREKEKLKQEA 2468
Cdd:COG1196 801 -------SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
42-149 |
2.20e-28 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 111.80 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
167-266 |
2.74e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.61 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 167 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 245
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 254675119 246 VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
151-275 |
5.56e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 111.33 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 254675119 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQD 275
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF---SGAQK 119
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1245-2033 |
7.29e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.70 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1245 AAREQLRQEKALLEEIERHGEKVEECQKFAKQYI---NAIKDYELQLITYkaqlepvaspakkpkvqsgsesviqEYVDL 1321
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSLERQAEKAERYKelkAELRELELALLVL-------------------------RLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1322 RTRYSELTTLTSQYikfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQE 1401
Cdd:TIGR02168 238 REELEELQEELKEA----EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1402 EVARREEAAVDAQQQKRSIQE------ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG 1475
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1476 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqALDELRLQAEEAERRLR 1555
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE--ELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1556 QAEAERarqvqvaletaqRSAEVELQSKRASFAEKTAQLERtLQEEHVTVAQLREEAERRAQQQAEAERAREEAerelER 1635
Cdd:TIGR02168 472 EAEQAL------------DAAERELAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGILGVLSELISVD----EG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1636 WQLKANEALRLRLQA---EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQE----------------- 1695
Cdd:TIGR02168 535 YEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgvakdlvkfdpkl 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1696 --------------------LEKQRQL-----------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1732
Cdd:TIGR02168 615 rkalsyllggvlvvddldnaLELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1733 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfRELAEEAARL 1808
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEI-EELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1809 RALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAeialKEKEAENERLRRLAEDEAFQRRRLEEQAAL 1888
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1889 HKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQ-- 1966
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQle 928
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1967 ---AELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvalEEVERLKAKVEEARRLRERAEQE 2033
Cdd:TIGR02168 929 lrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEE 994
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
151-266 |
9.39e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.89 E-value: 9.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1344-2388 |
1.14e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 121.09 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAELEAQELQRRMQEEVARR-EEAAVDAQQQKRSIQ 1421
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIARLvGEATKEAEALKAEAE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1422 EELQhlrqssEAEIQAKAQQVEAAERSRMRIEEEIRVvrlQLETTERQrggAEgelQALRARAEEAEAQKRQAQEEAERL 1501
Cdd:NF041483 334 QALA------DARAEAEKLVAEAAEKARTVAAEDTAA---QLAKAART---AE---EVLTKASEDAKATTRAAAEEAERI 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1502 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELRLQaEEAeRRLRqAEAERARQVQVA----LETAQRSAE 1577
Cdd:NF041483 399 RREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLRAEAVAegerIRGEARREA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1578 VELQSKRASFAEKTAQLERTLQEEHVTVAQLREeaerraqqqaeaerareeaerelERWQLKANE-ALRLRLQAEEVAQQ 1656
Cdd:NF041483 472 VQQIEEAARTAEELLTKAKADADELRSTATAES-----------------------ERVRTEAIErATTLRRQAEETLER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1657 kslAQADAEKQKeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAEteqGEQQRQLLE 1735
Cdd:NF041483 529 ---TRAEAERLR----------AEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTE---AEERLTAAE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1736 EELARLQHEataATQKRQELEAELAKVRAEM-EVLLASKARAEEEsrstSEKSKQRLEAEAGRFRELAEEAA-RLRA-LA 1812
Cdd:NF041483 593 EALADARAE---AERIRREAAEETERLRTEAaERIRTLQAQAEQE----AERLRTEAAADASAARAEGENVAvRLRSeAA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1813 EEAKRQRQLAEEDAARQRAE----AERVLTEKL----AAISEATRLKTEAEIALKEKEAENERLRRLAedeafqRRRLEE 1884
Cdd:NF041483 666 AEAERLKSEAQESADRVRAEaaaaAERVGTEAAealaAAQEEAARRRREAEETLGSARAEADQERERA------REQSEE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1885 QAALHKADIEERLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEIMALKVSFEKAAA-GKAELELELGR 1952
Cdd:NF041483 740 LLASARKRVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADR 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1953 IRSnaeDTMRSKEQAELEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEE-ARRLRERA- 2030
Cdd:NF041483 820 VRS---DAYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEAs 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2031 ------EQESARQLQLAQEAAQK-RLQAEEKAHAFVVQQREEELQQTLQQEQNMlDRLRSEAEAARRAAEEAEEAREQAE 2103
Cdd:NF041483 884 dtlasaEQDAARTRADAREDANRiRSDAAAQADRLIGEATSEAERLTAEARAEA-ERLRDEARAEAERVRADAAAQAEQL 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2104 REAAQS---RKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA------------ADAE 2168
Cdd:NF041483 963 IAEATGeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKdankrrseaaeqADTL 1042
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2169 MEKHKKFAEQtLRQKAQVEQELTTLRLQlEETDHQKSILDEELQRLKAEVT-----EAARQRSQVEEELFSVRVQM---- 2239
Cdd:NF041483 1043 ITEAAAEADQ-LTAKAQEEALRTTTEAE-AQADTMVGAARKEAERIVAEATvegnsLVEKARTDADELLVGARRDAtair 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2240 EELGKLKARIEAENRALilrdkdnTQRFLEEEAEKMKQVAEEAARLSVAAQEaarlrQLAEEDLAQQRALAE---KMLKE 2316
Cdd:NF041483 1121 ERAEELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE-----QLAEAEAKAKELVSDansEASKV 1188
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 2317 KMQAVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAEAERLK 2388
Cdd:NF041483 1189 RIAAVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ 1254
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1486-2468 |
1.78e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 120.32 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1486 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELRLQAE-EAERRLR 1555
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1556 QAEAERARQVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaqlreEAERRAQQQAEAERAREEAERE 1632
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE---------AESARAEAEAILRRARKDAERL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1633 LERWQLKANEALRlrlQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQRLA 1712
Cdd:NF041483 224 LNAASTQAQEATD---HAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVVAEAKEAAAKQLA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1713 AeqelirlrAETeQGEQQRQLLEEELARLQHEATA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSK 1788
Cdd:NF041483 298 S--------AES-ANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1789 QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI---------------SEATRLKTE 1853
Cdd:NF041483 369 AARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1854 AEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAALHKADIEErlaqLRKASESELERQKG-LVEDTLRQRRQVEE 1927
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE----LRSTATAESERVRTeAIERATTLRRQAEE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1928 eimALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLA------AEEE 2001
Cdd:NF041483 525 ---TLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAeealadARAE 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2002 AARQRKVALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqNMLD 2079
Cdd:NF041483 602 AERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGE-----------------------NVAV 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2080 RLRSEAEaarraaeeaeeareqaereaaqsrkqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2159
Cdd:NF041483 659 RLRSEAA---------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEAL 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 kqkQAADAEMEKHKKFAEQTL------------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2227
Cdd:NF041483 702 ---AAAQEEAARRRREAEETLgsaraeadqereRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2228 -VEEELFSVRVQM-EELGKLkaRIEAENRAlilrdkDNTQRFLEEEAEKMKqvAEEAARLSVAAQEAARLRQLAEEDLAQ 2305
Cdd:NF041483 779 qVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDANRLRREAQEETEA 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2306 QRALAEKMLKEkmqAVQEATRLKAEAELLQQQ-------------------KELAQEQARRLQEDKEQMAQQLVEETQGF 2366
Cdd:NF041483 849 AKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAQADRLIGEATSE 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2367 QRTLEAE-----RQRQLEMSAEAERLKLRMAEMS-RAQARAEEDAQRFRKQAEEIgeklhrTELATQEKVTLVQTLEIQR 2440
Cdd:NF041483 926 AERLTAEaraeaERLRDEARAEAERVRADAAAQAeQLIAEATGEAERLRAEAAET------VGSAQQHAERIRTEAERVK 999
|
1050 1060
....*....|....*....|....*....
gi 254675119 2441 QQSDHDAERLR-EAIAELEREKEKLKQEA 2468
Cdd:NF041483 1000 AEAAAEAERLRtEAREEADRTLDEARKDA 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1407-2053 |
3.61e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.86 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1407 EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE 1486
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1487 aEAQKRQAQEEAERLRRqvqdeSQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQ-AEEAERRLRQAEAERARQV 1565
Cdd:PTZ00121 1114 -ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1566 QVALETaqRSAEvelQSKRASFAEKtAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALR 1645
Cdd:PTZ00121 1188 RKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1646 L--------------RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEKQRQLAEGT 1706
Cdd:PTZ00121 1262 MahfarrqaaikaeeARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1707 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL-EAELAKVRAEMEVLLASKARAEEESRSTSE 1785
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1786 KSKQRLEA-----EAGRFRELAEEAARLRALAEEAKRQRQL---AEE----DAARQRAEAERVLTEKLAAISEATRLKTE 1853
Cdd:PTZ00121 1422 EAKKKAEEkkkadEAKKKAEEAKKADEAKKKAEEAKKAEEAkkkAEEakkaDEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1854 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA---LHKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEEEIM 1930
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEELKKAEEKKKAEE---AKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1931 ALKVSFEKAAAGKAELELELGRIRSnaEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL 2010
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2011 EEV----ERLKAKVEEARR----LRERAEQESARQLQLAQEAAQKRlQAEE 2053
Cdd:PTZ00121 1657 EENkikaAEEAKKAEEDKKkaeeAKKAEEDEKKAAEALKKEAEEAK-KAEE 1706
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
28-151 |
4.49e-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: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 28 KGHrqAKDEQDERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQ 106
Cdd:cd21247 7 KGH--IRKLQEQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 254675119 107 NVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21247 82 NNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
151-266 |
2.58e-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: 104.00 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 151 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 230
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 231 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
169-264 |
2.71e-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: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 169 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 247
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 254675119 248 VPQPDEKSIITYVSSLY 264
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
42-149 |
3.35e-25 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 102.95 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERE 77
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21228 78 SIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
163-269 |
8.22e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.59 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 163 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 239
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 240 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 269
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
42-152 |
1.85e-24 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 101.26 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDRE 89
|
90 100 110
....*....|....*....|....*....|....
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21310 90 HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1340-2056 |
2.99e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 113.00 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1340 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAELEAQELQRRMQEEVAR-REEA 1409
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1410 AVDAQQQKRSIQEELQHLRqsSEAEiQAKAQQVEAAERSRMRIEEEIRVVRLQLE-TTERQRGGAEGELQALRARAEE-- 1486
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1487 --AEAQKRQAQEEAERLRRQVQDESQRKRqaeaelalrvkaeAEAArEKQRALQAldelrlQAEEAERRLRQAEAERARQ 1564
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLR-------------TEAA-ERIRTLQA------QAEQEAERLRTEAAADASA 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1565 VQVALEtaqrSAEVELQSKrasfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeaerelerwqlKANEAL 1644
Cdd:NF041483 649 ARAEGE----NVAVRLRSE-------------------------------------------------------AAAEAE 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1645 RLRLQAEEVAQQ-KSLAQADAEKqkeEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI---RL 1720
Cdd:NF041483 670 RLKSEAQESADRvRAEAAAAAER---VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1721 RAETEQGEQQRqLLEEELARLQHEATAATQKRQELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAEAG 1796
Cdd:NF041483 747 RVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSDAY 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1797 RFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED 1874
Cdd:NF041483 826 AERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADARE 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1875 EAFQRRrlEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAElelelgRIR 1954
Cdd:NF041483 903 DANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------RLR 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1955 SNAEDTMRSKEQAeleAARQRQLAAEEEQRrreaeervqrslaAEEEAARQRKVALEEVERL--KAKVEEARRLRERAEQ 2032
Cdd:NF041483 975 AEAAETVGSAQQH---AERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAAEQ 1038
|
730 740
....*....|....*....|....
gi 254675119 2033 ESARQLQLAQEAAQKRLQAEEKAH 2056
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
46-148 |
3.20e-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: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 46 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKL 122
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKV 76
|
90 100
....*....|....*....|....*.
gi 254675119 123 VNIRNDDIADGnPKLTLGLIWTIILH 148
Cdd:smart00033 77 VLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1683-2521 |
4.19e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.46 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1683 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1762
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1763 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-- 1840
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELes 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1841 -LAAISEATRLKTEAEIALKEKEAENERLRRLaedeafqRRRLEEQAALHKADIEERLAQLrKASESELERQKGLVEDtl 1919
Cdd:TIGR02168 356 lEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEE-- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1920 RQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEdtmrsKEQAELEAARQRQLaaeeeqrrreaeervqrSLAAE 1999
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2000 EEAARQRKVALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA---------QKRLQAEEKAHA 2057
Cdd:TIGR02168 484 LAQLQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlggrlqavvVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2058 FVVQQREEELQQTLqqeqnmLDRLRSEAEAARRAAEEAEEAREQAEREAAqsrkqVEEAERLKQSAEEQAQAQAQAQAAA 2137
Cdd:TIGR02168 564 FLKQNELGRVTFLP------LDSIKGTEIQGNDREILKNIEGFLGVAKDL-----VKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2138 EKLRKEAEQEAARRAQAEQAALKQKQAADAEmeKHKKFAEQTLRQKaqveQELTTLRLQLEETDHQKSILDEELQRLKAE 2217
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITG--GSAKTNSSILERR----REIEELEEKIEELEEKIAELEKALAELRKE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2218 VTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALiLRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQ 2297
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2298 LAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLVEETQgfqrtleaerqr 2376
Cdd:TIGR02168 786 ELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE------------ 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2377 qlEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE 2456
Cdd:TIGR02168 849 --ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2457 LEREKEKLKQE-AKLLQLKSEEMQTVQQEqilqetqALQKSFLSEKDSLLQRERfIEQEKAKLEQL 2521
Cdd:TIGR02168 927 LELRLEGLEVRiDNLQERLSEEYSLTLEE-------AEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
165-264 |
4.46e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.56 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 165 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 244
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 254675119 245 D-VDVPQPDEKSIITYVSSLY 264
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
164-264 |
1.14e-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: 98.27 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 254675119 244 EDVDVPQ-PDEKSIITYVSSLY 264
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
167-267 |
1.44e-23 |
|
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: 97.92 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 167 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 246
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 254675119 247 DVPQPDEKSIITYVSSLYDAM 267
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
43-151 |
1.65e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 98.13 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 43 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-V 120
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgV 78
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 121 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:pfam00307 79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
164-268 |
7.87e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.01 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 254675119 244 EDVDVPQPDEKSIITYVSSLYDAMP 268
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1353-2057 |
1.18e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.83 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1353 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQA-KAQAELEAQELQRRMQEEV-ARREEAAVDAQQQKRSIQEELQHLRQ 1429
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILnELERQLKSLERQAeKAERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1430 SSEAEIQAKAQQVEAAERSRMRIEEEIRVvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRR------ 1503
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEE--------------LQKELYALANEISRLEQQKQILRERLANLERqleele 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1504 -QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLR--QAEAERarqvqvaletaQRSAEVEL 1580
Cdd:TIGR02168 323 aQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEelEEQLET-----------LRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1581 QSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1660
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1661 QADAEKQKEeaerearrrgKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQ---------ELIRLRAETEQG--- 1727
Cdd:TIGR02168 472 EAEQALDAA----------ERELAQLQARlDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1728 --------------EQQRQ----LLEEELARL----------------QHEATAATQKRQELEAELAKVRAEMEVLLA-- 1771
Cdd:TIGR02168 542 alggrlqavvvenlNAAKKaiafLKQNELGRVtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSyl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1772 --------SKARAEEESRSTSEK-----------------SKQRLEAEAGRF---RELAEEAARLRALAEEAKRQRQlAE 1823
Cdd:TIGR02168 622 lggvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggviTGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK-AL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1824 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEErLAQLRKA 1903
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1904 SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQlaaeeeq 1983
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------- 852
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1984 rrreAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLqlaQEAAQKRLQAEEKAHA 2057
Cdd:TIGR02168 853 ----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL---RELESKRSELRRELEE 919
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1018-1563 |
1.24e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1018 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1097
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1098 RSTQGAEEVLKTHEEQLKEAQAvpATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE 1177
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1178 RWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvpiancqAAREQLRQEKALL 1257
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1258 EEIERHGEKVEEcqkfAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyik 1337
Cdd:COG1196 470 EEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1338 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA----HAQAKAQAELEAQELQRRMQEEVARREEAAVDA 1413
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1414 QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1493
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1494 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQA-----------------EEAERRLRQ 1556
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEelleeealeelpeppdlEELERELER 771
|
....*..
gi 254675119 1557 AEAERAR 1563
Cdd:COG1196 772 LEREIEA 778
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
164-262 |
2.44e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 94.61 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 254675119 243 PEDVDVPQPDEKSIITYVSS 262
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1065-1903 |
3.87e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.29 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1065 LRSELELTLGKLEQVRSLSaiylEKLKTISLVIRSTQGAeeVLKTHEEQLKEAQAvpATLQELEATKASLKKLRAQAEAQ 1144
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKA----ERYKELKAELRELELA--LLVLRLEELREELE--ELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1145 QPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAW 1224
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1225 LQDAKRRQEQIQAVPIANC----------QAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQ 1294
Cdd:TIGR02168 346 LEELKEELESLEAELEELEaeleelesrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1295 LEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ 1374
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1375 RQLAEAHAQAKAQAELEAQELQRRMQE-EVARREEAAVDAQQQKR----------SIQEELQHLRQSSE------AEIQA 1437
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAALGGRlqavvvenlnAAKKAIAFLKQNELgrvtflPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1438 KAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAea 1517
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG-- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1518 eLALRVKAEAEAAREKQRalQALDELRLQAEEAERRLRQAEAE--RARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1595
Cdd:TIGR02168 660 -VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1596 RtLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERwQLKANEALRLRLQAeEVAQQKSLAQADAEKQKEEAEREA 1675
Cdd:TIGR02168 737 R-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1676 RRRGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL 1755
Cdd:TIGR02168 814 LLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1756 EAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRA 1831
Cdd:TIGR02168 893 RSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1832 EAERvLTEKLAAISEATRLkteaeiALKEKEAENERLRRLAEdeafqrrrleeqaalHKADIEERLAQLRKA 1903
Cdd:TIGR02168 973 RLKR-LENKIKELGPVNLA------AIEEYEELKERYDFLTA---------------QKEDLTEAKETLEEA 1022
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
795-861 |
7.52e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.55 E-value: 7.52e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 795 QLKPRNpaHPVRGHVPLIAVCDYKQVEVTVHKGDQCQLVGPAQPSHWKVLSGSSSEAAVPSVCFLVP 861
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1548-2422 |
1.77e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.98 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1548 EEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVTVAQLREEAERRAQQQAeaera 1625
Cdd:TIGR02168 175 KETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1626 reeaerelerwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAE-----QELEKQR 1700
Cdd:TIGR02168 247 -----------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1701 QLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllaskaraeeES 1780
Cdd:TIGR02168 305 QILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-----------EL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1781 RSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-LAAISEATRLKTEAEIALK 1859
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1860 EKEAENERLRRLAEdEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVED--TLRQRRQVEEEIMALKVSFE 1937
Cdd:TIGR02168 451 ELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSGLSGILGVLSELI 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1938 KAAAG-KAELELELGRIRSNAedTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERL 2016
Cdd:TIGR02168 530 SVDEGyEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2017 KAKVEEARRL----------RERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAE 2086
Cdd:TIGR02168 608 VKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2087 AARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAAD 2166
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2167 AEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLK 2246
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2247 ARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR 2326
Cdd:TIGR02168 848 EELSEDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2327 LKAEAEL----LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQLEMS------------AEAERLKLR 2390
Cdd:TIGR02168 923 KLAQLELrlegLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-RRLKRLENKikelgpvnlaaiEEYEELKER 1001
|
890 900 910
....*....|....*....|....*....|..
gi 254675119 2391 MAEMSRAQaraeEDAQRFRKQAEEIGEKLHRT 2422
Cdd:TIGR02168 1002 YDFLTAQK----EDLTEAKETLEEAIEEIDRE 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1878-2467 |
7.88e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 7.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1878 QRRRLEEQAA---LHKADIEERLAQLRKASE---------SELERQKGLVEdtlRQRRQVEE-------------EIMAL 1932
Cdd:COG1196 156 ERRAIIEEAAgisKYKERKEEAERKLEATEEnlerledilGELERQLEPLE---RQAEKAERyrelkeelkeleaELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1933 KVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvaleE 2012
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR-----L 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2013 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvvQQREEELQQTLQQEQNMLDRLRSEAEAARRAA 2092
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA------EEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2093 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2172
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2173 KKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAE 2252
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2253 NRAL-----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRL 2327
Cdd:COG1196 542 AALAaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2328 KAEAELLQQQKELAQEQARRLQEDKE------QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARA 2401
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLRevtlegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 2402 EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA--------IAELEREKEKLKQE 2467
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppdLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1127-1929 |
9.89e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.67 E-value: 9.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1127 LEATKASLKKLRAQAEAQQPvFNTLRDELRgaqevgerlqqrhgerDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ 1206
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAER-YKELKAELR----------------ELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1207 LGRQLRYYRESADPLSAWLQDAKRRQEQIQAV------PIANC----QAAREQLRQEKALLEEIERHGEKVEECQKFAKQ 1276
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKElyalanEISRLeqqkQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1277 YINAIKDYELQLITYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEE-ERLAEQ 1355
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLE--AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1356 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR------Q 1429
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1430 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAE----GELQALRARAEEAEAQKRQAQEEAERLRR-- 1503
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVtf 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1504 --------QVQDESQRKRQAEAELALRVKAEAEAAREK-QRALQALDELRLQAEEAERRLRQAEAERARQVQVALE---- 1570
Cdd:TIGR02168 576 lpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1571 ----------TAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1640
Cdd:TIGR02168 656 rpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1641 NEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1720
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1721 RAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1800
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1801 LAEEAARLRALAEEAKRQRQLAEE------DAARQRAEAERVLTEKLAAISEatRLKTEAEIALkEKEAENERLRRLAED 1874
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNLQERLSE--EYSLTLEEAE-ALENKIEDDEEEARR 972
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1875 EAFQ-RRRLEEQAALHKADIEErlaqLRKASE--SELERQKglvEDTLRQRRQVEEEI 1929
Cdd:TIGR02168 973 RLKRlENKIKELGPVNLAAIEE----YEELKEryDFLTAQK---EDLTEAKETLEEAI 1023
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
168-265 |
1.09e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 90.10 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 168 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 246
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 254675119 247 DVPQPDEKSIITYVSSLYD 265
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1858-2610 |
2.92e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1858 LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE-LERQKGLVEDTlrqrrqveeeimalkvsf 1936
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEaTEEAFGKAEEA------------------ 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1937 EKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQrqlaaeeeqrrreaeervqrslaaEEEAARQRKVALEEVERl 2016
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK------------------------AEEARKAEDAKRVEIAR- 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2017 kaKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAFVVQQREEElqqtlqqeqnmldRLRSEAEAARRAAEEAE 2096
Cdd:PTZ00121 1159 --KAEDARKAEEARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAA-------------RKAEEERKAEEARKAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2097 EAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ--KQAADAEMEKHKK 2174
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKK 1302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2175 FAEQtLRQKAQVEQELTTLRLQLEETDHQKSILDE--ELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAE 2252
Cdd:PTZ00121 1303 KADE-AKKKAEEAKKADEAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2253 NraliLRDKDNTQRfleeEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAE 2332
Cdd:PTZ00121 1382 A----AKKKAEEKK----KADEAKKKAEEDKKKADELKKAAAAKKKADE------------AKKKAEEKKKADEAKKKAE 1441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2333 LLQQQKELAQ--EQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRK 2410
Cdd:PTZ00121 1442 EAKKADEAKKkaEEAKKAEEAKKK-AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKADEAKK 1517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2411 QAE-EIGEKLHRTELATQEKvtlvqtlEIQRQQSDHDAERLREAiAELEREKEKLKQEAKllqlKSEEMQTVQQEQILQE 2489
Cdd:PTZ00121 1518 AEEaKKADEAKKAEEAKKAD-------EAKKAEEKKKADELKKA-EELKKAEEKKKAEEA----KKAEEDKNMALRKAEE 1585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2490 TQALQKSFLSEKDSLLQrerfiEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMAsmEEARR----RQREAE 2565
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYE-----EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA--EEKKKaeelKKAEEE 1658
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 254675119 2566 EGVRRKQEELQHLEQQRQQQEKLLAEENQRLR-ERLQRLEEEHRAA 2610
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaEALKKEAEEAKKA 1704
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
164-263 |
4.45e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 88.31 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 254675119 244 ED-VDVPQPDEKSIITYVSSL 263
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
42-152 |
5.83e-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: 88.98 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRE 90
|
90 100 110
....*....|....*....|....*....|....
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21309 91 SIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
42-152 |
7.47e-20 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 88.60 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRE 93
|
90 100 110
....*....|....*....|....*....|....
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21308 94 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1480-2466 |
1.06e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.21 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1480 LRARAEEAEAQKRQAQEEAER-------LRRQVQdesqrKRQAEAELALRVKAEAEAAREKQRALQALdelRLQAEEAER 1552
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRledilneLERQLK-----SLERQAEKAERYKELKAELRELELALLVL---RLEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1553 RLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKtaqlertlqEEHVTVAQlreeaerraqqqaeaerareeaere 1632
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL---------EEEIEELQ------------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1633 lERWQLKANEalrlrlqaeevaqqkslaQADAEKQKeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgTAQQRLA 1712
Cdd:TIGR02168 288 -KELYALANE------------------ISRLEQQK-------------QILRERLANLERQLEELEAQLEE-LESKLDE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1713 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQRLE 1792
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1793 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAErvLTEKLAAISEATRLKTEAEIALKEKEAENERLR-RL 1871
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE--LERLEEALEELREELEEAEQALDAAERELAQLQaRL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1872 AEDEAFQRRRLEEQAALHKAdieerlaqlrKASESELERQKGLVEDTLRqrrqVEEEimalkvsFEKAaagkaeLELELG 1951
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKAL----------LKNQSGLSGILGVLSELIS----VDEG-------YEAA------IEAALG 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1952 RIRSNAedTMRSKEQAELEAARQRQlaaeeeqrrreaeervqrslaaeeeaARQRKVALEEVERLKAKVEEARRLRERAE 2031
Cdd:TIGR02168 545 GRLQAV--VVENLNAAKKAIAFLKQ--------------------------NELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2032 QESARQLQLAQEAAQKRLQAEEK---AHAFVVQQREEELQQTLQQEQNMldRLRSEAEAARRAAEEAEEAREQAEREAAQ 2108
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNALELAKKLRPGY--RIVTLDGDLVRPGGVITGGSAKTNSSILE 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2109 SRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2188
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2189 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRvqmEELGKLKARIEAENRAL--ILRDKDNTQR 2266
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELTLLNEEAanLRERLESLER 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2267 FLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2346
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2347 RLQEDKEQMAQQLVEETQGFQRtLEAERQRQLEMSAEAERLKLRMAEmsRAQARAEEDAQRFRKQAEEIGEKLHR----T 2422
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAE--ALENKIEDDEEEARRRLKRLENKIKElgpvN 988
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 254675119 2423 ELATQEKVTLVQTLE-IQRQQSDHDA--ERLREAIAELERE-KEKLKQ 2466
Cdd:TIGR02168 989 LAAIEEYEELKERYDfLTAQKEDLTEakETLEEAIEEIDREaRERFKD 1036
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
164-264 |
1.44e-19 |
|
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: 86.63 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 243
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 254675119 244 EDVDV--PQPDEKSIITYVSSLY 264
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1440-2256 |
1.59e-19 |
|
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: 97.43 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1440 QQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1508
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1509 SQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEveLQSKRASFA 1588
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE--LESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1589 EKTAQLERTLQEEHVTVAQLREEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQK 1668
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAE---------------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1669 EEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1748
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1749 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA---- 1822
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvve 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1823 EEDAARQRAEAERVLTEKLAAISEATRLKteaeialkEKEAENERLRRLAEDEAFQR--RRLEEQAALHKADIEERLAQL 1900
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGRVTFLPLDSIK--------GTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLGGV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1901 RKASEselerqkglVEDTLRQRRQVEEEIM-------------ALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQA 1967
Cdd:TIGR02168 626 LVVDD---------LDNALELAKKLRPGYRivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1968 ELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQK 2047
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2048 RLQAEEKAHAfvVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKqsaeeqa 2127
Cdd:TIGR02168 777 LAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI------- 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2128 QAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIL 2207
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 254675119 2208 DEELQRLKAEVteaARQRSQVEEElfsVRVQMEELGKLKARIEAENRAL 2256
Cdd:TIGR02168 928 ELRLEGLEVRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1475-2369 |
2.00e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 97.35 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1475 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERR 1553
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1554 LRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvtvaqlreeaeRRAQQQAEAERAREEAEREL 1633
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL-----------AKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1634 ERWQLKANEALRLRLQAEEVAQQKSLAQAdaEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1713
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1714 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA 1793
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1794 EagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER--------VLTEKLAAISEATRLKTEAEIALKEKEAEN 1865
Cdd:pfam02463 470 S---EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvllaliKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1866 ---ERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMA-LKVSFEKAAA 1941
Cdd:pfam02463 547 tavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAdEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1942 GKAELELELGRIRSNAEDTMRSKEQAELEAARQRqlaaeeeqrrreaEERVQRSLAAEEEAARQRKVALEEVERLKAKVE 2021
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAE-------------KSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2022 EARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQ 2101
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2102 AEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLR 2181
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2182 QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDK 2261
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKY 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2262 DNTQRFLEEEAEKMKQVAEEAarlsvaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2341
Cdd:pfam02463 934 EEEPEELLLEEADEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
890 900
....*....|....*....|....*...
gi 254675119 2342 QEQARRLQEDKEQMAQQLVEETQGFQRT 2369
Cdd:pfam02463 1002 EEKKKLIRAIIEETCQRLKEFLELFVSI 1029
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
160-265 |
3.13e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 86.15 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 160 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 239
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 254675119 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 |
3.76e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.45 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 167 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 242
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 254675119 243 PEDVDVPQPDEKSIITYVSSL 263
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1316-1900 |
4.08e-19 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 96.14 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1316 QEYVDLRTRYSELTTLTSQY-IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEL 1390
Cdd:COG4913 262 ERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1391 EAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1470
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1471 GGAEGELQALRARA---EEAEAQKRQAQEEAERLRR----------QVQDESQRKRQAeAELALR-------VKAEAEAA 1530
Cdd:COG4913 422 RELEAEIASLERRKsniPARLLALRDALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLGgfaltllVPPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1531 rekqrALQALDEL----RLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEVELQsKRASFA--EKTAQLERTl 1598
Cdd:COG4913 501 -----ALRWVNRLhlrgRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELG-RRFDYVcvDSPEELRRH- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1599 qEEHVTVAQLREEAERRAQQQAEAERAreeaerelERWQL-KANEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearr 1677
Cdd:COG4913 574 -PRAITRAGQVKGNGTRHEKDDRRRIR--------SRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL-------- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1678 rgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEATAATQKRQE 1754
Cdd:COG4913 637 --EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1755 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1834
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1835 RVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED------EAFQRRRLEE--------QAALHKA--DIEERLA 1898
Cdd:COG4913 791 RAMRA---FNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeERFKELLNENsiefvadlLSKLRRAirEIKERID 867
|
..
gi 254675119 1899 QL 1900
Cdd:COG4913 868 PL 869
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1692-2612 |
1.12e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 94.89 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1692 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQHEA-TAATQKRQELEAELAKVRAEMEV 1768
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1769 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLtekLAAISE 1846
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1847 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR----LEEQAALHKADIEERLAQLRKASESELE-------RQKGLV 1915
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRqaaeLSRAAEQRMQEAEEALREARAEAEKVVAeakeaaaKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1916 EDTLRQR-RQVEEEIMALKVSFEK-AAAGKAELELELG-------RIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRR 1986
Cdd:NF041483 300 ESANEQRtRTAKEEIARLVGEATKeAEALKAEAEQALAdaraeaeKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1987 EAEERVQRSLAAEEEAARQRKVALEEVERLKAKV--------------------------EEARRLRERAEQ-------- 2032
Cdd:NF041483 380 ASEDAKATTRAAAEEAERIRREAEAEADRLRGEAadqaeqlkgaakddtkeyraktvelqEEARRLRGEAEQlraeavae 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2033 ------ESARQ-LQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRL----RSEAEAARRAAEEAEEAREQ 2101
Cdd:NF041483 460 gerirgEARREaVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERAttlrRQAEETLERTRAEAERLRAE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2102 AEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlkqkqAADAEMEK-HKKFAEQTL 2180
Cdd:NF041483 540 AEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA-----DARAEAERiRREAAEETE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2181 RQKAQVEQELTTLRLQLEetdhqksildEELQRLKaevTEAARQRSQVEEELFSVRVqmeelgKLKARIEAENRALILRD 2260
Cdd:NF041483 615 RLRTEAAERIRTLQAQAE----------QEAERLR---TEAAADASAARAEGENVAV------RLRSEAAAEAERLKSEA 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2261 KDNTQRFLEEEAEKMKQVAEEAAR-LSVAAQEAARLRQLAEEDLAQQRALAEkmlKEKMQAVQEATRLKAEAellQQQKE 2339
Cdd:NF041483 676 QESADRVRAEAAAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA---RKRVE 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2340 LAQEQARRLQEDKEQMAQQLV---EETQGFQRTLEAERQRQlemsAEAERLKLRMAemsraqarAEEDAQRFRKQAEEIG 2416
Cdd:NF041483 750 EAQAEAQRLVEEADRRATELVsaaEQTAQQVRDSVAGLQEQ----AEEEIAGLRSA--------AEHAAERTRTEAQEEA 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2417 EKLHRTELATQEKVTLVQTLEIQRQQSDHDAER------LREAIAELEREKEKLKQEAKLLQLK-SEEMQTVQQEQILQE 2489
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAKalaertVSEAIAEAERLRSDASEYAQRVRTEaSDTLASAEQDAARTR 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2490 TQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASM-----EEARRRQREA 2564
Cdd:NF041483 898 ADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLiaeatGEAERLRAEA 977
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 254675119 2565 EEGVRRKQEELQHLEQQRQQQEKLLAEENQRL----RERLQRLEEEHRAALA 2612
Cdd:NF041483 978 AETVGSAQQHAERIRTEAERVKAEAAAEAERLrteaREEADRTLDEARKDAN 1029
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1334-1930 |
1.13e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.34 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1334 QYIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAELEAQELQRRMQEEV 1403
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1404 ARREEaavdaqqqkrsIQEELQHLRQSSE---AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAL 1480
Cdd:PRK02224 286 ERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1481 RARAEEaeaqkrqAQEEAERLrrqvqdesqrkrqaEAELalrvkAEAEAAREKQRAlqALDELRLQAEEAERRLRQAEae 1560
Cdd:PRK02224 355 EERAEE-------LREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAP-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1561 rarqvqVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELE--RWQL 1638
Cdd:PRK02224 405 ------VDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEedRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1639 KANEALRLRLQAEEVAQQKSLAQADAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQ 1715
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1716 ELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEA 1795
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1796 GRFRELAEEAARLRALAEEAKRQRqLAEEDAARQRAEaervltEKLAAISEATRLKTEAEIALKEK----EAENERLRRL 1871
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEAR-IEEAREDKERAE------EYLEQVEEKLDELREERDDLQAEigavENELEELEEL 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1872 aedeafqRRRLEEQAALHkadieERLAQLRKASEsELERQKGLVEDTLRQRRQVEEEIM 1930
Cdd:PRK02224 697 -------RERREALENRV-----EALEALYDEAE-ELESMYGDLRAELRQRNVETLERM 742
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1995-2607 |
4.78e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1995 SLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQE 2074
Cdd:COG1196 204 PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2075 QNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2154
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2155 EQAALKQKQAADAEMEKhkkfAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFS 2234
Cdd:COG1196 364 EEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2235 VRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2314
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2315 KEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2392
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2393 EMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2472
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2473 LKSEEMQTVQQEQILQETQALQKSFLSEKDS-LLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELM 2551
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAeAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2552 ASMEEARRRQREAEEGVRRkqeelqhleqqrqqqekllAEENQRLRERLQRLEEEH 2607
Cdd:COG1196 760 PDLEELERELERLEREIEAlgpv-----------nllaIEEYEELEERYDFLSEQR 804
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
44-149 |
4.93e-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: 82.24 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 44 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVK 121
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVD 77
|
90 100
....*....|....*....|....*...
gi 254675119 122 LVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21212 78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1333-2264 |
6.86e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 92.34 E-value: 6.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1333 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD 1412
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1413 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELqalraraEEAEAQKR 1492
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE-------EELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1493 QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarEKQRALQALDELRLQAEEAERRLRQAEAERARQVQValeta 1572
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL----- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1573 qrsAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEaerelerwqLKANEALRLRLQAEE 1652
Cdd:pfam02463 377 ---AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL---------EILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1653 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1732
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1733 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL--EAEAGRFRELAEEAARLRA 1810
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLipKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1811 LAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaLHK 1890
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ--ELQ 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1891 ADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1970
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1971 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQ 2050
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2051 AEEKahaFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQ 2130
Cdd:pfam02463 840 LELK---EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2131 AQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEE 2210
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2211 LQRLKAEVTEAARQRSQVEEELF------SVRVQMEELGKLKARIEAENRALILRDKDNT 2264
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQRLkeflelFVSINKGWNKVFFYLELGGSAELRLEDPDDP 1056
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
164-263 |
8.85e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 81.82 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 243
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 254675119 244 ED-VDVPQPDEKSIITYVSSL 263
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1339-1970 |
1.38e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.28 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1339 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAELEAQELQRRMqEEVARREEAAVDAQQQKR 1418
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1419 SIQEELQHLRQSSEAEIQAKAQQVEAaersrmrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1492
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1493 --------QAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQA-LDELRLQAEEAERRLRQAEAER-- 1561
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1562 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEE-----------------HVTVAQLREEAerraqqqaeaer 1624
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggraveevlkasiqgvHGTVAQLGSVG------------ 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1625 areeaerelERWQLKANEALRLRLQA-----EEVAQQ--KSLAQADAE----------KQKEEAEREARRRG-------- 1679
Cdd:TIGR02169 535 ---------ERYATAIEVAAGNRLNNvvvedDAVAKEaiELLKRRKAGratflplnkmRDERRDLSILSEDGvigfavdl 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 ----KAEEQAVR---QRELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQ 1726
Cdd:TIGR02169 606 vefdPKYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEG 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1727 GEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQRLEAEAgrfrELA 1802
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEIENVKS----ELK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1803 EEAARLRALaEEAKRQRQLAEEDAARQRAEAE--------RVLTEKLAAISEATRlktEAEIALKEKEAENERLRRLAED 1874
Cdd:TIGR02169 762 ELEARIEEL-EEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1875 EAFQRRRLEEQAALHKADIEERLAQLRKAsESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIR 1954
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
730
....*....|....*.
gi 254675119 1955 SNAEDTMRSKEQAELE 1970
Cdd:TIGR02169 917 KRLSELKAKLEALEEE 932
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1329-2053 |
2.09e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 90.41 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1329 TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREE 1408
Cdd:TIGR00618 134 DLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1409 AAVDAQQQKRSIQEELQHLR--QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaEGELQALRARAEE 1486
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ----EAVLEETQERINR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1487 AEAQKRQA--QEEAERLRRQVQDESQRKRQAEAELA-LRVKAEAEAAREKQRALQALDELRLQAEEAERRlRQAEAERAR 1563
Cdd:TIGR00618 289 ARKAAPLAahIKAVTQIEQQAQRIHTELQSKMRSRAkLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR-DAHEVATSI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1564 QVQVALETAQRSAEVELQSKRASFAEK---TAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1640
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKlqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1641 NEALRLrLQAEEVAQQKSLAQADAEKQ---------KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-------- 1703
Cdd:TIGR00618 448 TCTAQC-EKLEKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQdidnpgpl 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1704 ----EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1779
Cdd:TIGR00618 527 trrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1780 SRSTSEKS------------KQRLEAEAGRF-RELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLTEKLAAISE 1846
Cdd:TIGR00618 607 EDMLACEQhallrklqpeqdLQDVRLHLQQCsQELALKLTALHALQLTLTQERV--REHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1847 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASES--ELERQK--GLVEDTLRQR 1922
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSlkELMHQArtVLKARTEAHF 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1923 RQVEEEIMALKVSFEKAAAgKAELElelgrirsnaedtmrskEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 2002
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHL-AAEIQ-----------------FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2003 ARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2053
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
45-147 |
2.22e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.46 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 45 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-K 121
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpE 76
|
90 100
....*....|....*....|....*..
gi 254675119 122 LVNIRNDDI-ADGNPKLTLGLIWTIIL 147
Cdd:cd00014 77 LDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
168-265 |
5.44e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.54 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 168 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 246
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 254675119 247 DVPQPDEKSIITYVSSLYD 265
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
966-1600 |
1.06e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.19 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 966 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkdpaRECAQRIAEQQK----AQAEVEGLGK 1040
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1041 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKE--- 1116
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqle 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1117 --AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQ-QRHGERDVEVERWRERVTQLLERWQAV 1193
Cdd:TIGR02168 383 tlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1194 LAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvPIANCQAAREQLRQEKALLEEIERHGEKVEEC--- 1270
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAiea 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1271 -------------QKFAKQYINAIKDYELQLITYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTL 1331
Cdd:TIGR02168 542 alggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1332 TSQYikFISETL-------RRMEEEERL--------------------AEQQRAEERERLAEVEAALEK-QRQLAEAHAQ 1383
Cdd:TIGR02168 622 LGGV--LVVDDLdnalelaKKLRPGYRIvtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEElEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1384 ----AKAQAELEAQELQRRMQEEVARREEAAVDAQQQK-RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRV 1458
Cdd:TIGR02168 700 laelRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1459 VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQ 1538
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1539 ALDELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEVELQSKRASFAEKTAQLERTLQE 1600
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1348-1825 |
1.18e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 87.52 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1348 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ-AELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1426
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1427 LRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1505
Cdd:COG4717 151 LEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1506 QDESQRKRQAEAELALRvkaeaeAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALetaqrSAEVELQSKRA 1585
Cdd:COG4717 230 EQLENELEAAALEERLK------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA-----LLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1586 SFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAE 1665
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1666 KQkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEA 1745
Cdd:COG4717 379 AG-----------VEDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1746 TAATQKRQELEAELAKVRAEMEVLlaskaraeEESRSTSEKSKQRLEAEAgRFRELAEEAARLRALAEEAKRQRQLAEED 1825
Cdd:COG4717 442 EELEEELEELREELAELEAELEQL--------EEDGELAELLQELEELKA-ELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1823-2609 |
3.00e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.95 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1823 EEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAlhkadIEERLAQLRK 1902
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAK-----KALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1903 ASESELERQKGLVEDTLRQRRQVEEEimalkvsfEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEE 1982
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQ--------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1983 QRRREAEERVQRSLAAEeeaaRQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvVQQ 2062
Cdd:pfam02463 290 LLAKEEEELKSELLKLE----RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE-----EEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2063 REEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERlKQSAEEQAQAQAQAQAAAEKLRK 2142
Cdd:pfam02463 361 LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ-LEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2143 EAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELqrlkaEVTEAA 2222
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG-----LKVLLA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2223 RQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAE------EAARLSVAAQEAARLR 2296
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElplgarKLRLLIPKLKLPLKSI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2297 QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2376
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2377 QLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE 2456
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2457 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA-KQLREE 2535
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEeKIKEEE 834
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 2536 QQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRA 2609
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2268-2689 |
4.13e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2268 LEEEAEKmkqvAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2346
Cdd:COG1196 205 LERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2347 RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAT 2426
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2427 QEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQ 2506
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2507 RERFIEQEKAKLEQLFQDEVA----KAKQLREEQQRQQQQMEQEKQELMA-----SMEEARRRQREAEEGVRRKQEELQH 2577
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEAllelLAELLEEAALLEAALAELLEELAEAaarllLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2578 LEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALPNGRDAPDGPSVEAEPEytfegLRQKVPAQ 2657
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA-----ALAAALAR 594
|
410 420 430
....*....|....*....|....*....|..
gi 254675119 2658 QLQEAGILSQEELQRLAQGHTTVAELTQREDV 2689
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1791-2607 |
5.82e-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: 85.88 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1791 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLTEKLAAISEATRlKTEAE 1855
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1856 IALKEKEAENERLRRLAED-EAFQRRRLEEQAALHKAdiEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMA 1931
Cdd:TIGR02168 229 LLVLRLEELREELEELQEElKEAEEELEELTAELQEL--EEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1932 LKVSFEKAAAGKAELELELgrirsnaEDTMRSKEQAELEAARQRQlaaeeeqrRREAEERVQRSLAAEEEAARqrkvalE 2011
Cdd:TIGR02168 307 LRERLANLERQLEELEAQL-------EELESKLDELAEELAELEE--------KLEELKEELESLEAELEELE------A 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2012 EVERLKAKVEEARRLRERAEQESArQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARR 2090
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVA-QLELQIASLNNEIErLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2091 AAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADaeme 2170
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG---- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2171 khkkfAEQTLRQKAQVEQElttLRLQLEETdhqksiLDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIE 2250
Cdd:TIGR02168 521 -----ILGVLSELISVDEG---YEAAIEAA------LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2251 AENRALILRDKDNTQRF---LEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEED------------------LAQQRA 2308
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVakdLVKFDPKLRKALSYLlGGVLVVDDLDNALELAKKLRpgyrivtldgdlvrpggvITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2309 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLK 2388
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2389 LRMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA 2468
Cdd:TIGR02168 747 ERIAQLSKELTELEA-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2469 KLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQ 2548
Cdd:TIGR02168 820 ANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELE 897
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 2549 ELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2607
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1234-1939 |
5.93e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.79 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1234 QIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSES 1313
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1314 VIQEYVDLRTRYSELttltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ 1393
Cdd:TIGR00618 302 VTQIEQQAQRIHTEL------------------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1394 ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVR----LQLETTERQ 1469
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkqqeLQQRYAELC 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1470 RGGAEGELQALRARAEEAE--AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQA 1547
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQesAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1548 EEAERRLRQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQlreeaerraqqqaeaerare 1627
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQ-----LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------------------- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1628 eaerelerWQLKANEALRLRLQAEEVaqQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA 1707
Cdd:TIGR00618 579 --------DNRSKEDIPNLQNITVRL--QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1708 QQ---RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLAS-KARAEEESRST 1783
Cdd:TIGR00618 649 HAlqlTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASS 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1784 SEKSK--QRLEAEA---GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeiaL 1858
Cdd:TIGR00618 729 SLGSDlaAREDALNqslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------L 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1859 KEKEAENERLRRLAEDEafqrrrLEEQAALHKADIEERLAQLRKASES--ELERQKGLVEDTLRQRRQVEEEIMALKVSF 1936
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDI------LNLQCETLVQEEEQFLSRLEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
...
gi 254675119 1937 EKA 1939
Cdd:TIGR00618 876 DKL 878
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
166-264 |
7.02e-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: 76.57 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 166 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 254675119 246 -VDVPQPDEKSIITYVSSLY 264
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1415-2358 |
7.21e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1415 QQKRSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEA----- 1489
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1490 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR------EKQRALQALDELRLQAEEAE-----RRLRQAE 1558
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1559 AERARQVQVALETaqrsaEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQaeaerareeaerelerwql 1638
Cdd:TIGR02169 311 AEKERELEDAEER-----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1639 kanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQEL 1717
Cdd:TIGR02169 367 ---EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1718 IRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAE 1794
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1795 AGRFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLTEKLAAiseatrlktEAEIALKEKEAENER---LRRL 1871
Cdd:TIGR02169 524 HGTVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKM 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1872 AEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQVEEEIMalkVS-----FEKAAAgkael 1946
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRM---VTlegelFEKSGA----- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1947 eLELGRIRSNAEDTMRSKEQAELEAARQRqlaaeeeqrrreaeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRL 2026
Cdd:TIGR02169 655 -MTGGSRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQE 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2027 RERAEQE----SARQLQLAQEAAQKRLQAEEkahafvVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQA 2102
Cdd:TIGR02169 711 LSDASRKigeiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2103 EREAAQSRKQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQ 2182
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2183 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENraliLRDKD 2262
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSE 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2263 NTQRfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2342
Cdd:TIGR02169 922 LKAK-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
|
970
....*....|....*.
gi 254675119 2343 EQARRLQEDKEQMAQQ 2358
Cdd:TIGR02169 1000 EERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1637-2497 |
1.30e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1637 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1712
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1713 --AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1790
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1791 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLTEKLAAISEatrlKTEAEIALKEKEAENERLRR 1870
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINELEEE----KEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1871 LAEDEAFQRRRLEEQAalhkADIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEImalkvsfEKAAAGKAELELEL 1950
Cdd:TIGR02169 463 DLSKYEQELYDLKEEY----DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1951 GRIrsnaedtmRSKEQAELEAARQRQLaaeeeqrrreaeervqRSLAAEEEAarqrkVALEEVERLKA------------ 2018
Cdd:TIGR02169 531 GSV--------GERYATAIEVAAGNRL----------------NNVVVEDDA-----VAKEAIELLKRrkagratflpln 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2019 KVEEARRLRERAEQESARQLQLAQEAAQKRLqaeEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEA 2098
Cdd:TIGR02169 582 KMRDERRDLSILSEDGVIGFAVDLVEFDPKY---EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2099 REQAEREAAQSRKQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2175
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2176 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSVRVQMEELGKLKARIEAENRA 2255
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2256 L--ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAEL 2333
Cdd:TIGR02169 817 IeqKLNRLTLEKEYLEKEIQELQEQRIDL-----KEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGD 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2334 LQQQKELAQEQARRLQEDKEQMAQQlVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2413
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2414 EIgeklhrtelatqEKVTLVQTLEIQrqqsdhDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2493
Cdd:TIGR02169 966 EI------------RALEPVNMLAIQ------EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
....
gi 254675119 2494 QKSF 2497
Cdd:TIGR02169 1028 NENF 1031
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3465-3503 |
1.30e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 73.13 E-value: 1.30e-15
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3465 LLEAQVATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 3503
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2334-2755 |
1.71e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2334 LQQQKELAqEQARRLQEDKEQM-AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQA 2412
Cdd:COG1196 205 LERQAEKA-ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2413 EEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2492
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2493 LQKSFLSEKDSLLQRERFIEQEKAKLEQLfqdevaKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQ 2572
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2573 EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgpsveaepeytFEGLRQ 2652
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-------------------LLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2653 KVPAQQLQEAGILSQEELQRLAQGHTTVAELTQREDVYRYLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALILLE 2732
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420
....*....|....*....|...
gi 254675119 2733 AQAASGFLLDPVRNRRLTVNEAV 2755
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAV 601
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
169-264 |
1.89e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.09 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 169 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 247
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 254675119 248 VPQPDEKSIITYVSSLY 264
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
166-265 |
2.13e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.00 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 166 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 254675119 246 VDV--PQPDEKSIITYVSSLYD 265
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4043-4081 |
3.13e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.13e-15
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 4043 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4081
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
166-269 |
3.19e-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: 74.70 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 166 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 254675119 246 VDV--PQPDEKSIITYVSSLYDAMPR 269
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2806-2844 |
4.86e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 4.86e-15
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 2806 LLEAQIATGGIIDPVHSHRVPVDVAYKRGYFDEEMNRIL 2844
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1067-1932 |
1.20e-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: 81.65 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1067 SELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATK--ASLKKLRAQAEAQ 1144
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1145 QPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLaqtdvrQRELEQLGRQLRYYRESADPLSAW 1224
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV------KEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1225 LQDAKRRQEQIQAvpiancqaareqlrQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKK 1304
Cdd:TIGR02169 317 LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1305 PKvqsgsesviQEYVDLRTRYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqa 1384
Cdd:TIGR02169 383 TR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1385 kAQAELEAQElqRRMQEEVARREeaavDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLE 1464
Cdd:TIGR02169 446 -KALEIKKQE--WKLEQLAADLS----KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1465 TTERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDESQRKRQAEaeLALRVKA------EAEAAREKQR 1535
Cdd:TIGR02169 515 VLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIE--LLKRRKAgratflPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1536 ALQALDE-----LRLQAEEAERRLRQAEAERARQVQV--ALETAQR--------SAEVELQSKRA-----SFAEKTAQLE 1595
Cdd:TIGR02169 589 DLSILSEdgvigFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGILF 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1596 RTLQEEhvtvaqlreeaerraqqqaeaerareeaerelerwqlkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREA 1675
Cdd:TIGR02169 669 SRSEPA----------------------------------------ELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1676 RRRGKAEEQAV---RQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqhEA 1745
Cdd:TIGR02169 709 QELSDASRKIGeieKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EA 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1746 TAATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1824
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1825 DAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIE---ERLAQLR 1901
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIE 937
|
890 900 910
....*....|....*....|....*....|...
gi 254675119 1902 KASESELERQKGL--VEDTLRQRRQVEEEIMAL 1932
Cdd:TIGR02169 938 DPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3724-3762 |
1.23e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.23e-14
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3724 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3762
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1728-2598 |
1.25e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 81.56 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1728 EQQRQLLEEELARLQHEAtaatQKRQELEaELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1807
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKR----KKKEALK-KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1808 L--RALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKtEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1885
Cdd:pfam02463 227 LylDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK-ENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1886 AALHKADIEERlaqlrKASESE---LERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDT-- 1960
Cdd:pfam02463 306 ERRKVDDEEKL-----KESEKEkkkAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkk 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1961 ----MRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR 2036
Cdd:pfam02463 381 leseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2037 QLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEA 2116
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2117 ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLR---QKAQVEQELTTL 2193
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaqlDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2194 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAE 2273
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2274 KMKQVAEEAARLSVAAQEA----ARLRQLAEEDLAQQRALAEKMLKEKMQaVQEATRLKAEAELLQQQKELAQEQARRLQ 2349
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKIDEEEE-EEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2350 EDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhrtELATQEK 2429
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL----EKLAEEE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2430 VTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRER 2509
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2510 FIEQEK-AKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREaeegVRRKQEELQHLEQQRQQQEKL 2588
Cdd:pfam02463 936 EPEELLlEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY----NKDELEKERLEEEKKKLIRAI 1011
|
890
....*....|
gi 254675119 2589 LAEENQRLRE 2598
Cdd:pfam02463 1012 IEETCQRLKE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
968-1877 |
1.45e-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: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 968 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKDPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1045
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1046 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEEVLKTHEEQLKE 1116
Cdd:TIGR02169 250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1117 AQAVPATLQ-ELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1195
Cdd:TIGR02169 320 AEERLAKLEaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1196 qtdvRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvpiancqaareqlrqekalleEIERHGEKVEECQKFAK 1275
Cdd:TIGR02169 390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1276 QYINAIKDYELQLITYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQ 1355
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1356 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQElqrRMQEEVARREEAAVDAQQQKRS-------------IQE 1422
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ELQHLRQSSEAEIQAKA-------QQVEAAER-------------SRMRIEEEIRVVRLQLETTERQ---RGGA-EGELQ 1478
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAvdlvefdPKYEPAFKyvfgdtlvvedieAARRLMGKYRMVTLEGELFEKSgamTGGSrAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1479 ALRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeAEAAREKQRALQALDELRLQAEEAERRlRQAE 1558
Cdd:TIGR02169 666 ILFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1559 AERARQVQVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERraqqqaeaerareeaerelERWQL 1638
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIE-NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------SRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1639 KANEALRLRlqAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAvRQRELAEQELEKQRQLAEGTAQQRlAAEQELI 1718
Cdd:TIGR02169 796 IQAELSKLE--EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEIENLNGKKE-ELEEELE 871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1719 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE--AEAG 1796
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEEL 951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1797 RFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLTEKLAaiseatRLKTEAEiALKEKEAENERLRRLA 1872
Cdd:TIGR02169 952 SLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILERIEEYEKKKREV 1019
|
....*
gi 254675119 1873 EDEAF 1877
Cdd:TIGR02169 1020 FMEAF 1024
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1103-1601 |
1.61e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1103 AEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAqaeaqqpvfnTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1182
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERERE----------ELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1183 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQ---AVPIANCQAAREQLRQEKALLEE 1259
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1260 IERHGEKVEECQKFAkqyinaikdyelqlitykaqlepvasPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfI 1339
Cdd:PRK02224 389 LEEEIEELRERFGDA--------------------------PVDLGNAEDFLEELREERDELREREAELEAT-------L 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1340 SETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAKAQAELEAQ----- 1393
Cdd:PRK02224 436 RTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEDLVEAEDRierle 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1394 ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvRLQLETTERQRGGA 1473
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESLER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1474 EGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDESQRKRQAEAELAlrvKAEAEAARE-KQRALQALdelrlqaE 1548
Cdd:PRK02224 594 IRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL-------E 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 1549 EAERRLRQAEAERARqVQVALETAQRSAE--VELQSKRASFAEKTAQLErTLQEE 1601
Cdd:PRK02224 664 QVEEKLDELREERDD-LQAEIGAVENELEelEELRERREALENRVEALE-ALYDE 716
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
979-1601 |
1.72e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 979 QEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKDPAR--ECAQRIAEQQKAQaeveglgkgVARLSAEAEKVlalp 1056
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKrvEIARKAEDARKAE---------EARKAEDAKKA---- 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1057 EPSPAAPTLRSELELTlgKLEQVRSL-SAIYLEKLKTISLVIRSTQG--AEEVLKTHE-----EQLKEAQAVPATLQELE 1128
Cdd:PTZ00121 1179 EAARKAEEVRKAEELR--KAEDARKAeAARKAEEERKAEEARKAEDAkkAEAVKKAEEakkdaEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1129 ATKASLKKLRAQAEAQQPVFNTLRDELRGAQEV--GERLQQRHGERDVE------------------VERWRERVTQLLE 1188
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKkkADEAKKAEEKKKADeakkkaeeakkadeakkkAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1189 RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQ--AVPIANCQAAREQLRQEKALLEEIERHGE- 1265
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkAEEKKKADEAKKKAEEDKKKADELKKAAAa 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1266 ---------KVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYI 1336
Cdd:PTZ00121 1417 kkkadeakkKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1337 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQR--QLAEAHAQAKAQAELEAQELQR----RMQEEVARREE-- 1408
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKKAEEKKKADELKKAEELKKaeekKKAEEAKKAEEdk 1576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1409 --AAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSR-----MRIEEEIRVVRLQLETTERQRGGAEGELQA-- 1479
Cdd:PTZ00121 1577 nmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKae 1656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1480 ---------LRARAEE----------AEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvKAEAEAAREKQRALQAl 1540
Cdd:PTZ00121 1657 eenkikaaeEAKKAEEdkkkaeeakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK---KAEELKKAEEENKIKA- 1732
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1541 DELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKrasfaEKTAQLERTLQEE 1601
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK-----EKEAVIEEELDEE 1788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1107-1583 |
2.08e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.20 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1107 LKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRH---GERDVEVERWrERV 1183
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1184 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAW-LQDAKRRQEQIQavpiANCQAAREQLRQEKALLEEIER 1262
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ----QRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1263 HGEKVEEcQKFAKQYINAIKDYELQLITYKAQLEPVAspakkpkVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET 1342
Cdd:COG4717 228 ELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLG-------LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1343 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmqeevARREEAAVDAQQQKRSIQE 1422
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE-----AEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ELQHLRQSSEAEIQAKAQQVEAAErsrmRIEEEIRVVRLQLE--TTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1500
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQ----ELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1501 LRRQVQDESQRKRQAEAElalrvkaeaeaarekqralQALDELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEV 1578
Cdd:COG4717 451 LREELAELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYRE 511
|
....*
gi 254675119 1579 ELQSK 1583
Cdd:COG4717 512 ERLPP 516
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1144-2054 |
2.47e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 80.60 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1144 QQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1213
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1214 YRESADPLSAWLQ-DAKRRQEQIQAVP--IANCQAAREQLRQEKALLE-EIERHGEKVEECQKFAKQYINAIKDYELQLI 1289
Cdd:pfam01576 83 RLEEEEERSQQLQnEKKKMQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1290 TYKAQLEPVASPAKK-PKVQSGSESVIQEyVDLRTRYSElttltsqyikfisETLRRMEEEERLAEQQRAEERERLAEVE 1368
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1369 AalekqrQLAEAHAQAkAQAELEAQELQRRMQEEVARREEaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQqveaAERS 1448
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1449 RMRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeA 1527
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1528 EAAREKQRALQALDELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEktAQLERTLQEEHVTVAQ 1607
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1608 LREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAqadaekqkeeaereaRRRGKAEEQAVR 1687
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLS---------------TRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1688 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK------ 1761
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1762 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1820
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1821 LAEEDAARQRAEAERVLTEKLAA---ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERL 1897
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1898 AQLRKASEselERQKGLVedtlRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQL 1977
Cdd:pfam01576 734 QARDEQGE---EKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1978 AAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEK 2054
Cdd:pfam01576 807 MKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEK 884
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
620-798 |
2.48e-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: 75.17 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 620 LHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQ 699
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 700 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLQKLQETLRRKYSCDrtiTVTRLEDLLQDAQDEKEQLNEY 779
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 254675119 780 KGHLSGLAKRAKAIVQLKP 798
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
35-148 |
2.83e-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: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 35 DEQDERdrvqkkTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHK 104
Cdd:cd21219 2 GSREER------AFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKK 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 254675119 105 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 148
Cdd:cd21219 64 VENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1376-1746 |
3.54e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.40 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1376 QLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQsseAEIQAKAQQVeaAERSRMRIEEE 1455
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ---AEMDRQAAIY--AEQERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1456 IRVVRLQLEttERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEAELALRVK-AEAEAAREKQ 1534
Cdd:pfam17380 348 RELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1535 RALQALDELRLQAEEA-ERRLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvtvaqlreeae 1613
Cdd:pfam17380 417 QQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE------------ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1614 rraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQavrQRELA 1692
Cdd:pfam17380 470 --------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE---RRREA 538
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1693 EQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAT 1746
Cdd:pfam17380 539 EEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1995-2688 |
4.55e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1995 SLAAEEEAARQRKVALEEVERLKAKVEEARRlRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQE 2074
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2075 QNMLDRLRSEaeaarraaeeaeeareqaereaaqsrKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2154
Cdd:PTZ00121 1154 VEIARKAEDA--------------------------RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2155 EQAALKQKQAADAEMEKHK---KFAEQTlRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2231
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAeavKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2232 lfSVRVQMEELGKLKARIEAENraliLRDKDNTQRFLEE---EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA 2308
Cdd:PTZ00121 1287 --EEKKKADEAKKAEEKKKADE----AKKKAEEAKKADEakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2309 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLveetqgfqRTLEAERQRQLEMSAEAErlK 2388
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADEL--------KKAAAAKKKADEAKKKAE--E 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2389 LRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvqtleiQRQQSDHDAERLREAiAELEREKEKLKQEA 2468
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------KADEAKKKAEEAKKA-DEAKKKAEEAKKKA 1499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2469 KLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQ 2548
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2549 ELMAsmEEARRRQREAEEGVRRKQEElqhlEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAlahSEIATTQAASTKALP 2628
Cdd:PTZ00121 1580 LRKA--EEAKKAEEARIEEVMKLYEE----EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV---EQLKKKEAEEKKKAE 1650
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 2629 NGRDAPDGPSVEAEPEY--TFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTVAELTQRED 2688
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
166-267 |
5.71e-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: 71.27 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 166 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 254675119 246 -VDVPQPDEKSIITYVSSLYDAM 267
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
44-149 |
6.31e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 70.79 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 44 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRH 117
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMAS 73
|
90 100 110
....*....|....*....|....*....|..
gi 254675119 118 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21213 74 KRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
164-261 |
7.47e-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: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 239
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 254675119 240 LLDPEDVDVPQPDEKSIITYVS 261
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
164-264 |
7.82e-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: 70.87 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 243
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 254675119 244 ED-VDVPQPDEKSIITYVSSLY 264
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
41-145 |
8.87e-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: 70.25 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 41 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRH 117
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEE 77
|
90 100
....*....|....*....|....*....
gi 254675119 118 R-QVKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21225 78 DlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
990-1590 |
2.19e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 990 ELKDIRLQLEAcETRTVHRLRlpldkdPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1069
Cdd:COG4913 236 DLERAHEALED-AREQIELLE------PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1070 ELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEvlktheEQLKeaqavpatlQELEATKASLKKLRAQAEAQQPVFN 1149
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLE---------REIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1150 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLSAWLQDAK 1229
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1230 RRQEQ-----IQAVPIAnC---QAAREQLRQEKAlleeIER--HGEKV-----EECQKFAKQYINAIKDyELQLITYKAQ 1294
Cdd:COG4913 447 DALAEalgldEAELPFV-GeliEVRPEEERWRGA----IERvlGGFALtllvpPEHYAAALRWVNRLHL-RGRLVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1295 LEPVASPAKKPKVQSGSEsviqeyvdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-EV 1367
Cdd:COG4913 521 TGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1368 EAALEK--QRQLAEAH------AQAKAQAELEAQELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEIqaka 1439
Cdd:COG4913 587 GTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEI---- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1440 qQVEAAERSRMRIEEEIRvvrlQLETterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1519
Cdd:COG4913 662 -DVASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1520 -ALRVKAEAEAAREKQRALQALDELRlqAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEK 1590
Cdd:COG4913 730 dELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1150-1975 |
2.97e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.92 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1150 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQRelEQLGRqlryYRESADPLSAw 1224
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQ--EKIER----YQADLEELEE- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1225 lqdakRRQEQIQAVPIANCQAAREQLRQEKAlLEEIER-------HGEKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1296
Cdd:PRK04863 363 -----RLEEQNEVVEEADEQQEENEARAEAA-EEEVDElksqladYQQALDVQQTRAIQYQQAVQALErAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1297 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERlaeveaALEKQRQ 1376
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR------RLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1377 LAEAHAQAKAQ-AELEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1455
Cdd:PRK04863 511 LAEQLQQLRMRlSELEQRLRQQQRAERLLAE---FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1456 IRvvrlqletterqrggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDE---SQRKRQAEAELALRVKAEAEAARE 1532
Cdd:PRK04863 588 LE------------------QLQARIQRLAARAPAWLAAQDALARLREQSGEEfedSQDVTEYMQQLLERERELTVERDE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1533 KQRALQALDE--LRLQAEEAER--RLRQAeAERARQV-------QVALETA---------QRSAEVELQSKRAsfAEKTA 1592
Cdd:PRK04863 650 LAARKQALDEeiERLSQPGGSEdpRLNAL-AERFGGVllseiydDVSLEDApyfsalygpARHAIVVPDLSDA--AEQLA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1593 QLERTLQE------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEAL--RLRLQAEEVAQQks 1658
Cdd:PRK04863 727 GLEDCPEDlyliegdpdsfdDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLFGR---AAREKRieQLRAEREELAER-- 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1659 LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEEL 1738
Cdd:PRK04863 802 YATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLN-------RRRVELERALADHESQEQQQRSQLEQAKEGL 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1739 ARL-QHEATAATQKRQELEAELAKVRAEMEvllaskaRAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEEA 1815
Cdd:PRK04863 875 SALnRLLPRLNLLADETLADRVEEIREQLD-------EAEEAKRFVQQHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQA 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1816 KRQRQlaeedAARQRAEAervLTEklaAISEATRLKTEAEIALKEKEAE-NERLR-RLAEDEAfQRRRLEEQAALHKA-- 1891
Cdd:PRK04863 948 QQTQR-----DAKQQAFA---LTE---VVQRRAHFSYEDAAEMLAKNSDlNEKLRqRLEQAEQ-ERTRAREQLRQAQAql 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1892 -DIEERLAQLRKASeselerqkglveDTLRQRRQ-VEEEIMALKVSF-----EKAAAGKAELELEL--GRIRSNAEDTMR 1962
Cdd:PRK04863 1016 aQYNQVLASLKSSY------------DAKRQMLQeLKQELQDLGVPAdsgaeERARARRDELHARLsaNRSRRNQLEKQL 1083
|
890
....*....|...
gi 254675119 1963 SKEQAELEAARQR 1975
Cdd:PRK04863 1084 TFCEAEMDNLTKK 1096
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3058-3096 |
3.04e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 3.04e-13
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3058 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPELHEKL 3096
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1397-1921 |
3.70e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1397 RRMQEEVA---RREEAAVDAQQQKRSiqeeLQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggA 1473
Cdd:COG4913 228 DALVEHFDdleRAHEALEDAREQIEL----LEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--L 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1474 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAER 1552
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1553 RLrQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTlqeehvtvaqlreeaerraqqqaeaerareeaERE 1632
Cdd:COG4913 381 EF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--------------------------------EAE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1633 LERwqLKAN--------EALRLRLQAE---------------EVAQ-----------------------QKSLAQA---- 1662
Cdd:COG4913 428 IAS--LERRksniparlLALRDALAEAlgldeaelpfvgeliEVRPeeerwrgaiervlggfaltllvpPEHYAAAlrwv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1663 DAEKQKEEAEREARRRGKAEEQAVR--QRELAEqELEKQRQLAEGTAQQRLAA---------EQELIRL-RAETEQG--- 1727
Cdd:COG4913 506 NRLHLRGRLVYERVRTGLPDPERPRldPDSLAG-KLDFKPHPFRAWLEAELGRrfdyvcvdsPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1728 ------------------------EQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1783
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1784 S--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEklaaiseatrlkteaE 1855
Cdd:COG4913 665 SaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---------------L 729
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1856 IALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQ 1921
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1088-1938 |
4.76e-13 |
|
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: 76.16 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1088 EKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQ--PVFNTLRDELRGAQEVGERL 1165
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEEriDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1166 QQRHGERDVEVERWR---ERVTQLLERWQAVLAqtdvrqRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIAN 1242
Cdd:pfam02463 260 IEKEEEKLAQVLKENkeeEKEKKLQEEELKLLA------KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1243 CQAAREQLRQEKALLEEIERHGEKVEEC-QKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDL 1321
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELeKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1322 RTRYSELTTLTSQYIKFISEtlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQE 1401
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILE-----EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1402 EVARREEAAVDAQQQKrsiqeelqhlrqSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALR 1481
Cdd:pfam02463 489 LLSRQKLEERSQKESK------------ARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1482 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAER 1561
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1562 ARQVQVALETaQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1641
Cdd:pfam02463 637 LKESAKAKES-GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1642 EALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1721
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1722 ----AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR 1797
Cdd:pfam02463 796 lkaqEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1798 FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE--AENERLRRLAEDE 1875
Cdd:pfam02463 876 EEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELllEEADEKEKEENNK 955
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1876 AFQRRRlEEQAALHKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEEEIMALKVSFEK 1938
Cdd:pfam02463 956 EEEEER-NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE---KERLEEEKKKLIRAIIEE 1014
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
63-146 |
5.19e-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: 68.39 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 63 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGN 134
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGH 100
|
90
....*....|..
gi 254675119 135 PKLTLGLIWTII 146
Cdd:cd21223 101 REKTLALLWRII 112
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
164-264 |
7.11e-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: 67.75 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 243
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 254675119 244 ED-VDVPQPDEKSIITYVSSLY 264
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1347-2054 |
7.82e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.49 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1347 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEAQELQRRMQE----EVARREEAAVdaqQQKRSIQE 1422
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyegyELLKEKEALE---RQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ELQHLRQS---SEAEIQAKAQQVEAAERSRMRIEEEIRVVrlqletterqrggAEGELQALRARAEEAEAqkrqaqeEAE 1499
Cdd:TIGR02169 245 QLASLEEElekLTEEISELEKRLEEIEQLLEELNKKIKDL-------------GEEEQLRVKEKIGELEA-------EIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1500 RLRRQVQDESQRKRQAEAELAlrvKAEAEaarekqralqaLDELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEVE 1579
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLA---KLEAE-----------IDKLLAEIEELEREIEEERKRRD-----KLTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1580 LQSKRASFAEKTAQLERTLQEehvtvaqlreeaerraqqqaeaeraREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1659
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDE-------------------------LKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1660 AQADAEKQkeeaeREARRRGKAEEQAVRqrELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1739
Cdd:TIGR02169 421 ELADLNAA-----IAGIEAKINELEEEK--EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1740 RLQHEATAATQ-----KRQELE------------AELAKVRAEMEVLLASKA----------------------RAEEES 1780
Cdd:TIGR02169 494 EAEAQARASEErvrggRAVEEVlkasiqgvhgtvAQLGSVGERYATAIEVAAgnrlnnvvveddavakeaiellKRRKAG 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1781 RST-----------SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE-DAARQRAEAERVLT------EKLA 1842
Cdd:TIGR02169 574 RATflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDiEAARRLMGKYRMVTlegelfEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1843 AI-----------SEATRLKTEA-EIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLR-KASESELE 1909
Cdd:TIGR02169 654 AMtggsraprggiLFSRSEPAELqRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEiEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1910 RQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELeaaRQRQLAAEEEQRRREAE 1989
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI---PEIQAELSKLEEEVSRI 810
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1990 ERVQRSLAAEEEAARQRKVALE-EVERLKAKVE--EARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2054
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEkEIQELQEQRIdlKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1102-1598 |
1.17e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1102 GAEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELrgAQEVGERLQQRHGERDVEVERWRE 1181
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1182 RVTQLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEI 1260
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1261 ErhgEKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIS 1340
Cdd:COG4913 397 E---EELEALEEALAEAEAALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAELEAQELQRRM- 1399
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1400 ----------QEEVARREEAA-VDAQQQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKAQQVEA 1444
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1445 AERSRMRIEEEIRVVRLQLETTERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDESQRK 1512
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1513 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSKRASFAEK 1590
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 254675119 1591 TAQLERTL 1598
Cdd:COG4913 782 LNRAEEEL 789
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4312-4350 |
1.49e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 1.49e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 4312 LLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMVDRI 4350
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
166-265 |
1.85e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 66.21 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 166 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 241
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 254675119 242 DPEDVdVPQPDEKSIITYVSSLYD 265
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1361-1886 |
3.32e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 73.35 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1361 RERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQ 1440
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1441 QVEAAERSRMRIEEEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEA 1517
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1518 ELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1597
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1598 LQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR 1677
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1678 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA 1757
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1758 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1837
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 254675119 1838 TEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1886
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3134-3172 |
3.39e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.39e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3134 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETNRAL 3172
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1475-2053 |
3.52e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 73.35 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1475 GELQALRARAEEA--EAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAeAEAARekqralqaldeLRLQAEEAER 1552
Cdd:COG3899 699 GERDRAARLLLRAarRALARGAYAEALRYLERALELLPPDPEEEYRLALLLEL-AEALY-----------LAGRFEEAEA 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1553 RLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQlreeaerrAQQQAEAERAREEAERE 1632
Cdd:COG3899 767 LLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAE--------RLGDRRLEARALFNLGF 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1633 LERWQLKANEALRLRLQAEEVAQQKSLAQADAekqkeeaEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1712
Cdd:COG3899 839 ILHWLGPLREALELLREALEAGLETGDAALAL-------LALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAA 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1713 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskQRLE 1792
Cdd:COG3899 912 ALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAA---------AAAA 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1793 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1872
Cdd:COG3899 983 AAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAAL 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1873 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGR 1952
Cdd:COG3899 1063 AAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAAL 1142
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1953 IRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQ 2032
Cdd:COG3899 1143 ALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAAL 1222
|
570 580
....*....|....*....|.
gi 254675119 2033 ESARQLQLAQEAAQKRLQAEE 2053
Cdd:COG3899 1223 LLLLLLAALALAAALLALRLL 1243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3389-3427 |
3.67e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 3.67e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3389 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3427
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
166-261 |
3.79e-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: 65.49 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 166 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 244
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 254675119 245 DVDVPQPDEKSIITYVS 261
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1112-1834 |
3.86e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.45 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1112 EQLKEAQAvpATLQELEATKASLKKLRAQAEAQQPV------FNTLRDELRGAQEVGERLQQRHGERDVEVERWRERV-- 1183
Cdd:COG3096 316 EELSARES--DLEQDYQAASDHLNLVQTALRQQEKIeryqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVds 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1184 --TQLLERWQAVlaqtDVRQRE----------LEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQ------A 1245
Cdd:COG3096 394 lkSQLADYQQAL----DVQQTRaiqyqqavqaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsvadA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1246 AREQLRQEKALLEEIERHGEKVEECQKfAKQYINAIKDYELQLitykAQLEPVAspakkpkvqsgsesviQEYVDLRTRY 1325
Cdd:COG3096 470 ARRQFEKAYELVCKIAGEVERSQAWQT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1326 S---ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAE---------LEAQ 1393
Cdd:COG3096 529 RqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaarapawLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1394 ELQRRMQEEVArreEAAVDAQQQKRSIQEELQHLRQsseaeiqAKAQQVEAAERsRMRIEEEIRvvRLQletterQRGGA 1473
Cdd:COG3096 609 DALERLREQSG---EALADSQEVTAAMQQLLERERE-------ATVERDELAAR-KQALESQIE--RLS------QPGGA 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1474 E-GELQALRAR-----------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQR 1511
Cdd:COG3096 670 EdPRLLALAERlggvllseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVF 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1512 KRQaEAELALRVKAE---------------AEAAREKQralqaLDELRLQAEE-----AERRLRQAEAER---------A 1562
Cdd:COG3096 750 DAE-ELEDAVVVKLSdrqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1563 RQVQVALETaqrSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRA-------QQQAEAERAREEAERELER 1635
Cdd:COG3096 824 GHLAVAFAP---DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1636 WQLKANEALR-LRLQAEEVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLA 1712
Cdd:COG3096 901 ELDAAQEAQAfIQQHGKALAQLEPLVAVlQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLG 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1713 AEQELI-RLRAETEQGEQQRQLLEEELARLQHEATAATQKR--------------QELEAELakvrAEMEVLLAskARAE 1777
Cdd:COG3096 981 ENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAE 1054
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1778 EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1834
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1345-2468 |
5.11e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 72.90 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1345 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHA----QAKAQAEL--EAQELQRRMQ------EEVARREE 1408
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalqeQLQAETELcaEAEEMRARLAarkqelEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1409 AAVDaQQQKRSIQeeLQHLRQSSEAEIQAKAQQVEAAERSRMrieeeirvvRLQLETTErqrggAEGELQALRARAEEAE 1488
Cdd:pfam01576 82 SRLE-EEEERSQQ--LQNEKKKMQQHIQDLEEQLDEEEAARQ---------KLQLEKVT-----TEAKIKKLEEDILLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1489 AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKaeaeaAREKQRALQALDELRLQAEEAERRlrqaEAERARQVQVA 1568
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSK-----LKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1569 LETAQRSAEVELQskrASFAEKTAQLERtlQEEHVTVAQLreeaerraqqqaeaerareeaerELERWQLKANEALRlrl 1648
Cdd:pfam01576 216 ESTDLQEQIAELQ---AQIAELRAQLAK--KEEELQAALA-----------------------RLEEETAQKNNALK--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1649 QAEEVAQQKSLAQADAEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTaQQRLAAEQELiRLRAETEQGE 1728
Cdd:pfam01576 265 KIRELEAQISELQEDLESERA-----------ARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQEL-RSKREQEVTE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1729 QQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfREL 1801
Cdd:pfam01576 332 LKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlQQAKQDSEHKR-KKL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1802 AEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-------------LTEKLAAIS-----------EATRLKTEAEIA 1857
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegknikLSKDVSSLEsqlqdtqellqEETRQKLNLSTR 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1858 LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEIMALKVSFE 1937
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLE 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1938 KAAAGKAELELELGRIRSNAEDTMrskeqaeLEAARQRQLAAEEEQRRREAEErvqrsLAAEEEAARQRKVALEEVERLK 2017
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAE 630
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2018 AKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqnmLDRLRSEAEAARRAAEEAEE 2097
Cdd:pfam01576 631 AREKETRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELER 685
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2098 AREQAEREAAQSRKQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalKQKQAADAEMEKHKKfae 2177
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR--- 745
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2178 QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2257
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2258 LRDKDNTQRFLEEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2337
Cdd:pfam01576 826 AQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSN 904
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2338 KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQrqleMSAEAERLKLRMAEMSRAQ---------------ARAE 2402
Cdd:pfam01576 905 TELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ----LERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLE 980
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2403 EDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA 2468
Cdd:pfam01576 981 EQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2730-2768 |
6.72e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 6.72e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 2730 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2768
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
166-266 |
7.54e-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: 64.68 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 166 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 245
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 254675119 246 VdVPQPDEKSIITYVSSLYDA 266
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3967-4005 |
8.58e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 8.58e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3967 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4005
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3800-3838 |
9.10e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 9.10e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3800 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3838
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1428-2054 |
1.51e-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: 71.41 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1428 RQSSEAEIQAKAQQVEA--AERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1501
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1502 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1581
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1582 SKRASFAEKTAQLERTLQEEHVT-VAQLREEAERRAQQQAEAERAREEAERELE---RWQLKAN------EALRLRLQAE 1651
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALEselREQLEAGklefneEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1652 EVAQQKSLAQADAEK--QKEEAEREARRRGKAEEQAVRQRELAEQELekqrqlaegtAQQRLAAEQELIRLRAETEQGEQ 1729
Cdd:pfam12128 448 ELKLRLNQATATPELllQLENFDERIERAREEQEAANAEVERLQSEL----------RQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1730 QRQLLEEelARLQHEATAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAE 1803
Cdd:pfam12128 518 RQSALDE--LELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1804 EAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE 1883
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1884 EQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEkaaagkAELELELGRIRSN--AEDTM 1961
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSG 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1962 RSKEQAELEAARQRQLAAE-EEQRRREAEERVQRSLAAEEEAARQRKVA------------LEEVERLKAKVEEARRLRE 2028
Cdd:pfam12128 745 AKAELKALETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAIS 824
|
650 660
....*....|....*....|....*.
gi 254675119 2029 RAEQESARQlqlaQEAAQKRLQAEEK 2054
Cdd:pfam12128 825 ELQQQLARL----IADTKLRRAKLEM 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1680-1896 |
1.70e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1759
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1760 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1835
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1836 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEER 1896
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
964-1600 |
2.55e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 964 SRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACEtrtvhrLRLPLDKDPARECAQRIAEQQKAQA-EVEGLGKGV 1042
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLT------LRSQLLTLCTPCMPDTYHERKQVLEkELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1043 ARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVlKTHEEQLKEAQAVPA 1122
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1123 TLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE-------------RWRERVTQLLER 1189
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREiscqqhtltqhihTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1190 WQAVLAQTDVRQRELEQLGRQLRYYR-------------ESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKAL 1256
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1257 LEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTRYSELTTL 1331
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1332 TSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAV 1411
Cdd:TIGR00618 555 RKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1412 DAQQQKRsIQEELQHLRQssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALraraEEAEAQK 1491
Cdd:TIGR00618 634 LQQCSQE-LALKLTALHA--LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML----AQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1492 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAeaarekqralQALDELRLQAEEAERRLRQAEAERARQVQVALET 1571
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALN----------QSLKELMHQARTVLKARTEAHFNNNEEVTAALQT 776
|
650 660 670
....*....|....*....|....*....|.
gi 254675119 1572 AQRSAEV--ELQSKRASFAEKTAQLERTLQE 1600
Cdd:TIGR00618 777 GAELSHLaaEIQFFNRLREEDTHLLKTLEAE 807
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
46-152 |
2.71e-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: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 46 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHR 118
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1315-1813 |
3.32e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 70.37 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1315 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaqakaqaeleaqE 1394
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1395 LQRRMQEEVARREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrgg 1472
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1473 aegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQR----------KRQAEAELAlRVKA-------EAEAAREKQR 1535
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALE-RAKQlcglpdlTADNAEDWLE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1536 ALQA-LDELRLQAEEAERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVTVAQLreeae 1613
Cdd:PRK04863 446 EFQAkEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL----- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1614 rraqqqaeaerareeaerelerwqlkanEALRLRLQAeevAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE 1693
Cdd:PRK04863 516 ----------------------------QQLRMRLSE---LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1694 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEATAATQKRQELEAELAKvraemevlL 1770
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------L 636
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 254675119 1771 ASKARAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1813
Cdd:PRK04863 637 LERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1655-1864 |
3.96e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.29 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1655 QQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAegtaQQRLAAeQELIRLRAETEQGEQQRQLL 1734
Cdd:PRK09510 68 QQQQKSAKRAEEQRKK---------KEQQQAEELQQKQAAEQERLKQLE----KERLAA-QEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1735 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1814
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAE---AKKKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1815 AKRQRQLAEEDAARQ-RAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1864
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1321-1977 |
4.32e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 69.40 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1321 LRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQ---AELEAQELQR 1397
Cdd:pfam07111 53 LELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEglrAALAGAEMVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1398 RMQEEVARREeaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSrmrieeeirvvrlqLETTERQRGGAEGEL 1477
Cdd:pfam07111 132 KNLEEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1478 QalraraeeaeaqkrQAQEEAERLRRQVqdeSQRKRQAEAELALrvkaeAEAAReKQRALQALDELRLQAEEAERRLRQA 1557
Cdd:pfam07111 193 A--------------EAQKEAELLRKQL---SKTQEELEAQVTL-----VESLR-KYVGEQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1558 EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLreeaerraqqqaeaeraREEAERELERWQ 1637
Cdd:pfam07111 250 TMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEF-----------------PKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1638 LKANeALRLRLQAEEVAQQKSLAQADAEkqkeEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLAEGTAQQRLAAEQ 1715
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQ----VAELQEQVTSQSQEQAILQRALQDKaaEVEVERMSAKGLQMELSRAQE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1716 ELIRLRAETEQGEQQRQL-----------LEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASK---ARAEEESR 1781
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKvalAQLRQESC 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1782 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1861
Cdd:pfam07111 467 PPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1862 EAENER--LRRLAEDEAFQRRRLEEQAALHKADIEERLAQLrkasESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKA 1939
Cdd:pfam07111 546 QLEVARqgQQESTEEAASLRQELTQQQEIYGQALQEKVAEV----ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
650 660 670
....*....|....*....|....*....|....*...
gi 254675119 1940 AAGKAELELELGRIRSNAEdtmrsKEQAELEAARQRQL 1977
Cdd:pfam07111 622 ATQEKERNQELRRLQDEAR-----KEEGQRLARRVQEL 654
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1358-1874 |
9.10e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.83 E-value: 9.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1358 AEERERLaeVEAALEKQRQLAEAHAQAKAQaeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqssEAEIQA 1437
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAE-----QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ---TALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1438 KA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRkrqa 1515
Cdd:PRK04863 348 EKieRYQADLEELEERLEEQNEVVEEADE------------------QQEENEARAEAAEEEVDELKSQLADYQQA---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1516 eaelalrVKAEAEAAREKQRALQALDELR-------LQAEEAERRLRQAEAERARQVQVALETAQRsaeVELQSKRASFA 1588
Cdd:PRK04863 406 -------LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1589 EKTAQLERTLQEEHVtvaqlreeaerraqqqaeaerareeaerelerwqlkanealrlRLQAEEVAQQkslaqadaekqk 1668
Cdd:PRK04863 476 EQAYQLVRKIAGEVS-------------------------------------------RSEAWDVARE------------ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1669 eeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1748
Cdd:PRK04863 501 ------------LLRRLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1749 tqkRQELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdAAR 1828
Cdd:PRK04863 567 ---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE-YMQ 634
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 254675119 1829 QRAEAERVLTEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAED 1874
Cdd:PRK04863 635 QLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1544-1883 |
9.46e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 68.23 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1544 RLQAEEAER----RLRQAEAERARQVQV--ALETAQRSAEVELQSKRASFAEKtaqlERTLQEEHvtvaqlreeaerraq 1617
Cdd:pfam17380 287 RQQQEKFEKmeqeRLRQEKEEKAREVERrrKLEEAEKARQAEMDRQAAIYAEQ----ERMAMERE--------------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1618 qqaeaerareeaeRELERWQL----KANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGkAEEQAVRQRELAE 1693
Cdd:pfam17380 348 -------------RELERIRQeerkRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA-ARKVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1694 QELEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQHeataaTQKRQELEAELAKVRAEMEVLLASK 1773
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1774 ARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLTEKLAAISEATRL 1850
Cdd:pfam17380 487 KRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEMEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|...
gi 254675119 1851 KTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1883
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2160-2362 |
1.30e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2239
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2240 EEL----------GKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAL 2309
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2310 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2362
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1327-1544 |
1.33e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 67.21 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1327 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAELEA 1392
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1393 QELQRRMQEEVARRE-EAAVDAQQQKRSIQEELQhlrqsseAEIQAKAQQVEAAERSRMRIEEEirvvrlqLETTERQRg 1471
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANAEREVQRQ-------LEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1472 gAEGELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELR 1544
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1655-1850 |
2.15e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1655 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1734
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1735 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1814
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 254675119 1815 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRL 1850
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1645-2057 |
2.17e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1645 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRA 1722
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1723 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1802
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1803 EEAARLRALAEEAKRQRQLAEED---------------AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENER 1867
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1868 LRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEIMALKVSFEKAAAGKAEl 1946
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1947 elelgRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAE-EEAARQRKVALEEVERLKAKVEEAR- 2024
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEa 460
|
410 420 430
....*....|....*....|....*....|...
gi 254675119 2025 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2057
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4388-4426 |
2.20e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.20e-10
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 4388 FLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTAQKL 4426
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1358-1846 |
2.28e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.67 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1358 AEERERLaeVEAALEKQRQLAEAHAQAkaqaeLEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELqhlrqsseAEIQA 1437
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQL-----AEEQYRLVEMARELEELSARESDLEQDYQAASDHL--------NLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1438 KAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQAEA 1517
Cdd:COG3096 342 ALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1518 ELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqSKRASFAEKTAQLERT 1597
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD--AARRQFEKAYELVCKI 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1598 LQEehVTVAQlreeaerraqqqaeaerareeaereleRWQlKANEALR----LRLQAEEVAQ-QKSLAQAdaekqkeeae 1672
Cdd:COG3096 485 AGE--VERSQ---------------------------AWQ-TARELLRryrsQQALAQRLQQlRAQLAEL---------- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1673 rearrrgkaeEQAVRQRELAEQELEkqrQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1752
Cdd:COG3096 525 ----------EQRLRQQQNAERLLE---EFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1753 QELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1822
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPG 667
|
490 500
....*....|....*....|....
gi 254675119 1823 EEDAARQRAEAERVLTEKLAAISE 1846
Cdd:COG3096 668 GAEDPRLLALAERLGGVLLSEIYD 691
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
36-143 |
3.48e-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: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 36 EQDERDRVqkktFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQN 107
Cdd:cd21300 4 EGEREARV----FTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVEN 72
|
90 100 110
....*....|....*....|....*....|....*.
gi 254675119 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 |
3.55e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 60.28 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 45 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 114
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 254675119 115 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 146
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1719-2273 |
3.68e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1719 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1798
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1799 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE---AENERLRRLA 1872
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1873 EDEAFQRRRLEEQA---ALHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAEL 1946
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1947 ELELGRIRSNAEDTmRSKE---QAELEAARQR------------------QLAAEEEQRRREAEERVQRSLAAEEEAARQ 2005
Cdd:PRK02224 411 EDFLEELREERDEL-REREaelEATLRTARERveeaealleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2006 RKVALEE-VERLKAKVEEARRLRERAEQESArqlqLAQEAAQKRLQAEEKAHAfvvqqreeelqqtlqqeqnmLDRLRSE 2084
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRER--------------------AEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2085 AEAARRAAEEAEEAREQAereaaqsRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA 2164
Cdd:PRK02224 546 AAELEAEAEEKREAAAEA-------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2165 ADAEMEKHKKFAEQTLRqKAQVEQELTTLRlqLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGK 2244
Cdd:PRK02224 619 AELNDERRERLAEKRER-KRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
570 580 590
....*....|....*....|....*....|
gi 254675119 2245 LKARIEA-ENRALILRDkdntqrfLEEEAE 2273
Cdd:PRK02224 696 LRERREAlENRVEALEA-------LYDEAE 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1377-1601 |
4.12e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1377 LAEAHAQAKAQAELEAQelQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEI 1456
Cdd:COG4942 12 ALAAAAQADAAAEAEAE--LEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1457 RVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR-------QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1529
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1530 AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1601
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1461-1902 |
5.08e-10 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 66.15 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1461 LQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAL 1540
Cdd:COG4995 17 LALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1541 DELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQA 1620
Cdd:COG4995 97 ALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1621 EAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR 1700
Cdd:COG4995 177 LALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1701 QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1780
Cdd:COG4995 257 LLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1781 RSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKE 1860
Cdd:COG4995 337 LLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAAL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1861 KEAENERLRRLAEDEAFQR-------RRLEEQAALHK---ADIEERLAQLRK 1902
Cdd:COG4995 417 ALLLALAAYAAARLALLALieyiilpDRLYAFVQLYQlliAPIEAELPGIKR 468
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
524-713 |
6.71e-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: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 524 LRYLQDLLAWVEENQRRIDSAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQLSPATRGAY---RDCLGRLD 600
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 601 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEI 677
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 254675119 678 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 713
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1355-1921 |
6.85e-10 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 65.98 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1355 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQeevarreeAAVDAQQQKRSIQEELQHLRQSSEAE 1434
Cdd:PRK10246 219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ--------ALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1435 I-----QAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRggAEGELQALRARAEEAEAQKRQAQ--EEAERLR----- 1502
Cdd:PRK10246 291 QlrphwERIQEQSAALAHTRQQIEE----VNTRLQSTMALR--ARIRHHAAKQSAELQAQQQSLNTwlAEHDRFRqwnne 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1503 ---------RQVQDESQRKRQAEAELALRVK----------------AEAEAAREKQRAL-QALDELRLQAEEAERRLRQ 1556
Cdd:PRK10246 365 lagwraqfsQQTSDREQLRQWQQQLTHAEQKlnalpaitltltadevAAALAQHAEQRPLrQRLVALHGQIVPQQKRLAQ 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1557 AEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLE--RTLQEEHVTVAQLREEAERRAQQQAEAE--RAREEAERE 1632
Cdd:PRK10246 445 LQVAIQN-----VTQEQTQRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEA 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1633 LERWQLKANEALRLRLQaEEVAQQKS-----LAQADAEKQKEEaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTA 1707
Cdd:PRK10246 520 YQALEPGVNQSRLDALE-KEVKKLGEegaalRGQLDALTKQLQ---------RDESEAQSLRQ-EEQALTQQWQAVCASL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1708 QQRLAAEQELIRLRAETEQGEQQRQLLEEELArLQHEATAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESR 1781
Cdd:PRK10246 589 NITLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1782 STSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLTEKLAAISEATrLKTEAEIALKEK 1861
Cdd:PRK10246 668 ATRQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQ 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1862 EAENERlRRLAE-----DEAFQRRRLEEQAALHKADIEE----RLAQLRKASESELERQKGLVEDTLRQ 1921
Cdd:PRK10246 739 QDVLEA-QRLQKaqaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVTQTAQA 806
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2260-2606 |
6.90e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.53 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2260 DKDNTQRFLEEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaEAELLQQQKE 2339
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------QAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2340 LAQEQARRLQEDKEQmaqqlveetqgfQRTLEAERQRQLEMSAEAERlklrMAEMSRAQARAEEDAQRFRKQAEEIGE-K 2418
Cdd:pfam17380 342 MAMERERELERIRQE------------ERKRELERIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKvK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2419 LHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEakllqlkseEMQTVQQEQILQETQALQKSFL 2498
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE---------EQERQQQVERLRQQEEERKRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2499 SEKDSLLQRERFIEQEKAKLEQLFQDEVAKAkqlreeqqrqqqQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHL 2578
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKELEERKQA------------MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK 544
|
330 340
....*....|....*....|....*...
gi 254675119 2579 EQQRqqqekllaEENQRLRERLQRLEEE 2606
Cdd:pfam17380 545 QQEM--------EERRRIQEQMRKATEE 564
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2161-2467 |
7.83e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2161 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEEL------FS 2234
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-------LTEEISELEKRLEEIEQLLEELNKKIkdlgeeEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2235 VRVQmEELGKLKARIEaenralilrdkdNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRalaekml 2314
Cdd:TIGR02169 290 LRVK-EKIGELEAEIA------------SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2315 KEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAqQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEM 2394
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2395 SRAQARAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQsdhdAERLREAIAELEREKEKLKQE 2467
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEI---KKQEWKLEQLAADLSKYEQE----LYDLKEEYDRVEKELSKLQRE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1650-2053 |
8.22e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1650 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQ 1729
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1730 QRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1809
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1810 ALAEEAKRQRQLAEE----DAARQRAEAERV--LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1883
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLE 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1884 EQAalhkADIEERLAQLRKASESELERQkglveDTLRQRRQVEEEIMALKvsfeKAAAGKAELELELGRIRSNAEDtmrs 1963
Cdd:PRK02224 516 ERR----EDLEELIAERRETIEEKRERA-----EELRERAAELEAEAEEK----REAAAEAEEEAEEAREEVAELN---- 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1964 KEQAELEAARQRqlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLA-- 2041
Cdd:PRK02224 579 SKLAELKERIES--------------LERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfd 644
|
410
....*....|....*.
gi 254675119 2042 ----QEAAQKRLQAEE 2053
Cdd:PRK02224 645 eariEEAREDKERAEE 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1314-1879 |
8.65e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1314 VIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQAELEAQ 1393
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE-KLEKEVKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1394 ELQRRMQEEvarrEEAAVDAQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRG 1471
Cdd:PRK03918 249 SLEGSKRKL----EEKIRELEERIEELKKEIEELEEKVKelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1472 GAEGELQAL---RARAEEAEAQKRQAQEEAERLRRQVQdESQRKRQAEAELAlRVKAEaEAAREKQRALQALDELRLQAE 1548
Cdd:PRK03918 325 GIEERIKELeekEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELE-RLKKR-LTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1549 EAERRLRQAEAERARQVQ---------VALETAQRSAEV----------------------ELQSKRASFAEKTAQLERT 1597
Cdd:PRK03918 402 EIEEEISKITARIGELKKeikelkkaiEELKKAKGKCPVcgrelteehrkelleeytaelkRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1598 LQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR 1677
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1678 RGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA 1757
Cdd:PRK03918 562 EKKLDELEEELAEL-LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1758 ELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAarqraeaeRVL 1837
Cdd:PRK03918 641 RLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAELEELEKRREEIKKTL--------EKL 699
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 254675119 1838 TEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 1879
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1343-1559 |
1.01e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1343 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1422
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ---ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1499
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1500 RLRRQVqdesQRKRQAEAELALRVKAEAEAAREKQRALQALDEL--RLQAEEAERRLRQAEA 1559
Cdd:COG4942 189 ALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2159-2675 |
1.01e-09 |
|
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: 65.46 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2159 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQ 2238
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2239 MEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2318
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2319 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVE-ETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRA 2397
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2398 QARAEEDAQRFRKQAEEIGEKLHRTE-----------------------------LATQEKVT----------------- 2431
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVDegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2432 -LVQTLEIQRQ--QSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEE-----------------------MQTVQQEQ 2485
Cdd:TIGR02168 550 vVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2486 ILQETQALQKS------------------------FLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQ 2541
Cdd:TIGR02168 630 DLDNALELAKKlrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2542 QMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQA 2621
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 2622 ASTKALPNGRDAPDGPSVEAEPEYT---FEGLRQKVPAQQLQEAGILSQEELQRLAQ 2675
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTllnEEAANLRERLESLERRIAATERRLEDLEE 845
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
922-1542 |
1.17e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 922 EEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLV----AEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQ 997
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 998 LEacetrtvhrlrlpldkdparecaQRIAEQqkaqaeveglgkGVARLSAeaekvlalpepspaaptLRSELELTLGKLE 1077
Cdd:COG4913 328 LE-----------------------AQIRGN------------GGDRLEQ-----------------LEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1078 QVRSLSAIYLEKLKTISLVIRSTqgaeevlkthEEQLKEAQA-VPATLQELEATKASLKKLRAQAEAQqpvFNTLRDELR 1156
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPAS----------AEEFAALRAeAAALLEALEEELEALEEALAEAEAA---LRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1157 GAQEVGERLQQRHGERDVEVERWRERVTQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----R 1212
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1213 YYREsadpLSAWLQDAKRRQE-QIQAVPIANCQAAREQLrQEKALLEEIERhgeKVEECQKFAKQYINAIKDYELqlity 1291
Cdd:COG4913 497 HYAA----ALRWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLDF---KPHPFRAWLEAELGRRFDYVC----- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1292 kaqlepVASPAkkpkvqsgsesviqeyvDLRtRYSELTTLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERE 1362
Cdd:COG4913 564 ------VDSPE-----------------ELR-RHPRAITRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1363 RLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmqEEVARREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKAQQV 1442
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQL 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1443 EAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDESQRKRQAEAELAL 1521
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELRENLEER 774
|
650 660
....*....|....*....|.
gi 254675119 1522 RVKAEAEAAREKQRALQALDE 1542
Cdd:COG4913 775 IDALRARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1383-2529 |
1.18e-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: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 65.20 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1383 QAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQhlrqsSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlq 1462
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1463 letterqrggaegeLQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEAELALRVKAEAEAAREKQRALQALDE 1542
Cdd:pfam01576 77 --------------LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAARQKLQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1543 LRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT-AQLERTLQEEHVTVAQLREEAERRAQQQAE 1621
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1622 AERAREEAERELE--RWQL--KANEALRLRLQAEEVAQQKSLAQA---DAEKQKEEAEREARRRGKAEEQAVRQRELAEQ 1694
Cdd:pfam01576 220 LQEQIAELQAQIAelRAQLakKEEELQAALARLEEETAQKNNALKkirELEAQISELQEDLESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1695 ELEKQRQLAEGTaQQRLAAEQELiRLRAETEQGEQQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1771
Cdd:pfam01576 300 ELEALKTELEDT-LDTTAAQQEL-RSKREQEVTELKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1772 SKARAEEESRSTSEK----SKQRLEAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV----------- 1836
Cdd:pfam01576 378 AKQALESENAELQAElrtlQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegkn 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1837 --LTEKLAAIS-----------EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdieeRLAQLRKA 1903
Cdd:pfam01576 457 ikLSKDVSSLEsqlqdtqellqEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKK 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1904 SESELERQKGLVEDtlrqRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMrskeqaeLEAARQRQLAAEEEQ 1983
Cdd:pfam01576 533 LEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEK 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1984 RRREAEErvqrsLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqr 2063
Cdd:pfam01576 602 KQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAE----------- 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2064 eeelqqtlqqeqnmLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQaqaqaqaqaaaeKLRKE 2143
Cdd:pfam01576 666 --------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA------------KLRLE 719
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2144 AEQeaarraqaeqaalkqkQAAdaemekhkkfaeqtlrqKAQVEQELTTLRLQLEEtdhQKSILDEELQRLKAEVTEAAR 2223
Cdd:pfam01576 720 VNM----------------QAL-----------------KAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERK 763
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2224 QRSQveeeLFSVRVQME-ELGKLKARIEAENRAlilRDkdntqrfleeeaEKMKQVAEEAARLSVAAQEAARLRQLAEED 2302
Cdd:pfam01576 764 QRAQ----AVAAKKKLElDLKELEAQIDAANKG---RE------------EAVKQLKKLQAQMKDLQRELEEARASRDEI 824
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2303 LAQQRAlAEKMLKekmqavqeatrlKAEAELLQQQKELA-QEQARR-LQEDKEQMAQQLVEETQGfqRTLEAERQRQLEm 2380
Cdd:pfam01576 825 LAQSKE-SEKKLK------------NLEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE- 888
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2381 saeaERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDHDAERLREAIAELERE 2460
Cdd:pfam01576 889 ----ARIAQLEEELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKELKAKLQEMEGT 960
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2461 -KEKLKQ-----EAKLLQLKSEEMQTVQQEQilQETQALQKSFLSEKDSLLQRErfieqekakleqlfqDEVAKA 2529
Cdd:pfam01576 961 vKSKFKSsiaalEAKIAQLEEQLEQESRERQ--AANKLVRRTEKKLKEVLLQVE---------------DERRHA 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1156-1581 |
1.38e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.97 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1156 RGAQEvgERLQQRHGERDVEVERWR---------ERVTQLLERW-------------QAVLAQTDVRQRELEqlgRQLRY 1213
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELE---RELAQ 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1214 YRESADPLSAWLQDAKRRQEQIQA-VPIANCQAArEQLRQekaLLEEIERHGEKVEECQKFAKQYINAIkdyelqlityk 1292
Cdd:COG3096 855 HRAQEQQLRQQLDQLKEQLQLLNKlLPQANLLAD-ETLAD---RLEELREELDAAQEAQAFIQQHGKAL----------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1293 AQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltSQYIKFISETLRRM------EEEERLAEQQRAEE--RERL 1364
Cdd:COG3096 920 AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRL----KQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEklRARL 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1365 AEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHLrqsseaEIQAKAQQVEA 1444
Cdd:COG3096 994 EQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL------GVQADAEAEER 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1445 AERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEA 1517
Cdd:COG3096 1057 ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERRLHRR 1136
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1518 ELalrvkaeaeaarekqrALQALDELRLQAEEAERRLRQAEAERArQVQVALETAQ--RSAEVELQ 1581
Cdd:COG3096 1137 EL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEdpRRPERKVQ 1185
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4310-4347 |
1.48e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 55.95 E-value: 1.48e-09
10 20 30
....*....|....*....|....*....|....*...
gi 254675119 4310 QRLLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMV 4347
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1353-1564 |
1.54e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1353 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMqeevARREEAAVDAQQQKRSIQEEL-------Q 1425
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELaelekeiA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1426 HLRQSSEAEIQAKAQQVEAAERSRMR-----------IEEEIRVVRLQLETTERQRggaeGELQALRARAEEAEAQKRQA 1494
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARR----EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1495 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1564
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1369-1601 |
1.65e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 64.20 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1369 AALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLR--QSSEAEIQAKAQQVEAA 1445
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEArAAKDKDAVAAALARVKakKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1446 ERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1525
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1526 EAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1601
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1167-1975 |
1.85e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.59 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1167 QRHGERDVEVER-WRERVTQLLERwQAVLAQTdvrQRELEQLGRQLRYYRESADPLSAWL---QDAKRRQEQIQAVpIAN 1242
Cdd:COG3096 281 RELSERALELRReLFGARRQLAEE-QYRLVEM---ARELEELSARESDLEQDYQAASDHLnlvQTALRQQEKIERY-QED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1243 CQAAREQLRQEKALLEEIErhgEKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpkVQSGSESVIQEYVDLR 1322
Cdd:COG3096 356 LEELTERLEEQEEVVEEAA---EQLAEAEARLEAAEEEVDSLKSQLADYQQALD----------VQQTRAIQYQQAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1323 TRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAA---LEKQRQLAEAHAQA--KAQAELEAQELQR 1397
Cdd:COG3096 423 EKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAArrqFEKAYELVCKIAGEveRSQAWQTARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1398 RMQEEVARreeaAVDAQQQKRSIQEELQHLRQSSEAEIQAK------AQQVEAA---ERSRMRIEEEIRVVRLQLETTER 1468
Cdd:COG3096 503 RYRSQQAL----AQRLQQLRAQLAELEQRLRQQQNAERLLEefcqriGQQLDAAeelEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1469 QRGGAEGELQALRARAEEAEAQK---RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRL 1545
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1546 QAeeaeRRLRQAE-AERARQVQ----------------VALETA---------QRSAEVELQSKRAsfAEKTAQLERTLQ 1599
Cdd:COG3096 659 QI----ERLSQPGgAEDPRLLAlaerlggvllseiyddVTLEDApyfsalygpARHAIVVPDLSAV--KEQLAGLEDCPE 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1600 E------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANE--ALRLRLQAEEVAQQksLAQADAE 1665
Cdd:COG3096 733 DlyliegdpdsfdDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGR---AAREkrLEELRAERDELAEQ--YAKASFD 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1666 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegtaqQRLAAEQELIRLRAETEQGEQQRQLLEEE---LARLQ 1742
Cdd:COG3096 808 VQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQ-------RRSELERELAQHRAQEQQLRQQLDQLKEQlqlLNKLL 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1743 HEATA-----ATQKRQELEAELAKvraemevllaskarAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEEA 1815
Cdd:COG3096 881 PQANLladetLADRLEELREELDA--------------AQEAQAFIQQHGKAlaQLEPLVAVLQSDPEQFEQLQADYLQA 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1816 KRQRQlaeedAARQRAEAERVLTEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRRLEEQAALHKAD 1892
Cdd:COG3096 947 KEQQR-----RLKQQIFALSEVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQ 1016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1893 IEERLAQLRKASESELErqkglvedtlrQRRQVEEEIMALKVSF-----EKAAAGKAELELELGRIRS--NAEDTMRSKE 1965
Cdd:COG3096 1017 YNQVLASLKSSRDAKQQ-----------TLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSrrSQLEKQLTRC 1085
|
890
....*....|
gi 254675119 1966 QAELEAARQR 1975
Cdd:COG3096 1086 EAEMDSLQKR 1095
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1645-2053 |
1.93e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1645 RLRLQAEEVAQQ-KSLAQADAEKQKEEAEREARRRGKAE------EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL 1717
Cdd:COG4913 239 RAHEALEDAREQiELLEPIRELAERYAAARERLAELEYLraalrlWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1718 IRLRAETEQGEQQRQLLE-EELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1796
Cdd:COG4913 319 DALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1797 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV---LTEKLAAISEATRLKTEA------EIALKEKEAE--- 1864
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAElpfvgeLIEVRPEEERwrg 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1865 -------NERLRRLAEDEAFQ-------RRRLEEQAALHKADIEERLAQLRKAS-------------------ESELERQ 1911
Cdd:COG4913 479 aiervlgGFALTLLVPPEHYAaalrwvnRLHLRGRLVYERVRTGLPDPERPRLDpdslagkldfkphpfrawlEAELGRR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1912 KGLV----EDTLRQ-RRQVEEEIM--ALKVSFEK---------------AAAGKAELELELGRIRSNAEDTmrskeQAEL 1969
Cdd:COG4913 559 FDYVcvdsPEELRRhPRAITRAGQvkGNGTRHEKddrrrirsryvlgfdNRAKLAALEAELAELEEELAEA-----EERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1970 EAAR------QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALE----EVERLKAKVEEARRLRERAEQESARQLQ 2039
Cdd:COG4913 634 EALEaeldalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKG 713
|
490
....*....|....
gi 254675119 2040 LAQEAAQKRLQAEE 2053
Cdd:COG4913 714 EIGRLEKELEQAEE 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1436-1668 |
2.21e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1436 QAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1515
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1516 EAELALRVKAEAEAAREKQR-ALQALDELRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1593
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1594 LERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQKSLAQADAEKQK 1668
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1380-1835 |
2.53e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 63.88 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1380 AHAQAKAQAELEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVV 1459
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1460 RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA 1539
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1540 LDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQ 1619
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1620 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1699
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1700 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1779
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1780 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1835
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAA 927
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1334-2051 |
2.90e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1334 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDA 1413
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1414 QQQKRSIQEELQHLRQ---SSEAEIQA-KAQQVEAAERSRMRIEEEIRVVRLQLetteRQRGGA--------EGELQALR 1481
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1482 AR----AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEAELAlRVKAEAEAAREKQRALQAldelrlQAEEAERRLRQ 1556
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1557 AEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTL------------------QEEHVTVAQLREEAERRAQQ 1618
Cdd:pfam15921 311 QNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLvlanseltearterdqfsQESGNLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1619 QAEAERAREEAERELERWQLKANEALRLRLQAE----EVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAE 1693
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1694 QELEKQ--RQLAEGTAQQRL---AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAE---LAKVRAE 1765
Cdd:pfam15921 470 LESTKEmlRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1766 MEVL---LASKARAEEESRSTSEK-----------------SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1825
Cdd:pfam15921 550 CEALklqMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1826 AARQRAEAERVLTEKLAAISEatrLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLrKASE 1905
Cdd:pfam15921 630 LELEKVKLVNAGSERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL-KSAQ 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1906 SELERQKglveDTLRQRRQVEEEIMALKVSFEKA-AAGKAELELELGRIRSNAED-TMRSKEQAELEAARQRQLAAEEEQ 1983
Cdd:pfam15921 706 SELEQTR----NTLKSMEGSDGHAMKVAMGMQKQiTAKRGQIDALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTV 781
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1984 RRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVE--EARRLRERAEQESARqLQLAQEAAQKRLQA 2051
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaECQDIIQRQEQESVR-LKLQHTLDVKELQG 850
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1372-1593 |
2.91e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.52 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1372 EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEaavdaQQQKRSIQEELQhlRQSSEAEIQAKAQQVEAAERsrmr 1451
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-----LEKERLAAQEQK--KQAEEAAKQAALKQKQAEEA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1452 ieeeirvvrlQLETTERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEAELALRVKAEAEAA 1530
Cdd:PRK09510 138 ----------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1531 REKQRALQAldelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1593
Cdd:PRK09510 203 AEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1351-1932 |
3.48e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 63.72 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1351 RLAEQQRAEERERLAEVEAalekqRQLAEAHAQAKAQAELEA---QELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL 1427
Cdd:COG3899 674 RALEARGPEPLEERLFELA-----HHLNRAGERDRAARLLLRaarRALARGAYAEALRYLERALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1428 RQSSEAEIQAkaQQVEAAERSRmrieEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1507
Cdd:COG3899 749 LELAEALYLA--GRFEEAEALL----ERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAER 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1508 ESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAS 1586
Cdd:COG3899 823 LGDRRLEARALFNLgFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAA 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1587 FAEKTAQLERTLQEEH---VTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAD 1663
Cdd:COG3899 903 ALAAAAAAAALAAAELarlAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAA 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1664 AEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1743
Cdd:COG3899 983 AAAAAA-----------AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAA 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1744 EATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1823
Cdd:COG3899 1052 AAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARA 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1824 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA 1903
Cdd:COG3899 1132 AAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLA 1211
|
570 580
....*....|....*....|....*....
gi 254675119 1904 SESELERQKGLVEDTLRQRRQVEEEIMAL 1932
Cdd:COG3899 1212 LALLALEAAALLLLLLLAALALAAALLAL 1240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1653-1887 |
3.95e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1653 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1732
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1733 LLEEELARLQHEAtaatqKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRAL 1811
Cdd:COG4942 94 ELRAELEAQKEEL-----AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1812 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1887
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
164-266 |
4.09e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.39 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 164 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 242
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 254675119 243 PEDVDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2176-2610 |
5.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2176 AEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELfSVRVQMEELGKLKARIEAENRA 2255
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2256 LI-LRDKDNTQRFLEEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2334
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2335 QQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRKQAE 2413
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2414 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqQEQILQETQAL 2493
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---IAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2494 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQElmASMEEARRRQREAEEGVRRKQE 2573
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE--EELEELEEELEELREELAELEA 460
|
410 420 430
....*....|....*....|....*....|....*..
gi 254675119 2574 ELQHLEQQRQQQEKLLAEEnqRLRERLQRLEEEHRAA 2610
Cdd:COG4717 461 ELEQLEEDGELAELLQELE--ELKAELRELAEEWAAL 495
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1104-1294 |
6.35e-09 |
|
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: 59.38 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1104 EEVLKTHEEQLKEAQaVPATLQELEATKASLKKLRAQAEAQQPVFNTLrdelrgaQEVGERLQQRHGERDVEVerwRERV 1183
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1184 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLSAWLQDAKRRQEQIQavPIANCQAAREQLRQEKALLEEIERH 1263
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 254675119 1264 GEKVEECQKFAKQYINAIKDYELQLITYKAQ 1294
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
159-261 |
6.37e-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: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 159 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 237
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 254675119 238 TRLLDPEDVDVPQPDEKSIITYVS 261
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1049-1595 |
7.22e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1049 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEaqaVPATLQELE 1128
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1129 ATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLqqrhgerdveverwrERVTQLLERWQAVLAQTDVRQRELEQLG 1208
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---------------SRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1209 RQLRYYRESADPLSAW---LQDAKRRQEQIqavpiancqaarEQLRQEKALL--EEIERHGEKVEECQKFAKQYINAIKD 1283
Cdd:PRK03918 345 KKLKELEKRLEELEERhelYEEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1284 YELQLITYKAQLEPVASPAKKPKVQS---GSESVIQEYVDLRTRYSElttltsqYIKFISETLRRMEEEERlaeqqraEE 1360
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1361 RERLAEVEAALEKQRQLAEAHAQAKAQAELEaQELQRRMQEEVARREEAAvdaqqqkRSIQEELQHLrqssEAEIQAKAQ 1440
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEY-------EKLKEKLIKL----KGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1441 QVEAAERsrmrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1520
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1521 lRVKAEAEAAREK-QRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1595
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1344-1577 |
8.24e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.70 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKrsIQEE 1423
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER--IQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1424 LQHLRQSSEAEIQAKAQQVEAAERSRMRI---------EEEIRVVRLQLETTERQRggAEGELQALRARAEEAEAQKRQA 1494
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1495 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQR 1574
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
...
gi 254675119 1575 SAE 1577
Cdd:pfam13868 272 EDE 274
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1344-1551 |
8.37e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERErlaEVEAALEKQRQLaeahaqakAQAELEAQElQRRMQEEVARREeaavdAQQQKrsiQEE 1423
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQ---KQAAEQERLKQL--------EKERLAAQE-QKKQAEEAAKQA-----ALKQK---QAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1424 LQHLRQSSEAEIQAKAQQVEAAERSRmRIEEEIRvVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrr 1503
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK--- 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254675119 1504 qVQDESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELRLQAEEAE 1551
Cdd:PRK09510 211 -AAAEAKKKAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
168-263 |
8.45e-09 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.93 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 168 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 223
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 254675119 224 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 263
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1337-1579 |
9.17e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.70 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1337 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQ 1416
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1417 KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEGELQALRARAEEaEAQKRQAQE 1496
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREEAEKKARQ-RQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1497 EAERLRRQVQDESQRKRQAEAELALRVKAEAE------AAREKQRALQALDELRLQAEEAER-RLRQAEAERARQVQVAL 1569
Cdd:pfam13868 243 EQIELKERRLAEEAEREEEEFERMLRKQAEDEeieqeeAEKRRMKRLEHRRELEKQIEEREEqRAAEREEELEEGERLRE 322
|
250
....*....|
gi 254675119 1570 ETAQRSAEVE 1579
Cdd:pfam13868 323 EEAERRERIE 332
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1835-2573 |
1.02e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1835 RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaalhKADIEERLAQLRKASESELERQKGL 1914
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1915 VEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAED-TMRSKEQAELEAARQRQLAAEEEQRRREAEERVQ 1993
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1994 RSLAAEEEAARQRKVALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFVVqqre 2064
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETR---- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2065 eelqqtlqqeqnmlDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAaeklrkea 2144
Cdd:TIGR02169 385 --------------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE-------- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2145 eqeaarraqaeqaalkqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAE---VTEA 2221
Cdd:TIGR02169 443 -----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2222 ARQRSQVEEELFS----VRVQMEELGKLKAR------IEAENR--ALILRDKDNTQR---FLEEEA---------EKMKQ 2277
Cdd:TIGR02169 506 VRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2278 VAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAEA 2331
Cdd:TIGR02169 586 ERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2332 ELLQQQKElaqEQARRLQEDKEQMAQQLveetQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2411
Cdd:TIGR02169 666 ILFSRSEP---AELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2412 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELER-----------------EKEKLKQEAKLLQLK 2474
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqaelsklEEEVSRIEARLREIE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2475 SEEMQTVQQEQILQ-ETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQELMAS 2553
Cdd:TIGR02169 819 QKLNRLTLEKEYLEkEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
810 820
....*....|....*....|
gi 254675119 2554 MEEARRRQREAEEGVRRKQE 2573
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRK 917
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1163-1470 |
1.07e-08 |
|
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: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1163 ERLQQRHGERDVEVERWR-----ERVTQL-LERWQAVLAQTD----VRQRELEQLGrqlryyresadplsawLQDAKRRQ 1232
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRkleeaEKARQAeMDRQAAIYAEQErmamERERELERIR----------------QEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1233 EQIQAVPIAncqAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVaspakKPKVQSGSE 1312
Cdd:pfam17380 363 ERIRQEEIA---MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI-----RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1313 SVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEA 1392
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEE 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1393 QELQRRMQEEVARREEAAvdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQR 1470
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKATeERSRLEAMEREREMMRQIVESEKAR 588
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1422-1796 |
1.32e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.06 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1422 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1501
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1502 RRQVQDESQRKRQAEAELALRVKA-EAEAAREKQRALQA---LDELRLQAEEAERRLRQAEAERaRQVQVALETAQ---R 1574
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLEReteLERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1575 SAEVELQSKRASFAEKTAQLERtLQEehvTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1654
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-LQD---TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1655 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1734
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 1735 EEELARlqhEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1796
Cdd:pfam07888 345 EVELGR---EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2166-2627 |
1.47e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2166 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSVRVQMEELGKL 2245
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2246 KARIEAENRALILRDKDNTqrfLEEEAEKMKQVAEEAARLSVAAQEAARLR----------QLAEEDLAQQRALAEKMLK 2315
Cdd:TIGR00618 276 EAVLEETQERINRARKAAP---LAAHIKAVTQIEQQAQRIHTELQSKMRSRakllmkraahVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2316 EKMQAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMS 2395
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK------ELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2396 RAQARAEEDAQRFRKQAEEigekLHRTELATQEKVTLVQTLEIQrQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKS 2475
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2476 EEMQTVQqEQILQETQALQKSFLSEKDS-----LLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQEL 2550
Cdd:TIGR00618 501 EEPCPLC-GSCIHPNPARQDIDNPGPLTrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 2551 MASMEEArrrqreaeEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKAL 2627
Cdd:TIGR00618 580 NRSKEDI--------PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1358-1578 |
1.52e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 60.66 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1358 AEERERLAEVEAALEKQRQLAEAHAQ-AKAQAELEAQELQRRMQEEVARREEAAvdAQQQKRSIQEELQhlRQSSEAEIQ 1436
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIAE--AEAELAKKKAEER--REAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1437 AKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggaegelqalraRAEEAEAQKRQAQEEAERlrrqvqdesqrkrqae 1516
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREI-----------------ELQEKEAEREEAELEADV---------------- 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1517 aelalRVKAEAEAAREKQRALQALDELRLQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1578
Cdd:COG2268 311 -----RKPAEAEKQAAEAEAEAEAEAIRAKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
159-266 |
1.94e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.10 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 159 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 237
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 254675119 238 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
35-149 |
2.04e-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: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 35 DEQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQI 110
Cdd:cd21222 8 DEAPEKLAEVKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKL 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 254675119 111 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21222 83 ALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1353-2142 |
2.10e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.96 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1353 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ-HLRQSS 1431
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTeQLEQAK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1432 EAEIQ-AKAQQVEAAERSRMriEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ 1510
Cdd:pfam01576 370 RNKANlEKAKQALESENAEL--QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1511 RKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEVELQSKRASFA 1588
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1589 EktaqLERTLQEEHVTVAQLREEaerraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKslaqadAEKQK 1668
Cdd:pfam01576 528 D----MKKKLEEDAGTLEALEEG----------------------KKRLQRELEALTQQLEEKAAAYDK------LEKTK 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1669 EEAEREARRRGKAEEQavrQRELAEQELEKQRQLAEGTAQQRLAAEQELI-RLRAETEQGEQQRQLLEeelarLQHEATA 1747
Cdd:pfam01576 576 NRLQQELDDLLVDLDH---QRQLVSNLEKKQKKFDQMLAEEKAISARYAEeRDRAEAEAREKETRALS-----LARALEE 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1748 ATQKRQELEAELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAGRFRELAEEA---------ARLR------ALA 1812
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELedelqatedAKLRlevnmqALK 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1813 EEAKRQRQLAEEDA-------ARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1885
Cdd:pfam01576 727 AQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1886 AALHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEIMALKVSFEKAAAGKAELELEL- 1950
Cdd:pfam01576 807 MKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERDELADEIASGASGKSALQDEKr 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1951 ---GRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREaeervqrsLAAEEEAARQRKVALEEVER----LKAKVEEA 2023
Cdd:pfam01576 886 rleARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTE--------LAAERSTSQKSESARQQLERqnkeLKAKLQEM 957
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2024 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQae 2103
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL-- 1035
|
810 820 830
....*....|....*....|....*....|....*....
gi 254675119 2104 reaaqsRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRK 2142
Cdd:pfam01576 1036 ------KRQLEEAEEEAS----------RANAARRKLQR 1058
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1778-2061 |
2.39e-08 |
|
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: 60.52 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1778 EESRSTSEKSKQ----RLEAEagRFRELAEEAARlralaeEAKRQRQLAEEDAARQrAEAERvlteKLAAISEATRLKTE 1853
Cdd:pfam17380 279 QHQKAVSERQQQekfeKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1854 AE-----IALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQ----LRKASESELERQKGLVEDT--LRQR 1922
Cdd:pfam17380 346 RErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeleaARKVKILEEERQRKIQQQKveMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1923 RQVEEEIMALKV---------SFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQ 1993
Cdd:pfam17380 426 RAEQEEARQREVrrleeerarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1994 RSLAAEEeaaRQRKVALEEVE-RLKAKVEEARR------LRERAEQESARQLQLAQEAA---QKRLQAEEKAHAFVVQ 2061
Cdd:pfam17380 506 QAMIEEE---RKRKLLEKEMEeRQKAIYEEERRreaeeeRRKQQEMEERRRIQEQMRKAteeRSRLEAMEREREMMRQ 580
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1361-1830 |
2.44e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1361 RERLAEVEAALEKQRQLAEAHAQAKAQAEleaQELQRRMQEEVARREEAAVDaqqqkrSIQEELQHLRQSSEAEIqakAQ 1440
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAA---AELRGPDQLAWLARLDAEHD------NLRAALRWALAHGDAEL---AL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1441 QVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1520
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1521 LRvkAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1600
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1601 EHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGK 1680
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1681 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1760
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1761 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1830
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
37-148 |
2.80e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 54.82 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 37 QDERDrvqKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIA 111
Cdd:cd21299 1 ETSRE---ERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQV 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 112 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 148
Cdd:cd21299 71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1150-1942 |
3.03e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 60.35 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1150 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQREleQLGRqlryYRESADPLSAw 1224
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTE- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1225 lqdakRRQEQIQAVPIANCQAAREQLRQEKALlEEIERHG-------EKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1296
Cdd:COG3096 362 -----RLEEQEEVVEEAAEQLAEAEARLEAAE-EEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1297 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEER-ERLAEVEAALEK- 1373
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELlRRYRSQQALAQRl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1374 ---QRQLAEAHAQAKAQAELE--AQELQRRmqeevarreeaavdaQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERS 1448
Cdd:COG3096 515 qqlRAQLAELEQRLRQQQNAErlLEEFCQR---------------IGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1449 RMrieeeirvvrlqleTTERQRGGAEGELQALRARAEEAeaqkRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1528
Cdd:COG3096 580 RS--------------ELRQQLEQLRARIKELAARAPAW----LAAQDALERLREQSGEALADSQEVTAAMQQLLERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1529 AAREKQRALQALDELRLQAeeaeRRLRQAE-AERARQVQ----------------VALETA---------QRSAEVELQS 1582
Cdd:COG3096 642 ATVERDELAARKQALESQI----ERLSQPGgAEDPRLLAlaerlggvllseiyddVTLEDApyfsalygpARHAIVVPDL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1583 KRAsfAEKTAQLERTLQE------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANE--ALRLRL 1648
Cdd:COG3096 718 SAV--KEQLAGLEDCPEDlyliegdpdsfdDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGR---AAREkrLEELRA 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1649 QAEEVAQQksLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGE 1728
Cdd:COG3096 793 ERDELAEQ--YAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALR-------QRRSELERELAQHRAQEQQLR 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1729 QQRQLLEEE---LARLQHEATA-----ATQKRQELEAELAKVR-AEMEVLLASKARAE-EESRSTSEKSKQRLEAEAGRF 1798
Cdd:COG3096 864 QQLDQLKEQlqlLNKLLPQANLladetLADRLEELREELDAAQeAQAFIQQHGKALAQlEPLVAVLQSDPEQFEQLQADY 943
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1799 RELAEEAARLR----ALAEEAKRQRQLAEEDAARQRAEAeRVLTEKL-AAISEATRLKTEAEIALKEKEAE-NERLRRLA 1872
Cdd:COG3096 944 LQAKEQQRRLKqqifALSEVVQRRPHFSYEDAVGLLGEN-SDLNEKLrARLEQAEEARREAREQLRQAQAQySQYNQVLA 1022
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1873 E-DEAFQRRR--------------------LEEQAALHKADIEERLAQLRkASESELERQKGLVE---DTLRQR-RQVEE 1927
Cdd:COG3096 1023 SlKSSRDAKQqtlqeleqeleelgvqadaeAEERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSLQKRlRKAER 1101
|
890
....*....|....*
gi 254675119 1928 EIMALKVSFEKAAAG 1942
Cdd:COG3096 1102 DYKQEREQVVQAKAG 1116
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1498-1954 |
3.36e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.03 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1498 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1577
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1578 VELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1657
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1658 SLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1737
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1738 LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1817
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1818 QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERL 1897
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1898 AQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIR 1954
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1690-2604 |
3.46e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.19 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1690 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeME 1767
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1768 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervLTEKLAAISEA 1847
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1848 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaalhKADIEErlaqlrkasesELERQKGLVEDTLRQRRQVEE 1927
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ----RRDLGE-----------ELEALKTELEDTLDTTAAQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1928 EimalkvsfekaaagKAELELELGRIRSNAEDTMRSKEqAELEAARQRQLaaeeeqrrreaeervqrslAAEEEAARQrk 2007
Cdd:pfam01576 321 L--------------RSKREQEVTELKKALEEETRSHE-AQLQEMRQKHT-------------------QALEELTEQ-- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2008 vaLEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLDRLRSEA 2085
Cdd:pfam01576 365 --LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLqeLQARLSESERQRAELAEKLSKLQSEL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2086 EAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAA 2165
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2166 DAEMEKHKKFAEQTL-------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA----RQRSQVEeelfs 2234
Cdd:pfam01576 523 QAQLSDMKKKLEEDAgtlealeEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldHQRQLVS----- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2235 vrvQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKmkqvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2314
Cdd:pfam01576 598 ---NLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK----ETRALSLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2315 --------------KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQL-- 2378
Cdd:pfam01576 671 sskddvgknvheleRSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2379 ---EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIA 2455
Cdd:pfam01576 750 qvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQ 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2456 ELEREKEKLKQEAKLLQLKSE----EMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEvakakq 2531
Cdd:pfam01576 828 SKESEKKLKNLEAELLQLQEDlaasERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEE------ 901
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2532 lreeqqrqqqqmeqekqelMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAE---ENQRLRERLQRLE 2604
Cdd:pfam01576 902 -------------------QSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQlerQNKELKAKLQEME 958
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2276-2496 |
3.50e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2276 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2351
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2352 KEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2431
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2432 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKS 2496
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1341-1563 |
3.54e-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: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQkr 1418
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1419 siqEELQHlrqssEAEIQAKAQQVEAAERSRmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEE- 1497
Cdd:TIGR02794 146 ---EEAAK-----QAEEEAKAKAAAEAKKKA-----------------------EEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1498 ---AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERAR 1563
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1685-2057 |
4.04e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.97 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1685 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEATAATQK----RQ 1753
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1754 ELEAELAKVRAEMEVLLA---SKARAEEESRSTSEKSK----------QRLEAE---AGRFR------ELAEEAARLRAL 1811
Cdd:COG3096 355 DLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEVDslksqladyqQALDVQqtrAIQYQqavqalEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1812 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERlrrlaeDEAFQR-RRLEEQAALHK 1890
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER------SQAWQTaRELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1891 AdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1970
Cdd:COG3096 509 A-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1971 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQ 2050
Cdd:COG3096 580 RSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
....*..
gi 254675119 2051 AEEKAHA 2057
Cdd:COG3096 660 IERLSQP 666
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1019-1603 |
5.41e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1019 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLE-------- 1088
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMAlrqqleql 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1089 -----KLKTISLVIRSTQGAEEVLKTH-EEQLKEAQAVPATLQELeatkasLKKLRAQAEAqqpvfntlRDELRGAQEV- 1161
Cdd:PRK04863 592 qariqRLAARAPAWLAAQDALARLREQsGEEFEDSQDVTEYMQQL------LERERELTVE--------RDELAARKQAl 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1162 ---GERLQQRHGERDveverwrERVTQLLERWQAVLAQTDVRQRELEQLGrqlrYYresadplSAWLQDAKrrqeqiQAV 1238
Cdd:PRK04863 658 deeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YF-------SALYGPAR------HAI 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1239 PIANCQAAREQLRQEKALLEEI-------ERHGEKVEECQKFAKQYINAIKDYELQLITYKAqlEPVASPAKKPK----V 1307
Cdd:PRK04863 714 VVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqL 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1308 QSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ 1387
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1388 AELEAQELQRRM------------------QEEVARREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE- 1446
Cdd:PRK04863 870 AKEGLSALNRLLprlnlladetladrveeiREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQq 949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1447 ---RSRMRIE--EEIRVVRLQLETTERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEAEL 1519
Cdd:PRK04863 950 tqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1520 alrvKAEAEAAREK-QRALQALDELRLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAE 1589
Cdd:PRK04863 1026 ----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLE 1101
|
650
....*....|....
gi 254675119 1590 KTAQLERTLQEEHV 1603
Cdd:PRK04863 1102 RDYHEMREQVVNAK 1115
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1711-2606 |
5.88e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.42 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1711 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1790
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1791 LEAEAGRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLTE-KLAAISEATRLKTEAEIAL-KEKEAENERL 1868
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1869 RRLA------EDEAFQRRRLEEQAALHKADIEERLAQLRK-------------ASESELERQ----KGLVEDTLRQRRQV 1925
Cdd:pfam01576 162 SEFTsnlaeeEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqelekakrkleGESTDLQEQiaelQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1926 EEEIMALKVSFEKAAAGKAELE---LELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 2002
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2003 ARQRKvalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLR 2082
Cdd:pfam01576 322 RSKRE---QEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2083 SEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeqeaarraqaeqaalKQK 2162
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS---------------KDV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2163 QAADAEMEKHKKFAEQTLRQK-------AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQrsqVEEELFSV 2235
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDAGTL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2236 RvQMEElGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQvaeEAARLSVAAQeaaRLRQLAEEDLAQQRALAEKMLK 2315
Cdd:pfam01576 541 E-ALEE-GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ---ELDDLLVDLD---HQRQLVSNLEKKQKKFDQMLAE 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2316 EKMQAVQEA-TRLKAEAELLQQQKElAQEQARRLQEdkeqmAQQLVEETQGFQRTLEAERQrqlEMSAEAERLKLRMAEM 2394
Cdd:pfam01576 613 EKAISARYAeERDRAEAEAREKETR-ALSLARALEE-----ALEAKEELERTNKQLRAEME---DLVSSKDDVGKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2395 SRAQARAEEDAQRFRKQAEEIGEKLHRTELAtqeKVTLVQTLEIQRQQSDHD---------------AERLREAIAELER 2459
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQFERDlqardeqgeekrrqlVKQVRELEAELED 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2460 EKE--------KLKQEAKLLQLKSE-EMQTVQQEQILQETQALQKSFlseKDslLQRErfIEQEKAKLEQLFqdevAKAK 2530
Cdd:pfam01576 761 ERKqraqavaaKKKLELDLKELEAQiDAANKGREEAVKQLKKLQAQM---KD--LQRE--LEEARASRDEIL----AQSK 829
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2531 QLREEQQRQQQQMEQEKQELMASmeEARRRQREAEegvrrkQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEE 2606
Cdd:pfam01576 830 ESEKKLKNLEAELLQLQEDLAAS--ERARRQAQQE------RDELADEIASGASGKSALQDEKRRLEARIAQLEEE 897
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1344-1605 |
6.21e-08 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 58.12 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQ 1421
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1422 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrlqletterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1501
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1502 RRQVQDESQR-KRQA-EAELALRVKAEAEAARE--KQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1577
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 254675119 1578 VELQSKRASFAEKTAQLERTLQEEHVTV 1605
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1722-2284 |
6.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1722 AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAGRFR 1799
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1800 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-LTEKLAAIS-EATRLKTEA---EIALKEKEAENERLRRLAE 1873
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeYLDELREIEkRLSRLEEEIngiEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1874 DEAFQRRRLEEQAALHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEImalkvsfEKAAAGKAELE 1947
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEI-------SKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1948 LELGRIRSNAEdtmrskeqaELEAARQ------RQLAAEEEQRRREAEERVQRSLAAE----EEAARQRKVALEEVERLK 2017
Cdd:PRK03918 419 KEIKELKKAIE---------ELKKAKGkcpvcgRELTEEHRKELLEEYTAELKRIEKElkeiEEKERKLRKELRELEKVL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2018 AKVEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAFvvqqreeelqqtlQQEQNMLDRLRSEAEAARRAAEEAEE 2097
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEY-------------EKLKEKLIKLKGEIKSLKKELEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2098 AREQAEREAAQSRKQVEE-AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFA 2176
Cdd:PRK03918 554 LKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2177 EQTLRQKA--QVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARI 2249
Cdd:PRK03918 634 ELAETEKRleELRKELEELEKKYSEEEYEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
570 580 590
....*....|....*....|....*....|....*
gi 254675119 2250 EAENRALilrdkdntqRFLEEEAEKMKQVAEEAAR 2284
Cdd:PRK03918 714 EKLEKAL---------ERVEELREKVKKYKALLKE 739
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1772-2055 |
6.54e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 59.19 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1772 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAarqRAEAERVLTEKLAAISEATRL 1850
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDA---VAAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1851 KTEAEIALKEKEAEnERLRRLAEDEAFQRRRLEEQAALHKADIEERL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1928
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1929 ImalkvsfEKAAAGKAELelelgrirsnAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV 2008
Cdd:PRK05035 586 I-------ARAKAKKAAQ----------QAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 254675119 2009 ALeEVERLKAKVEEARRLRERAEQESARQLQlAQEAAQKRLQAEEKA 2055
Cdd:PRK05035 649 AA-AIARAKARKAAQQQANAEPEEAEDPKKA-AVAAAIARAKAKKAA 693
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1555-2473 |
6.62e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.21 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1555 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREeaerelE 1634
Cdd:TIGR00618 56 RRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSET------E 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1635 RWQLKAnealrLRLQAEEVAQQKSLAQADAEKqkeeaereaRRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAE 1714
Cdd:TIGR00618 130 EVIHDL-----LKLDYKTFTRVVLLPQGEFAQ---------FLKAKSKEKKELLMNL--FPLDQYTQLALMEFAKKKSLH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1715 QELIrlrAETEQGEQQRQLLEEELARLqheataaTQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK--QRLE 1792
Cdd:TIGR00618 194 GKAE---LLTLRSQLLTLCTPCMPDTY-------HERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqQLLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1793 AEAGRFRELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1872
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1873 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQR-RQVEEEIMALKVSFEKAAAGKAELELELG 1951
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1952 RIrsNAEDTMRSKEQAELEAAR-QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERA 2030
Cdd:TIGR00618 411 TI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2031 EQESARQLQLAQEaaQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAaqsr 2110
Cdd:TIGR00618 489 KAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK---- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2111 kqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKeaEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQEL 2190
Cdd:TIGR00618 563 ---EQMQEIQQSFSILTQCDNRSKEDIPNLQN--ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2191 TTlRLQLEETdhqkSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEE 2270
Cdd:TIGR00618 638 SQ-ELALKLT----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2271 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAELLQQQKELAQE---QAR 2346
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNeEVTAALQTGAELSHLAAEiqfFNR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2347 RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAraeedaqRFRKQAEEIGEKLHRTELAT 2426
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG-------EITHQLLKYEECSKQLAQLT 865
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2427 QEKVTLVQTLE----IQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQL 2473
Cdd:TIGR00618 866 QEQAKIIQLSDklngINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1746-1899 |
8.11e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.35 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1746 TAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRAlaEEAKRQRQLAEED 1825
Cdd:COG2268 212 TEIAIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1826 AARQR------AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAALHKADIEERLAQ 1899
Cdd:COG2268 286 AEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG-KRALAEAWNKLGDAAILLMLIE 364
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1068-1516 |
9.17e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1068 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEatkaslkKLRAQAEAQQPV 1147
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-------ALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1148 FNTLRDELRGAQEVGERLQqrhgERDVEVERWRERVTQLLERWQAVLAQTDVR-QRELEQLGRQLRYYRESADPLSAWLQ 1226
Cdd:COG4717 148 LEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1227 DAKRRQEQIQAVPIAncQAAREQLRQEK----------ALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLE 1296
Cdd:COG4717 224 ELEEELEQLENELEA--AALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1297 PVASPAKKPKVQSGSESviQEYVDLRTRYSELTTLTSQYIkfisETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ 1376
Cdd:COG4717 302 KEAEELQALPALEELEE--EELEELLAALGLPPDLSPEEL----LELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1377 LAEAHAQAKAQAELEAQELQRRmQEEVARREEAAVDAQQQKRSIQEELQHLRQSS-EAEIQAKAQQVEAAERSRMRIEEE 1455
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREE 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1456 IRVVRLQLETTERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAE 1516
Cdd:COG4717 455 LAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4041-4077 |
9.28e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 9.28e-08
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 4041 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4077
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
967-1603 |
9.76e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 967 YQQLLQSLEQGEQeesrcqrcISELKDirLQLEACETR-TVHRLRLPLDKDPARECAQRIAEQQKAQAEVEGLGKGVARL 1045
Cdd:COG3096 415 YQQAVQALEKARA--------LCGLPD--LTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1046 SAEAEKVLALPEpspAAPTLR--SELELTLGKLEQVRSlsaiyleKLKTISLVIRSTQGAEEVL----KTHEEQLKEAQA 1119
Cdd:COG3096 485 AGEVERSQAWQT---ARELLRryRSQQALAQRLQQLRA-------QLAELEQRLRQQQNAERLLeefcQRIGQQLDAAEE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1120 VPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRG--------------AQEVGERLQQRHGERDVEVERWRERVTQ 1185
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRArikelaarapawlaAQDALERLREQSGEALADSQEVTAAMQQ 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1186 LLERWQAVLAQTD---VRQRELEQLGRQLRYYRESADP-------------LS-----AWLQDA----KRRQEQIQAVPI 1240
Cdd:COG3096 635 LLEREREATVERDelaARKQALESQIERLSQPGGAEDPrllalaerlggvlLSeiyddVTLEDApyfsALYGPARHAIVV 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1241 ANCQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKKPKVQS 1309
Cdd:COG3096 715 PDLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRLEELRA 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1310 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAE 1389
Cdd:COG3096 793 ERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQL 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1390 LEAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEE 1455
Cdd:COG3096 870 KEQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQ 949
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1456 IRVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkRQAEAELA 1520
Cdd:COG3096 950 QRRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ--VLASLKSS 1027
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1521 LRVKAE--AEAARE-KQRALQALDELRLQAEEaERRLRQAEAERARQVQVALETAQRSAEVELQS--KRASFAEKTAQLE 1595
Cdd:COG3096 1028 RDAKQQtlQELEQElEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQE 1106
|
....*...
gi 254675119 1596 RTLQEEHV 1603
Cdd:COG3096 1107 REQVVQAK 1114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1232-1803 |
1.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1232 QEQIQAVPIANCQAAREQL-----RQEKALLEEIERHGEKVEECQKFAKQYINAIKdyelQLITYKAQLEPVASPAKKPK 1306
Cdd:COG4717 40 LAFIRAMLLERLEKEADELfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1307 VQSGSESVIQEYVDLRTRYSELTtltsqyikfisETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKA 1386
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALE-----------AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1387 QAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEE--EIRVV 1459
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqlENELEAAALEERLKEARLLLLIAAAllALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1460 RLQLETTERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQR 1535
Cdd:COG4717 265 GGSLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1536 ALQALDELRLQAEEAERRLRQAEAERARqvQVALETAQRSAEVELQSKRASFAEKTAQLERtlqeehvtvaqlreeaerr 1615
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEI--AALLAEAGVEDEEELRAALEQAEEYQELKEE------------------- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1616 aqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearrrgKAEEQAVRQRELAEQE 1695
Cdd:COG4717 404 -------------------------LEELEEQLEELLGELEELLEALDEEELEE----------ELEELEEELEELEEEL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1696 LEKQRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAE-LAKVRAEMEVLLASK 1773
Cdd:COG4717 449 EELREELAELEAElEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREErLPPVLERASEYFSRL 528
|
570 580 590
....*....|....*....|....*....|
gi 254675119 1774 ARAEEESRSTSEKSKQRLEAEAGRFRELAE 1803
Cdd:COG4717 529 TDGRYRLIRIDEDLSLKVDTEDGRTRPVEE 558
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1975 |
1.12e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1528 EAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaq 1607
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1608 lreeaerraqqqaeaerareeaereLERW-QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRgKAEEQAV 1686
Cdd:COG4717 145 -------------------------PERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-EELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1687 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEM 1766
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1767 EVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISE 1846
Cdd:COG4717 279 LFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1847 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALH--KADIEERLAQLRKASESELERQKGLVEDTLRQR-R 1923
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQelKEELEELEEQLEELLGELEELLEALDEEELEEElE 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1924 QVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQR 1975
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1649-1832 |
1.24e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1649 QAEEVAQQKslaQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1724
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1725 EQGEQQRQLLEEELARLQHEATAatqkRQELEAElAKVRAEMEvllaSKARAEEESRSTSEK-SKQRLEAEAGRFRELAE 1803
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEA----KKKAEAE-AAAKAAAE----AKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*....
gi 254675119 1804 EAArlRALAEEAKRQRQLAEEDAARQRAE 1832
Cdd:PRK09510 232 AEA--KAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
46-145 |
1.32e-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: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 46 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQ 119
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARG 75
|
90 100
....*....|....*....|....*.
gi 254675119 120 VKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21286 76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1713-1913 |
1.44e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1713 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1792
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1793 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA 1854
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1855 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKG 1913
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1649-1835 |
1.49e-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: 56.78 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1649 QAEEVAQQKSlAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1728
Cdd:TIGR02794 51 QANRIQQQKK-PAAKKEQERQK---------KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1729 QQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EA 1805
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEA 200
|
170 180 190
....*....|....*....|....*....|
gi 254675119 1806 ARLRALAEEAKRQRQLAeedAARQRAEAER 1835
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1754-2605 |
2.19e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1754 ELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRleaeaGRFRELAEEAARLRALAEEaKRQRQLAEEDAARQRAEA 1833
Cdd:TIGR02169 167 EFDRKKEKALEELEEV---EENIERLDLIIDEKRQQL-----ERLRREREKAERYQALLKE-KREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1834 ERVLTEKlaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHkadIEERLAQLrkasESELERQKG 1913
Cdd:TIGR02169 238 QKEAIER--QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR---VKEKIGEL----EAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1914 LVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNaedtmRSKEQAELEAARQRqlaaeeEQRRREAEERVQ 1993
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR-----RDKLTEEYAELKEE------LEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1994 RSLAAEEEAARQRKVALEEVERLKAKVE-EARRLRERAEQESARQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTL 2071
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKrELDRLQEELQRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2072 QQEQNMLDRLRSEAEAARRAAEEAEEAREqaereaaQSRKQVEEAERLKQSAEEQAQAQAqaqaaaeklrkeaeqeaarr 2151
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELS-------KLQRELAEAEAQARASEERVRGGR-------------------- 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2152 aqaeqaalkqkqAADAEMEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-EVT 2219
Cdd:TIGR02169 511 ------------AVEEVLKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgRAT 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2220 EAARQRSQVEEELFSVRVQMEELGKLKARIEAENR-----ALILRDKDNTQRfLEEEAEKMKQV---------------- 2278
Cdd:TIGR02169 577 FLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTLVVED-IEAARRLMGKYrmvtlegelfeksgam 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2279 ----AEEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2345
Cdd:TIGR02169 656 tggsRAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2346 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELA 2425
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEAR 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2426 TQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMqtvqqEQILQETQALQKSfLSEKDSLL 2505
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-----EEELEELEAALRD-LESRLGDL 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2506 QRERfiEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEqekqelmASMEEARRRQREAEEGVRRKQEElqhleQQRQQQ 2585
Cdd:TIGR02169 888 KKER--DELEAQLREL-ERKIEELEAQIEKKRKRLSELK-------AKLEALEEELSEIEDPKGEDEEI-----PEEELS 952
|
890 900
....*....|....*....|
gi 254675119 2586 EKLLAEENQRLRERLQRLEE 2605
Cdd:TIGR02169 953 LEDVQAELQRVEEEIRALEP 972
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2209-2477 |
2.22e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2209 EELQRLKAEVTEAARQRSQVE------EELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEA 2282
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2283 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2362
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2363 TQGFQRTLEAERQRQLEMSAEAERLklrmaemSRAQARAEEDAQRFRKQAEEIgeklhRTELAtqekvtlvqtlEIQRQQ 2442
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEAL-------EEALAEAEAALRDLRRELREL-----EAEIA-----------SLERRK 435
|
250 260 270
....*....|....*....|....*....|....*...
gi 254675119 2443 SDHDAE--RLREAIAE-LEREKEKLKQEAKLLQLKSEE 2477
Cdd:COG4913 436 SNIPARllALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2013-2688 |
2.26e-07 |
|
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: 57.76 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2013 VERLKAKVEEARRLRERAEQESARQLQLA----QEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQnmLDRLRSEAEAA 2088
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEELEELTAELQELEEK--LEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2089 RRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE 2168
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2169 MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEE--LGKLK 2246
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaeLKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2247 ARIEAENRAlilrdkdntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEkMLKEKMQAVQEATR 2326
Cdd:TIGR02168 440 AELEELEEE------------LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2327 lkAEAELLQQQKELAQEQARrlqedkeqmAQQLVEETQGFQRTLEA---ERQRQLEMS------------AEAERLKLRM 2391
Cdd:TIGR02168 507 --GVKALLKNQSGLSGILGV---------LSELISVDEGYEAAIEAalgGRLQAVVVEnlnaakkaiaflKQNELGRVTF 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2392 AEMSRAQARAEEDAQRFRKQAEE--IGEKLHRTELATQEKVTL---------VQTLEI---QRQQSDHDA---------- 2447
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPKLRKALsyllggvlvVDDLDNaleLAKKLRPGYrivtldgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2448 ------------------------ERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDS 2503
Cdd:TIGR02168 656 rpggvitggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2504 LLQRERFIEQEKAKLEQL-------------FQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRR 2570
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLskelteleaeieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2571 KQEELQHLEQQRQQQEKLLAEENQRLRERLQRLE--EEHRAALAHS-----EIATTQAASTKALPNGRDAPDGPSVEAEP 2643
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEelSEDIESLAAEieeleELIEELESELEALLNERASLEEALALLRS 894
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 254675119 2644 EYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTVAELTQRED 2688
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1375-1587 |
2.38e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1375 RQLAEAHAQAKAQAELEAQELQRRMQEEVARR--EEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAER 1447
Cdd:COG3206 147 PELAAAVANALAEAYLEQNLELRREEARKALEflEEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1448 SRMRIEEEIRVVRLQLETTERQRGGAEGE---------LQALRARAEEAEAQKRQAQE-------EAERLRRQVQDESQR 1511
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1512 KRQAEAELALRVKAEAEAAREKQRALQA-LDELRLQAE---EAERRLR--QAEAERARQVQVALETAQRSAEVELQSKRA 1585
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAqLAQLEARLAelpELEAELRrlEREVEVARELYESLLQRLEEARLAEALTVG 386
|
..
gi 254675119 1586 SF 1587
Cdd:COG3206 387 NV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1354-1757 |
2.67e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1354 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRM------------------QEEVARREEAAVDAQQ 1415
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLprlnlladetladrveeiREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1416 QKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE----RSRMRIE--EEIRVVRLQLETTERQR-GGAEGELQ-ALRARAE 1485
Cdd:PRK04863 916 HGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1486 EAEAQKRQAQEEAerlrRQVQDESQRKRQAEAELalrvKAEAEAAREK-QRALQALDELRLQA-EEAERRLRQAEAE--- 1560
Cdd:PRK04863 996 QAEQERTRAREQL----RQAQAQLAQYNQVLASL----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElha 1067
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1561 ---RARQVQVALETAQRSAEVELQS--KRASFAEKTAQLERTLQEEHVT--VAQLREEAERRAQQQAEAERAREEAEREL 1633
Cdd:PRK04863 1068 rlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKDNGVERRLHRRELAYLSADEL 1147
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1634 ERWQLKANEALRLrlqaeevaqqkslAQADAEKqkEEAEREARRRGKAEEQAVRQRELAEQEL-EKQRQLAEGTAQQRLA 1712
Cdd:PRK04863 1148 RSMSDKALGALRL-------------AVADNEH--LRDVLRLSEDPKRPERKVQFYIAVYQHLrERIRQDIIRTDDPVEA 1212
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1713 AEQ---ELIRLRAETEQGEQQRQLLEEELA-----RLQHEATAATQKRQELEA 1757
Cdd:PRK04863 1213 IEQmeiELSRLTEELTSREQKLAISSESVAniirkTIQREQNRIRMLNQGLQN 1265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1336-1576 |
2.70e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1336 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQ 1415
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1416 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAE----EAEAQK 1491
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1492 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALET 1571
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*
gi 254675119 1572 AQRSA 1576
Cdd:COG3883 258 AAGSA 262
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1829-2219 |
2.82e-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: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1829 QRAEAERVLTEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdiEERLAQLRkasESEL 1908
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1909 ERQKglVEDTLRQRRQVEEEIMALKVSFEKaaagkaELE-LELGRIRSNaedtmrSKEQAELEAARQRQLAaeeeqrrre 1987
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1988 aeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQReee 2066
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK--- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2067 lqqtlqqeqnmldRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeq 2146
Cdd:pfam17380 474 -------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA-- 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2147 eaarraqaeqaalKQKQAADAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT 2219
Cdd:pfam17380 539 -------------EEERRKQQEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1076-1522 |
2.96e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1076 LEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEaqaVPATLQE----LEATKASLKKLRAQAEAQQPVFNTL 1151
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD---LTASLQEkeraIEATNAEITKLRSRVDLKLQELQHL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1152 RDE---LRGAQEVGERLQQRHGERDVEVERWR---ERVTQLLERW----QAVLAQTDVRQRELEQLGRQLRYYRESADPL 1221
Cdd:pfam15921 537 KNEgdhLRNVQTECEALKLQMAEKDKVIEILRqqiENMTQLVGQHgrtaGAMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1222 SAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQkfaKQYINAIKDYELQLITYKAQLEPVASP 1301
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1302 AKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAH 1381
Cdd:pfam15921 694 TNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA-------------MKVAMGMQKQITAKR 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1382 AQAKAqaeleaqelqrrMQEEVARREEAAVDAQQQKRSIQEELQHLRQsseaeiqakaqqveaaersrmrieeeirvvrl 1461
Cdd:pfam15921 741 GQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ-------------------------------- 776
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1462 QLETTERQRGGAEGELQALRA---RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR 1522
Cdd:pfam15921 777 ELSTVATEKNKMAGELEVLRSqerRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1433-1570 |
3.23e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.82 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1433 AEIQAKAQQVEAAersrmrieeeIRVVRLQLETTERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE--SQ 1510
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGavSQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1511 RKRQaEAELALRV-KAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERArQVQVALE 1570
Cdd:COG1566 148 QELD-EARAALDAaQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1374-1502 |
3.93e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.44 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1374 QRQLAEAHAQ-AKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKaQQVEAAERSRMRI 1452
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ-QELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675119 1453 EEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1502
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1104-1763 |
4.45e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.72 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1104 EEVLKTHEEQLKE-----AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVER 1178
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1179 WRERVTQ-------LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKR-RQEQIQAVpiANCQAAREQL 1250
Cdd:pfam01576 417 LQARLSEserqraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQElLQEETRQK--LNLSTRLRQL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1251 RQEKALLEEieRHGEKVEECQKFAKQyinaIKDYELQLITYKAQLEPVASPAK-----KPKVQSGSESVIQEY------- 1318
Cdd:pfam01576 495 EDERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaay 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1319 ------------------VDLRTRYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlAEVEAALEKQRQLAEA 1380
Cdd:pfam01576 569 dklektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR-AEAEAREKETRALSLA 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1381 HAQAKAQAELEAQELQRRMQE--------------------EVARR--EEAAVDAQQQKRSIQEEL-------------- 1424
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRaemedlvsskddvgknvhelERSKRalEQQVEEMKTQLEELEDELqatedaklrlevnm 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1425 QHLRQSSEAEIQAKAqqvEAAERSRMRIEEEIRVVRLQLETTERQRGGA-------EGELQALRARAEEAEAQKRQAQEE 1497
Cdd:pfam01576 723 QALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQ 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1498 AERLRRQVQDesqrkRQAEAELALRVKAEAEA-AREKQRALQALDELRLQAEE----AERRLRQAEAERAR-QVQVALET 1571
Cdd:pfam01576 800 LKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGA 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1572 AQRSAeveLQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELE-----RWQL-KANEALR 1645
Cdd:pfam01576 875 SGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQksesaRQQLeRQNKELK 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1646 LRLQAEEVA---QQKSLAQA------DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1716
Cdd:pfam01576 952 AKLQEMEGTvksKFKSSIAAleakiaQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSR 1031
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 254675119 1717 LIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVR 1763
Cdd:pfam01576 1032 MKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1425-1713 |
4.53e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1425 QHLRQSsEAEIQAKAQQVEAAERSRMRIEEeiRVVRLQLETTERQrggaegelqalrARAEEAEAQKRQAQEEA-----E 1499
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAARE------------ARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1500 RLRRQVQDESQRKRQAEAELALRVKAEAEA-AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEV 1578
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAReARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1579 ELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAeaerareeaerelerwqlkANEALRLRLQAEEVAQQKS 1658
Cdd:PRK05035 574 EVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------------------AVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 1659 LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1713
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2318-2463 |
4.67e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 56.56 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2318 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLVEEtQGFQRTLEAERQRQLEMSAEAERLKL 2389
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2390 RMAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2463
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 ... |
2276-2492 |
5.39e-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: 55.24 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2276 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2355
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2356 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2435
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 2436 LEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2492
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1679-1887 |
5.44e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 55.73 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1679 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheataATQKRQEL 1755
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1756 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEeakRQRQLAEEDAARQRAEAER 1835
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQE---LQRKKQQEEAERAEAEKQR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1836 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1887
Cdd:pfam15709 454 QKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1156-1581 |
5.60e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1156 RGAQEvgERLQQRHGERDVEVERW--RERVTQLLERWQ-----------AVLAQTDVRQrELEQLGRQLRY-YRESADpl 1221
Cdd:PRK04863 781 RAARE--KRIEQLRAEREELAERYatLSFDVQKLQRLHqafsrfigshlAVAFEADPEA-ELRQLNRRRVElERALAD-- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1222 sawlQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEiERHGEKVEECQ---KFAKQYINAIKDYELQLitykAQLEPV 1298
Cdd:PRK04863 856 ----HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD-ETLADRVEEIReqlDEAEEAKRFVQQHGNAL----AQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1299 AS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAeereRLAEVEAALE 1372
Cdd:PRK04863 927 VSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1373 KQRqlaEAHAQAKAQAeleAQELQRRMQEEVARREeaavdAQQQKRSIQEELQHL--RQSSEAEIQAKAQqveaaersRM 1450
Cdd:PRK04863 1003 RAR---EQLRQAQAQL---AQYNQVLASLKSSYDA-----KRQMLQELKQELQDLgvPADSGAEERARAR--------RD 1063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1451 RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEAELALRV 1523
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRLVKDNGVERRLHRRELAYLS 1143
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1524 KAEAEAAREKqrALQALdelrlqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1581
Cdd:PRK04863 1144 ADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1494-2029 |
6.47e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1494 AQEEAERLRRQVQDESQRKR---QAEAELALRVKaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALE 1570
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIK---EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1571 TAQRSAEVE-LQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQ 1649
Cdd:PRK03918 240 IEELEKELEsLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1650 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLR 1721
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1722 AETEQGEQQRQLLEEELAR--LQHEATAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR----------- 1781
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytael 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1782 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLTEKLAAISEA 1847
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1848 TRLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA---------SESELERQKGLV 1915
Cdd:PRK03918 542 KSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKEL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1916 EDTLRQRRQVEEEIMALKVSFEKAaagKAELElELGRIRSnaEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRS 1995
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
570 580 590
....*....|....*....|....*....|....
gi 254675119 1996 LAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2029
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3722-3757 |
6.91e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 6.91e-07
10 20 30
....*....|....*....|....*....|....*.
gi 254675119 3722 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3757
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1348-1543 |
7.43e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1348 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR-REEAAVDAQQQKRSIQEElqh 1426
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKKAAA--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1427 lRQSSEAEIQAKAQQVEAAErsrmrieeeirvvrlqletterQRGGAEGELQALRARAEEAEAQKRQAQEEAErlrrqvq 1506
Cdd:PRK09510 182 -EAKKKAEAEAAAKAAAEAK----------------------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA------- 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 254675119 1507 desqRKRQAEAELALRVKAEAEAAREKQRAlqALDEL 1543
Cdd:PRK09510 232 ----AEAKAAAEKAAAAKAAEKAAAAKAAA--EVDDL 262
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1692-1907 |
8.41e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1692 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1771
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1772 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK 1840
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1841 LAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE 1907
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4144-4172 |
9.29e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.29e-07
10 20
....*....|....*....|....*....
gi 254675119 4144 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4172
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1322-1441 |
9.36e-07 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 53.45 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1322 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELeaqelqR 1397
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 254675119 1398 RMQEEVARREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKAQQ 1441
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKE 177
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2169-2472 |
9.87e-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: 55.41 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2169 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKAR 2248
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2249 IEAENRAL------ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2320
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2321 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaerqrqlemsaeaeRLKLRMAEMSRAQAR 2400
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 2401 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2472
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1343-1823 |
1.03e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.13 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1343 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1422
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ELQHLRQSSE------AEIQAKAQQVEAAERSRMRIEEEIR--VVRLQLET-------TERQRGGAEGELQALRARAEEA 1487
Cdd:pfam05557 133 ELEELQERLDllkakaSEAEQLRQNLEKQQSSLAEAEQRIKelEFEIQSQEqdseivkNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1488 EAQKRQAQEEAERLRRQVQDESQRKRQAEaelalrvKAEAEAAR---EKQRALQALDELRLQAEEAERRLRQAEAERARQ 1564
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREE-------KYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1565 VQValetaqRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQLK 1639
Cdd:pfam05557 286 EQL------QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkERDGYR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1640 AN-EALRLRLQAEEVAQQKSLAQADAE----KQKEEAEREARRRGKAEEQAVRQRELA---EQELEKQRQlAEGTAQQRL 1711
Cdd:pfam05557 360 AIlESYDKELTMSNYSPQLLERIEEAEdmtqKMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQALRQ-QESLADPSY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1712 AAE------QELIRLRAETEQGEQQRQLLEEELAR--------------LQHEATAATQKRQELEAELAKVRAEMEVLla 1771
Cdd:pfam05557 439 SKEevdslrRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERL-- 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1772 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEeaarLRALAEEA-KRQRQLAE 1823
Cdd:pfam05557 517 -KRLLKKLEDDLEQVLRLPETTSTMNFKEVLD----LRKELESAeLKNQRLKE 564
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1349-1726 |
1.05e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1349 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarREEAAVDAQQQKRSIQEELQHLR 1428
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE----LKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1429 QSSEAEIQAKAQQVEAAERSRMRIEE-EIRVVRLQLETTERqrggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1507
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLER-----ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1508 ESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKRA 1585
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1586 SFAEKTAQLERTLQEEH---VTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrLRLQAEEVAQQKSLAQA 1662
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRI-EKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1663 DAEKQKEEAEREARRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1726
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRREL--QELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2166-2627 |
1.22e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2166 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2234
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2235 VRvqmeeLGKLKARIeaeNRALILRDKDNTQRFLEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRaLAEKM 2313
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2314 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLE 2379
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2380 MSAEAERLKLRMAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLR 2451
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2452 EAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQ---ETQALQKSFLSEKDSLLQR-----ERFIEQEKAKLEQLfQ 2523
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartEKQAYWQVVEGALDAQLALlkaaiAARRSGAKAELKAL-E 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2524 DEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRL 2603
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARL 833
|
490 500
....*....|....*....|....
gi 254675119 2604 EEEHRAALAhsEIATTQAASTKAL 2627
Cdd:pfam12128 834 IADTKLRRA--KLEMERKASEKQQ 855
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1332-1498 |
1.31e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1332 TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ--ELQRRMQEEVARREE- 1408
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARYTPn 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1409 --AAVDAQQQ----KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRV---VRLQLETTERQRGGAEGELQA 1479
Cdd:COG3206 290 hpDVIALRAQiaalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYES 369
|
170
....*....|....*....
gi 254675119 1480 LRARAEEAEAQKRQAQEEA 1498
Cdd:COG3206 370 LLQRLEEARLAEALTVGNV 388
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1382-1596 |
1.32e-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: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1382 AQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAqqveaAERSRMRIEEEIRvvrl 1461
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1462 qletterqrggaegelQALRARAEEAEAQKRQAQEEAERlrrQVQDESQRKRQAEAelalRVKAEAEAAREKQRALQALD 1541
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1542 ELRLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1596
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2105-2694 |
1.39e-06 |
|
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: 54.98 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2105 EAAQSRKQVEEAERLKQ-SAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEqtlRQK 2183
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYlDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE---EEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2184 AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDN 2263
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2264 TQR-------------FLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL---AQQRALAEKMLKEKMQAVQEATRL 2327
Cdd:pfam02463 369 EQLeeellakkkleseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeeKKEELEILEEEEESIELKQGKLTE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2328 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAeAERLKLRMAEMSRAQARAEED--- 2404
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE---QLELLLSRQKLEERSQ-KESKARSGLKVLLALIKDGVGgri 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2405 ---AQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQqsdhdaeRLREAIAELEREKEKLKQEAKLLQLKSEEMQTV 2481
Cdd:pfam02463 525 isaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ-------KLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2482 QQEQILQETQALQKSFLSEKDSLLQRErFIEQEKAKLEQLFQdEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQ 2561
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKV-VEGILKDTELTKLK-ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2562 REAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgPSVEA 2641
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL---------KQKID 746
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2642 EPEYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTvaELTQREDVYRYLK 2694
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLK 797
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1495-2031 |
1.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1495 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQR 1574
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1575 SAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAerraqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVA 1654
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELE----------------------------AELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1655 QQKSLAQAdaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1734
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1735 EEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1814
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1815 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALH--KAD 1892
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQelKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1893 IEERLAQLRKASESELERQKGLVEDTLRQR-RQVEEEImalkvsfekaaagkAELELELGRIRsnaedtmrsKEQAELEA 1971
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEEL--------------EELEEELEELR---------EELAELEA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1972 ARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEAR--RLRERAE 2031
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERlpPVLERAS 522
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1104-1820 |
2.00e-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: 54.37 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1104 EEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAqqpvfntLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1182
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1183 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplSAWLQDAKRRQEQIQAvpiaNCQAAREQLRQEKALLEEIER 1262
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRK----QLSKTQEELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1263 H-GEKV------EECQKFAKQYINAIKDYELQLITYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTSQY 1335
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1336 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEAQeLQRRMQEEVARREEAAVDAq 1414
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDKAAEVEVERMSA- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1415 qqkRSIQEELQhlrQSSEAEIQAKaQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1494
Cdd:pfam07111 376 ---KGLQMELS---RAQEARRRQQ-QQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1495 QEEAER--LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldELRLQA----EEAERRLRQAEAERARQVQVA 1568
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA--ELQLSAhliqQEVGRAREQGEAERQQLSEVA 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1569 LETAQrsaevELQSKRASFAEKTAQLERTLQEEhvtvaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRl 1648
Cdd:pfam07111 527 QQLEQ-----ELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1649 qAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGE 1728
Cdd:pfam07111 566 -QELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK-ERNQELRRLQDEARKEE 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1729 QQR-----QLLEEE----LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRLEAE 1794
Cdd:pfam07111 644 GQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSLTVL 723
|
730 740
....*....|....*....|....*.
gi 254675119 1795 AGRFRELAEEAARLRALAEEAKRQRQ 1820
Cdd:pfam07111 724 LDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
39-151 |
2.05e-06 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 50.00 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 39 ERDRVQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIA 111
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675119 112 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2221-2469 |
2.12e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2221 AARQRSQVEEELFSVRVQMEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAE 2300
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2301 EDLAQQRALaekmLKEKMQAVQEATRLKAEAELLQQQKELaqeQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEM 2380
Cdd:COG4942 97 AELEAQKEE----LAELLRALYRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2381 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAeeigeklhrTELATQEKVTLVQTLEIQRQqsdhdAERLREAIAELERE 2460
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLL---------ARLEKELAELAAELAELQQE-----AEELEALIARLEAE 235
|
....*....
gi 254675119 2461 KEKLKQEAK 2469
Cdd:COG4942 236 AAAAAERTP 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1680-2053 |
2.20e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.72 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1759
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1760 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1837
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1838 TEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRRLEEQAAlhkadieerlaqlrKASESELERQKGLVED 1917
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKS--------------QNGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1918 TLRQRRQVEEEimalkvsfEKAAAGKAELELELGRIR-SNAEdtmrsKEQAELEAARQRQLAAEEEQRRREAEERVQRSL 1996
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1997 AAEEEaaRQRKValEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2053
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3927-3964 |
2.33e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.33e-06
10 20 30
....*....|....*....|....*....|....*...
gi 254675119 3927 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3964
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1739-2469 |
2.51e-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: 53.96 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1739 ARLQHEATAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1815
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1816 KRQRQLAEEDAAR---QRAEAERVLT------EKLAAISEATRLKTE---AEIALKEKEaENERLRRLAEDEAFQRRRLE 1883
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMdlnnniEKMILAFEELRVQAEnarLEMHFKLKE-DHEKIQHLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1884 EQAALHKADIEERlaqlrkasESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRS 1963
Cdd:pfam05483 240 KQVSLLLIQITEK--------ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1964 keqaeleaarQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR---KVALEEVERLKAKVEEARRLRERAEQESARQLQL 2040
Cdd:pfam05483 312 ----------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2041 AQEAAQKRLQAEEKAHAFVVQQREEelqqtlqqeqnmLDRLRSEAEAARRAAEEaeeareqaereaaqsRKQVEE-AERL 2119
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVE------------LEELKKILAEDEKLLDE---------------KKQFEKiAEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2120 KQSAEEQAQAQAQAQAAAEKLRkeaeQEAARRAQAEQAALKQKQAADAEMEKHK-KFAEQT------LRQKAQVEQELTT 2192
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLE----IQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTahcdklLLENKELTQEASD 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2193 LRLQLEetDHQKSILDEELQ--RLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkarieaENRALILRDKDNTQRFLEE 2270
Cdd:pfam05483 511 MTLELK--KHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFIQKGD-------EVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2271 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ---EATRLKAEAELLQQQKELAQEQARR 2347
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQK 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2348 LQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSaeaERLKLRMAEMSraqARAEEDAQRFRKQAEEIGEKLHRTELATQ 2427
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAEMV---ALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 254675119 2428 EKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAK 2469
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1364-1776 |
2.54e-06 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 54.09 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1364 LAEVEAALEKQRQLAEAHAQAKaqaelEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1432
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1433 --------AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1504
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1505 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1584
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1585 ASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADA 1664
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1665 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1744
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 254675119 1745 ATAATQKRQELEAELAKVRAEMEVLLASKARA 1776
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1103-1751 |
2.55e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1103 AEEVLKTHEEQLKEAQAVPATL-QELEATKASLKKLRAQAEA---QQPVFNTLRDE----LRGAQEVGERLQQR-HGERD 1173
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPAwlaAQDALERLREQsgeaLADSQEVTAAMQQLlERERE 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1174 VEVER-----WRERVTQLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLSAWLQDAKrrqeqiQAVPIA 1241
Cdd:COG3096 642 ATVERdelaaRKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPAR------HAIVVP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1242 NCQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKKPKVQSG 1310
Cdd:COG3096 716 DLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRLEELRAE 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1311 SESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEL 1390
Cdd:COG3096 794 RDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLK 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1391 EAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEEI 1456
Cdd:COG3096 871 EQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQ 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1457 RVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkrQAEAELAL 1521
Cdd:COG3096 951 RRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQV--LASLKSSR 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1522 RVKAE--AEAARE-KQRALQALDELRLQAEEaERRLRQAEAERARQVQVALETAQRSAEVELQS--KRASFAEKTAQLER 1596
Cdd:COG3096 1029 DAKQQtlQELEQElEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQER 1107
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1597 TLQEEHVtvaqlreeaerraqqqaeaerareeaerelERW----QLKANEALRLRLQAEEVAQQkslaqaDAEKQKEEAe 1672
Cdd:COG3096 1108 EQVVQAK------------------------------AGWcavlRLARDNDVERRLHRRELAYL------SADELRSMS- 1150
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1673 rearrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQR---------LAAEQEL-IRLRAETEQGEQQRQLLEE---ELA 1739
Cdd:COG3096 1151 ----------DKALGALRLAVADNEHLRDALRLSEDPRrperkvqfyIAVYQHLrERIRQDIIRTDDPVEAIEQmeiELA 1220
|
730
....*....|..
gi 254675119 1740 RLQHEATAATQK 1751
Cdd:COG3096 1221 RLTEELTSREQK 1232
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1484-1600 |
2.61e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1484 AEEAEAQKRQAQEEAErLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALdELRLQAEEAErrlrqaeaeraR 1563
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARAEAEA-AYEIAEANAE-----------R 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675119 1564 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1600
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1306-1520 |
2.66e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1306 KVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA 1382
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1383 QAKAQAELEAQELQRRMQEEVARREEAAVDAQQQkrsiQEELQHLRQSSEAEIQAKAQQVEAAERSRmrieeeirvVRLQ 1462
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEER---------AALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1463 LETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1520
Cdd:COG4942 192 ALKAERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1341-1574 |
2.77e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 53.12 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARReEAAVDAQQQKRSI 1420
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQ-EAEQRKQCQEQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1421 QEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA------EAQKRQA 1494
Cdd:pfam15558 130 KEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQRS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1495 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ----RALQALDELRL-QAEEAERRLRQAEAERARQVQVAL 1569
Cdd:pfam15558 210 QENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNLER 289
|
....*
gi 254675119 1570 ETAQR 1574
Cdd:pfam15558 290 EKNHH 294
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1347-1512 |
2.82e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1347 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1426
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1427 LRQSSEAEIQAKAQQVEA-AERSRMRIEEEI----RVVRLQLETTERQRGGAEGELQALRARAEEAEAQK------RQAQ 1495
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 254675119 1496 EEAERLRRQVQDESQRK 1512
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1577-2411 |
3.03e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1577 EVELQSKRASFAEKTAQ-LERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELerwQLKANEALRLRLQAEEVAQ 1655
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEhIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDL---QTKLQEMQMERDAMADIRR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1656 QKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQqrlaaeqELIRLRAETEQGEQQRQLLE 1735
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKKIYEH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1736 EELARLQHEA--TAATQKRQELEAELA-------KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEA 1805
Cdd:pfam15921 208 DSMSTMHFRSlgSAISKILRELDTEISylkgrifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1806 ARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1885
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1886 AALHKADIEERLAQL-----RKASESELERQkglvedtlrQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEdT 1960
Cdd:pfam15921 368 FSQESGNLDDQLQKLladlhKREKELSLEKE---------QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLK-A 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1961 MRSKEQAELEaarqRQLAaeeeqrrreaeervqrslaaeeeAARQRKVALEEVERLKAKVEEARR-LRERAEQESARQLQ 2039
Cdd:pfam15921 438 MKSECQGQME----RQMA-----------------------AIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMT 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2040 LAQE---------AAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREaaq 2108
Cdd:pfam15921 491 LESSertvsdltaSLQEKERAIEATNAEItkLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL--- 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2109 sRKQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalkqkqaadaeMEKHKKFAEQTLRQKAQVEQ 2188
Cdd:pfam15921 568 -RQQIENMTQL-------------------------------------------------VGQHGRTAGAMQVEKAQLEK 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2189 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----EEELFSVRVQMEELGKLKARIE---------AENRA 2255
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrnelnslSEDYE 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2256 LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK----MLKEKMQAVQEA- 2324
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKmqlksaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRgqidALQSKIQFLEEAm 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2325 TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLvEETQGFQRTLeaeRQRQLEMSAEAERLKLRMAEMSRAQARAEED 2404
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
....*..
gi 254675119 2405 AQRFRKQ 2411
Cdd:pfam15921 834 SVRLKLQ 840
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1682-1907 |
3.28e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1682 EEQAVRQRELAEQELEK-QRQLAEgtAQQRL-AAEQELIRLRAETE--QGEQQRQLLEEELARLQHEATAATQKRQELEA 1757
Cdd:COG3206 163 EQNLELRREEARKALEFlEEQLPE--LRKELeEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1758 ELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1837
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1838 TEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAALHKADIEERLAQLRKASESE 1907
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3132-3168 |
3.59e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.59e-06
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 3132 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3168
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2805-2840 |
3.84e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.84e-06
10 20 30
....*....|....*....|....*....|....*.
gi 254675119 2805 RLLEAQIATGGIIDPVHSHRVPVDVAYKRGYFDEEM 2840
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2161-2346 |
4.10e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.11 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2161 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQME 2240
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2241 ELGKLKARIEaenRAL-ILRDKDNT----QRFLEEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2312
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 254675119 2313 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2346
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2166-2621 |
4.26e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2166 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEE-TDHQKSILDE-ELQRLKAEVTEAAR-----QRSQVEEELFSVRVQ 2238
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEElEEERDDLLAEaGLDDADAEAVEARReeledRDEELRDRLEECRVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2239 MEELGK----LKARI-EAENRALILRDKDNTqrfLEEEAEKMK-QVAEEAARLSVAAQEAARLRQL---AEEDLAQQRAL 2309
Cdd:PRK02224 337 AQAHNEeaesLREDAdDLEERAEELREEAAE---LESELEEAReAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2310 AEKMLKEKMQAVQEATRLKAEaelLQQQKELAQEQARRLQEDKEQMAQQLVEETqGFQRTLEAERQRQLEMSAEAERLKL 2389
Cdd:PRK02224 414 LEELREERDELREREAELEAT---LRTARERVEEAEALLEAGKCPECGQPVEGS-PHVETIEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2390 RMAEMSRAQARAEE------DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2463
Cdd:PRK02224 490 EVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2464 LKQEAKLLQLKSEEM-QTVQQEQILQETQALQKSFLSEKDSLL-QRERFIEQEKAKLEQLFQDEVAKAKQLREEQQrqqq 2541
Cdd:PRK02224 570 AREEVAELNSKLAELkERIESLERIRTLLAAIADAEDEIERLReKREALAELNDERRERLAEKRERKRELEAEFDE---- 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2542 qmeqekqelmASMEEARRRQREAEE------GVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALA-HS 2614
Cdd:PRK02224 646 ----------ARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAlYD 715
|
....*..
gi 254675119 2615 EIATTQA 2621
Cdd:PRK02224 716 EAEELES 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1151-1601 |
4.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1151 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKR 1230
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1231 RQEQIQAVpiancQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLepvaspakkpkvqsg 1310
Cdd:COG4717 127 LLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1311 SESVIQEYVDLRTRYSELttltsqyikfiSETLRRMEEEERLAEQQRAEERERLAEVEAALE---KQRQLAEAHAQAKAQ 1387
Cdd:COG4717 187 SLATEEELQDLAEELEEL-----------QQRLAELEEELEEAQEELEELEEELEQLENELEaaaLEERLKEARLLLLIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1388 AELEAQELQRRMQEEVARREEAAVDAQQQ------KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRL 1461
Cdd:COG4717 256 AALLALLGLGGSLLSLILTIAGVLFLVLGllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1462 QLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESqrkrqaEAELALRVKAEAEAAREKQRALQALD 1541
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED------EEELRAALEQAEEYQELKEELEELEE 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1542 ELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1601
Cdd:COG4717 410 QLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1364-1458 |
4.65e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.42 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1364 LAEVEAALEKQRQLAEAHAQAKAQAeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKAQQV 1442
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQS----QALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 254675119 1443 EAAERSRMRI---EEEIRV 1458
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2286-2564 |
4.75e-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: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2286 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmaQQLVEETQG 2365
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK----QQQLAAISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2366 FQRTLEAERQRQLEMSAEAERlklrmaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2445
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2446 DAE---RLREAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSllqrerfiEQEKAKLEQ 2520
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 254675119 2521 LFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRR-QREA 2564
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1341-1577 |
4.95e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 52.68 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQ 1415
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1416 QKRSIQEElqhlrqsseaeiqAKAQQVEAAERSRMRIEEeirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQ 1495
Cdd:PRK07735 93 AKAKAAAA-------------AKAKAAALAKQKREGTEE---------VTEEEKAAAKAKAAAAAKAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1496 EEAERLRRQVQDESQRKRQAEAelalrVKAEAeAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRS 1575
Cdd:PRK07735 151 EEVTEEEEETDKEKAKAKAAAA-----AKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
..
gi 254675119 1576 AE 1577
Cdd:PRK07735 225 QG 226
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1728-1919 |
5.04e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1728 EQQRQLLEEELAR-LQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGRFR----ELA 1802
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1803 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 1881
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 254675119 1882 LEEQAALHKADIEERLAQLRKASESELERQKGLVEDTL 1919
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2268-2630 |
5.48e-06 |
|
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: 53.05 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2268 LEEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2347
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2348 LQEDKEQMAQQLVEETQgfqrtLEAERQRQLEMSAEAERLKLrmaemsraqaraEEDAQRFRKQAEEIGEKLHRtELATQ 2427
Cdd:pfam02463 249 EQEEIESSKQEIEKEEE-----KLAQVLKENKEEEKEKKLQE------------EELKLLAKEEEELKSELLKL-ERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2428 EKVTLVQTLEIQRQQSDHDAERLREAIAELEREKeKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQR 2507
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2508 ERFIEQEKAKLEQLFQdevaKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVR-RKQEELQHLEQQRQQQE 2586
Cdd:pfam02463 390 AKLKEEELELKSEEEK----EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTeEKEELEKQELKLLKDEL 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 254675119 2587 KLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALPNG 2630
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2252-2528 |
6.02e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2252 ENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA 2331
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2332 ELLQQQKELAQEQARRLQEDKEQMAQqlvEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2411
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRAR---IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2412 AEEIGEKLHRT------ELATQEKVTLVQTLEIQ----RQQSDHDAER---------LREAIAELEREKEKLKQeakLLQ 2472
Cdd:TIGR00618 320 MRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQeihiRDAHEVATSIreiscqqhtLTQHIHTLQQQKTTLTQ---KLQ 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2473 LKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAK 2528
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3463-3499 |
6.46e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.55 E-value: 6.46e-06
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 3463 IRLLEAQVATGGIIDPVHSHRLPVDVAYQRGYFDEEM 3499
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1694-2082 |
6.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1694 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EATAATQKRQELEAELAKVRAEMEvlla 1771
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1772 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRaeaervlteklaaISEATRLK 1851
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------------LAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1852 TEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVedtlrqrrQVEEEIMA 1931
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL--------FLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1932 LKVSF---EKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV 2008
Cdd:COG4717 288 LLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 2009 ALEEVERL--KAKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEKA-HAFVVQQREEELQQTLQQEQNMLDRLR 2082
Cdd:COG4717 368 LEQEIAALlaEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGElEELLEALDEEELEEELEELEEELEELE 445
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
621-713 |
6.77e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 621 HGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQA 700
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 254675119 701 ALQTQWSWMLQLC 713
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1354-1536 |
6.97e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1354 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRrmqeEVARREEAAVDAQQQKRSIQEELQHLRqsSEA 1433
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1434 EIQAKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1513
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 254675119 1514 QAEAELALRVKAEAEAAREKQRA 1536
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRK 185
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1328-1567 |
7.09e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1328 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAELEAQELQRrMQEEVAR 1405
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1406 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggAEGELQALRAR-A 1484
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1485 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEaAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1564
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
...
gi 254675119 1565 VQV 1567
Cdd:COG3206 388 VRV 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1783-2226 |
7.37e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1783 TSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1861
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1862 EAENERLRRLAEdeafQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAA 1941
Cdd:COG4717 145 PERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1942 GKAELELELGRIRSNAEDTMRSKEQAELEAArQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-- 2019
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2020 -VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEA 2098
Cdd:COG4717 300 lGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2099 REQAEREAAQSRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQAALKQK-QAADAEMEKHKKFAE 2177
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKE----------ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 254675119 2178 QTLRQKAQVEQELTTLrlqleETDHQKSILDEELQRLKAEVTEAARQRS 2226
Cdd:COG4717 450 ELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
159-266 |
7.47e-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: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 159 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 237
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 254675119 238 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 266
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2181-2466 |
8.75e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2181 RQKAQVEQELTTLRLQLeeTDHQKSiLDEE-------------LQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkA 2247
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQQA-LDVQqtraiqyqqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2248 RIEAENRaliLRDKDNTQRFLEEEAEKMKQVAEEaarlsVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKM 2318
Cdd:PRK04863 458 LLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGE-----VSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2319 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEEtqgfqrtLEAERQRQLEMSAEAERLKLRMAE-MSRA 2397
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARA 602
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2398 QA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLREAIAELEREKEKLKQ 2466
Cdd:PRK04863 603 PAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2178-2571 |
8.83e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2178 QTLRQKAQVE------QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS----QVEEELFSVRVQMEELGKLKA 2247
Cdd:pfam15921 445 QMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaSLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2248 RIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedLAQQRALAEKMLKEKMQAVQEAT 2325
Cdd:pfam15921 525 RVDLKLQELQhLKNEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEKEIN 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2326 RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDA 2405
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2406 QRFRKQAEEIgeklhrtELATQEkvtlvqtLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQlkseEMQTVQQEQ 2485
Cdd:pfam15921 681 RNFRNKSEEM-------ETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ----KQITAKRGQ 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2486 IlqetQALQK--SFLSEKDSLLQRER-FIEQEKAKLEQLFQdEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRR-- 2560
Cdd:pfam15921 743 I----DALQSkiQFLEEAMTNANKEKhFLKEEKNKLSQELS-TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKas 817
|
410 420
....*....|....*....|.
gi 254675119 2561 ----------QREAEEGVRRK 2571
Cdd:pfam15921 818 lqfaecqdiiQRQEQESVRLK 838
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2265-2574 |
9.82e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2265 QRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2344
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2345 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2424
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2425 ATQEKvtlvqTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLksEEMQTVQQEQILQETQALQKsflsekdsL 2504
Cdd:pfam13868 191 AQQEK-----AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQR--QELQQAREEQIELKERRLAE--------E 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2505 LQRERfieQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEE 2574
Cdd:pfam13868 256 AEREE---EEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLRE 322
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1344-1459 |
1.03e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-ELEAQELQRRMQEEVARREEAAVD---------A 1413
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675119 1414 QQQKR----SIQEELQHLRQSSEAEIQAkaqQVEAAERsRMRIEEEIRVV 1459
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAEEKA---RLEAEER-RQKEEEAARLA 508
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1712-1807 |
1.06e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.88 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1712 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1791
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 254675119 1792 EAEAGRFrELAEEAAR 1807
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1353-1781 |
1.08e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.83 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1353 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1432
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1433 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1512
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1513 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1592
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1593 QLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAE 1672
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1673 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1752
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 254675119 1753 QELEAELAKVRAEMEVLLASKARAEEESR 1781
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3929-3967 |
1.10e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.10e-05
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3929 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3967
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1487-1697 |
1.21e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1487 AEAQKRQAQEEAERLRRQVQDESQRKRQAEaELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQ 1566
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1567 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEaerelerwqlKANEALRL 1646
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA----------KKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1647 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1697
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
952-1565 |
1.23e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 952 DRLVAEREYGSCSRhyQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETrtvhrlrlplDKDPAREcaqRIAEQQKA 1031
Cdd:PRK02224 223 ERYEEQREQARETR--DEADEVLEEHEERREELETLEAEIEDLRETIAETER----------EREELAE---EVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1032 ----QAEVEGLGKGVARLSAEAEKVLALPEpspaapTLRSELELTLGKLEQVRSlsaiyleklkTISLVIRSTQGAEEVL 1107
Cdd:PRK02224 288 leelEEERDDLLAEAGLDDADAEAVEARRE------ELEDRDEELRDRLEECRV----------AAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1108 KTHEEQLKEAQAVPATLQ-ELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTql 1186
Cdd:PRK02224 352 DDLEERAEELREEAAELEsELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1187 lerwqavlaqtdvrqrELEqlgrqlryyresadplsawlqdakrrqeqiqavpiANCQAAREQLRQEKALLEEierhgEK 1266
Cdd:PRK02224 430 ----------------ELE-----------------------------------ATLRTARERVEEAEALLEA-----GK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1267 VEECQKFAKQ--YINAIKDYELQLITYKAQLEPVASpakkpkvqsgsesviqEYVDLRTRYSELTTLTSQyikfiSETLR 1344
Cdd:PRK02224 454 CPECGQPVEGspHVETIEEDRERVEELEAELEDLEE----------------EVEEVEERLERAEDLVEA-----EDRIE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1345 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevARREEAAVDAQQQkrSIQEEL 1424
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLA--ELKERI 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1425 QHLR--QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAlrARAEEAEAQKRQAQEEAErlr 1502
Cdd:PRK02224 589 ESLEriRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLE--- 663
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1503 rQVQDESQRKRQAEAELALRVKA------EAEAAREKQRAL----QALDELRLQAEEAERRLRQAEAE-RARQV 1565
Cdd:PRK02224 664 -QVEEKLDELREERDDLQAEIGAveneleELEELRERREALenrvEALEALYDEAEELESMYGDLRAElRQRNV 736
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2183-2608 |
1.29e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2183 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSVRVQMEELGKLKAriEAENRALILRDKD 2262
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2263 NTQ-RFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2337
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2338 ----KELAQEQARRLQEDKEQMaQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEmsraqaraEEDAQRFRKQAE 2413
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2414 EIGEKLHRTElatQEKVTLVQTleiqRQQSDHDAERLREAIAELE----REKEKLKQEAKLLQLKSEEMQTVQQEQILQE 2489
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQA----REKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2490 TQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQqqmeqEKQELMASMEEARRRQREAEEGVR 2569
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES-----VREEFIQKGDEVKCKLDKSEENAR 576
|
410 420 430
....*....|....*....|....*....|....*....
gi 254675119 2570 RKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2608
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1951-2616 |
1.58e-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: 51.51 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1951 GRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRR---------REAEERVQRSLAAEEEAARQRKVALEEVERLKAKVE 2021
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKklieetenlAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2022 EARRLR-------ERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEE 2094
Cdd:pfam02463 222 EEEYLLyldylklNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2095 AEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKK 2174
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2175 FAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGklKARIEAENR 2254
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK--EELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2255 ALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAqQRALAEKMLKEKMQAVQEATRLKAEAELL 2334
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL-KVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2335 QQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEE 2414
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2415 IGEKLHRTELATQEKVTLVQTLEIQRQQsdhdaeRLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQ 2494
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKES------GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2495 KSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEgvRRKQEE 2574
Cdd:pfam02463 693 EILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE--EKSELS 770
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 254675119 2575 LQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEI 2616
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1402-1567 |
1.80e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 51.30 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1402 EVARR----EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggaegel 1477
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1478 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEsqrkrqaeaelalrvKAEAEAAREKQRALQALDElRLQAEEAERRLRQ 1556
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 254675119 1557 AEAERARQVQV 1567
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3095-3131 |
1.81e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.81e-05
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 3095 KLLSAEKAVTGYRDPYSGQSVSLFQALKKGLIPREQG 3131
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1653-1974 |
1.85e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.37 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1653 VAQQKSLAQADA--EKQKEEAEREARRRGKAEEQAVRQRelaeQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ 1730
Cdd:NF012221 1535 VATSESSQQADAvsKHAKQDDAAQNALADKERAEADRQR----LEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1731 RQLLEEELARLQHEATAATQKRQELEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEAGRF----R 1799
Cdd:NF012221 1608 RDAILEESRAVTKELTTLAQGLDALDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQ 1685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1800 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1879
Cdd:NF012221 1686 KVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQA 1765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1880 RRLEEQAALHKADIEERlaqlRKASESELERQKGLVEDtlrqrrqVEEEIMALKVSFEKAAAGKaelelelgrirsNAED 1959
Cdd:NF012221 1766 QADAKGAKQDESDKPNR----QGAAGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG 1822
|
330
....*....|....*
gi 254675119 1960 tMRSKEQAELEAARQ 1974
Cdd:NF012221 1823 -LTEQEQEALEGATN 1836
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1637-1833 |
1.88e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1637 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQE 1716
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1717 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAE 1794
Cdd:COG2268 268 -----YEIAEANAEREVqRQLEIAEREREIELQEKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAE 339
|
170 180 190
....*....|....*....|....*....|....*....
gi 254675119 1795 AGRFRELAEEAARLRALAEEAKRQRQLAEedAARQRAEA 1833
Cdd:COG2268 340 AEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEAAAKP 376
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2286-2491 |
1.89e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.72 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2286 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQaVQEATRLKAEAELLQQQKelaQEQARRLQEDKEQMAQQLVEETQG 2365
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMRRLE-VERKRREQEEQRRLQQEQ---LERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2366 FQRTLEAERQRQlemsAEAERLKLRMAEMsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQE------KVTLVQTLEIQ 2439
Cdd:pfam15709 392 RKQRLEEERQRQ----EEEERKQRLQLQA--AQERARQQQEEFRRKLQELQRKKQQEEAERAEaekqrqKELEMQLAEEQ 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254675119 2440 RQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQ 2491
Cdd:pfam15709 466 KRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2170-2614 |
1.90e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2170 EKHKKFAEQTlRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELG- 2243
Cdd:COG4913 259 ELAERYAAAR-ERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGg 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2244 ----KLKARIEAENRALilRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2318
Cdd:COG4913 338 drleQLEREIERLEREL--EERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2319 QAVQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM---------------------------AQQLVEET 2363
Cdd:COG4913 416 DLRRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervlggfALTLLVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2364 QGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQS 2443
Cdd:COG4913 496 EHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA-ELGRRFDYVCVDSPEELRRHP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2444 ----------------DHDAERL-----------REAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQ 2494
Cdd:COG4913 575 raitragqvkgngtrhEKDDRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2495 KSFLSEKDsLLQRERFIEQEKAKLEQL--FQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQ 2572
Cdd:COG4913 655 EYSWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 254675119 2573 EELQHLEQQRQQQEKLLAEEnQRLRERLQRLEEEHRAALAHS 2614
Cdd:COG4913 734 DRLEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEER 774
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1494-1751 |
1.92e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1494 AQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERArqvqvALETAQ 1573
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELA-----ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1574 RSAEVELQSKRASFAEKTAQLERtlqeehvtvaQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEV 1653
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAE----------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1654 AQQKslaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQL 1733
Cdd:COG4942 156 RADL---AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR--------LEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 254675119 1734 LEEELARLQHEATAATQK 1751
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1159-1564 |
1.96e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1159 QEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKrrqeqiqav 1238
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK--------- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1239 piancqaarEQLRQEKALLEEIERHGEKVEECQK---FAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVI 1315
Cdd:TIGR00606 765 ---------NDIEEQETLLGTIMPEEESAKVCLTdvtIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1316 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAELEA 1392
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQLVELSTEVQsLIREIKDAKEQDSPLE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1393 Q---ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL------------------RQSSEAEIQAKAQQVEAAERSRMR 1451
Cdd:TIGR00606 916 TfleKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienkiqdgkddyLKQKETELNTVNAQLEECEKHQEK 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1452 IEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeAAR 1531
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKR 1068
|
410 420 430
....*....|....*....|....*....|...
gi 254675119 1532 EKQRALQALDELRLQAEEAERRLRQAEAERARQ 1564
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1579-1974 |
2.06e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1579 ELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1658
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1659 LAQADAEKQKEEAEREARRRGKAEEQ---AVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLE 1735
Cdd:pfam19220 101 EAEAAKEELRIELRDKTAQAEALERQlaaETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1736 EELARLQH-------EATAATQKRQELEAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAAR 1807
Cdd:pfam19220 174 QENRRLQAlseeqaaELAELTRRLAELETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1808 LRALAEEAKRQRQLAEEDAARQRaeaervltEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAA 1887
Cdd:pfam19220 250 LEALTARAAATEQLLAEARNQLR--------DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1888 lhKADIEERLAQLRKA---SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAG-KAELElelgrirsnAEDTMRS 1963
Cdd:pfam19220 320 --RAELEERAEMLTKAlaaKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRlKEELQ---------RERAERA 388
|
410
....*....|.
gi 254675119 1964 KEQAELEAARQ 1974
Cdd:pfam19220 389 LAQGALEIARE 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2208-2427 |
2.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2208 DEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIlRDKDNTQRFLEEEAEKMKQVAEEAARLSV 2287
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2288 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM---A 2356
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaeL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2357 QQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQ 2427
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1360-1874 |
2.12e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.80 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1360 ERERLAEVEAALEKQ-----RQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRsiQEELQHLRQ----- 1429
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeyKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQ--DSELAKLRVeemeq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1430 --SSEAEIQAKAQqVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQd 1507
Cdd:pfam05701 113 giADEASVAAKAQ-LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1508 esqrkrQAEAELALRVKAEAEAAREKQRALQALDELRL-------QAEEAERRLRQaEAERARQVQVALETAqrsaEVEL 1580
Cdd:pfam05701 191 ------ATKESLESAHAAHLEAEEHRIGAALAREQDKLnwekelkQAEEELQRLNQ-QLLSAKDLKSKLETA----SALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1581 QSKRASFAektAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEALRLRLQAEevaqqkSLa 1660
Cdd:pfam05701 260 LDLKAELA---AYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEK---AKDEVNCLRVAAA------SL- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1661 QADAEKQKeeaerearrrgkAEEQAVRQRELA--------EQELEKQRQLAEgTAQQRLAAEQE--------LIRLRAET 1724
Cdd:pfam05701 327 RSELEKEK------------AELASLRQREGMasiavsslEAELNRTKSEIA-LVQAKEKEAREkmvelpkqLQQAAQEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1725 EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK------ARAEEESRSTSEKSKQR-------L 1791
Cdd:pfam05701 394 EEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEklalaaIKALQESESSAESTNQEdsprgvtL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1792 EAE-----AGRFRElAEEAARLRalAEEAKRQRQLAEEDAAR---QRAEAERVLTEKLAAISEATrlkTEAEIALKEKEA 1863
Cdd:pfam05701 474 SLEeyyelSKRAHE-AEELANKR--VAEAVSQIEEAKESELRsleKLEEVNREMEERKEALKIAL---EKAEKAKEGKLA 547
|
570
....*....|.
gi 254675119 1864 ENERLRRLAED 1874
Cdd:pfam05701 548 AEQELRKWRAE 558
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2212-2496 |
2.16e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2212 QRLKAEVTEAARQRSQVEEELFSVRVQmeelgKLKARIEAENRALILRDKDNTQRFLEEEAE--KMKQVAEEAARLSVAA 2289
Cdd:pfam05667 220 QEWEEEWNSQGLASRLTPEEYRKRKRT-----KLLKRIAEQLRSAALAGTEATSGASRSAQDlaELLSSFSGSSTTDTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2290 QEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATrlkaeaelLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQ 2367
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQ--------QQREEELEelQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2368 RTLEAERQRQLEMSAEAE--RLKLRMAE--------MSRAQARAEEDAQRFRKQAEEIGEklHRT--------------- 2422
Cdd:pfam05667 367 QVEEELEELKEQNEELEKqyKVKKKTLDllpdaeenIAKLQALVDASAQRLVELAGQWEK--HRVplieeyralkeaksn 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2423 -ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA-------KLLQL-KSEEMQTVQQEQILQETQAL 2493
Cdd:pfam05667 445 kEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrsaytrRILEIvKNIKKQKEEITKILSDTKSL 524
|
...
gi 254675119 2494 QKS 2496
Cdd:pfam05667 525 QKE 527
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1382-1539 |
2.18e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 50.11 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1382 AQAKAQAEL-EAQELQRRMQEEVARReEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER--SRMRIEEEIRV 1458
Cdd:pfam00529 59 ALDSAEAQLaKAQAQVARLQAELDRL-QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIdlARRRVLAPIGG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1459 V-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALrvkAEAEAAREKQRA 1536
Cdd:pfam00529 138 IsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIaEAEAELKL---AKLDLERTEIRA 214
|
...
gi 254675119 1537 LQA 1539
Cdd:pfam00529 215 PVD 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2168-2617 |
2.19e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2168 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDE---ELQRLKAEVTEAARQRSQVEE---ELFSVRVQMEE 2241
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEErheLYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2242 LGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSvaaQEAARL------------------RQLAEED- 2302
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---KEIKELkkaieelkkakgkcpvcgRELTEEHr 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2303 ---LAQQRALAEKMLKEKMQAVQEATRLKAEAE----LLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAE 2373
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRelekVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2374 RQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtLEIQRQQSDHDAE-RLRE 2452
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-ERLKELEPFYNEYlELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2453 AIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKSFlSEKDSLLQRERFIEQEKakleqlfqdEVAKAK 2530
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKrlEELRKELEELEKKY-SEEEYEELREEYLELSR---------ELAGLR 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2531 qlreeqqrqqqqmeqekqelmASMEEARRRQREAEEGVR--RKQEELQHLEQQRQQQEKLLAEENQRLRERLQRL--EEE 2606
Cdd:PRK03918 680 ---------------------AELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERVEELREKVKKYkaLLK 738
|
490
....*....|.
gi 254675119 2607 HRAALAHSEIA 2617
Cdd:PRK03918 739 ERALSKVGEIA 749
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2279-2729 |
2.36e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 50.74 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2279 AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2358
Cdd:COG4995 23 ALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALALALAAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2359 LVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2438
Cdd:COG4995 103 LAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2439 QRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKL 2518
Cdd:COG4995 183 LLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2519 EQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRE 2598
Cdd:COG4995 263 ALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2599 RLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgpsvEAEPEYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHT 2678
Cdd:COG4995 343 ALLAAALAAALALAAALALALLAALLLLL------------AALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLR 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2679 TVAELTQREDVYRYLKGRSSIAGLLLKP--TNEKLSVYTALQRQLLSPGTALI 2729
Cdd:COG4995 411 LLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2165-2406 |
2.38e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2165 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGK 2244
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2245 LKARI----EAENRALILRDKDNTQRFLEEeAEKMKQVAEEAARLsVAAQEAARlrqlaeEDLAQQRALAEKMLKEKMQA 2320
Cdd:COG3883 91 RARALyrsgGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2321 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2400
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
....*.
gi 254675119 2401 AEEDAQ 2406
Cdd:COG3883 243 AASAAG 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2254-2450 |
2.44e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2254 RALILRDKDNTQRFLEEEAEKMKQVAEEAarLSVAAQEAARLRQLAEEDLAQQRalaekmlkEKMQAVQEatRLKAEAEL 2333
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERR--------NELQKLEK--RLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2334 LQQQKELAQEQARRLQEDKEQMAQQL--VEETQGFQRTLEAERQRQLE----MSAEAERLKLrmaeMSRAQARAEEDAQR 2407
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQqeLEKKEEELEELIEEQLQELErisgLTAEEAKEIL----LEKVEEEARHEAAV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254675119 2408 FRKQAEEIGEklhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2450
Cdd:PRK12704 174 LIKEIEEEAK-----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1388-1547 |
2.51e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1388 AELEAQELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEeeirvvRLQlette 1467
Cdd:COG1566 74 ARLDPTDLQAALAQ--AEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQ------ALY----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1468 RQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrKRQAEAELalrvkAEAEAAREKqrALQALDELRLQA 1547
Cdd:COG1566 141 KKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQ--AELNLARTTIRA 212
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1481-1667 |
2.95e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1481 RARAEEAEAQ------KRQAQEEAerlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALDELRLQAEEAER-- 1552
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1553 -RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLreeaerraqqqaeaerare 1627
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM------------------- 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254675119 1628 EAERELERWQLKANEALRLRLQAEEVAQQKS----LAQADAEKQ 1667
Cdd:pfam15709 472 AEEERLEYQRQKQEAEEKARLEAEERRQKEEeaarLALEEAMKQ 515
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2160-2369 |
2.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSVRV 2237
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2238 QMEELGKLKARIEAENRaLILRDKDNTQRFLEEEAE---KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2314
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2315 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRT 2369
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2160-2484 |
3.04e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQm 2239
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2240 EELGKLKARIEAENRALILRDKDNTQRFLEEE---------------AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLa 2304
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEEL- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2305 qQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGfqrTLEAERQRQLEMSAEA 2384
Cdd:COG4717 322 -EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDEEELRAALEQAEEY 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2385 ERLKLRMAEMSR--AQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTL---------EIQRQQSDHDAERLREA 2453
Cdd:COG4717 398 QELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELreelaeleaELEQLEEDGELAELLQE 477
|
330 340 350
....*....|....*....|....*....|.
gi 254675119 2454 IAELEREKEKLKQEAKLLQLKSEEMQTVQQE 2484
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1405-1758 |
3.23e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1405 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1484
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1485 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1564
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1565 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1644
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1645 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1724
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 254675119 1725 EQGEQQRQLLEEELARLQHEATAATQKRQELEAE 1758
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1339-1544 |
3.36e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1339 ISETLRRMEEEERLAEQQRAEERERLAEVEAALekqrqlaeahAQAKAQAELEAQELqRRMQEEVARREEAAVDAQQQKR 1418
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1419 siqeelQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1492
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1493 -----QAQEEAERLRRQVQDESQRKrQAEAELALR--VKAEAEAAREKQRALQALDELR 1544
Cdd:COG1842 157 gidsdDATSALERMEEKIEEMEARA-EAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3351-3389 |
3.68e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.47 E-value: 3.68e-05
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3351 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3389
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1718-2023 |
3.73e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1718 IRLRA-ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1790
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1791 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlteklaaiseatrlkteAEIALKEKEAENERLRR 1870
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1871 LAEDEAFQRRrleeqaalhkadieerlAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAlkvsfeKAAAGKAELELEL 1950
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA------RAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1951 grIRSNAEDTMRSKEQAELEAARQRQLaaeeeqrrreaeeRVQRSLAAEEEAARQRKVALE-EVERLKAKVEEA 2023
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKA-------------AQQQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1320-1599 |
3.78e-05 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 49.83 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1320 DLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-AKAQAELE-A 1392
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1393 QELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVE------AAERSRMRIEEEirVVRLQLETT 1466
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1467 ERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqaldelrl 1545
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKAREFEVEA--------- 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1546 qaeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1599
Cdd:pfam15450 453 --------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1369-1549 |
3.80e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1369 AALEKQRQLAEAHAQAKAQAELEAQelQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERS 1448
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHR--LKELPAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1449 RMRIEEEIRVVRlqletTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1528
Cdd:COG1579 75 IKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|.
gi 254675119 1529 AAREKQRALQALDELRLQAEE 1549
Cdd:COG1579 150 ELAELEAELEELEAEREELAA 170
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1320-1600 |
3.85e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1320 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAELEAQELQRRM 1399
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1400 QEEVARREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGE 1476
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1477 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAARE-KQRALQALDELRLQAE- 1548
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1549 EAERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1600
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4386-4423 |
3.93e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 3.93e-05
10 20 30
....*....|....*....|....*....|....*...
gi 254675119 4386 QRFLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTA 4423
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1200-1558 |
3.93e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1200 RQRELEQLGRQlryyRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEI----ERHGEKVEECQKFAK 1275
Cdd:pfam02029 12 RRRAREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTakreERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1276 QYINAIKDYElqlitykaqlEPVASPAKKPKVQSGSESVIQEYVDLR-TRYSELTTLTSQyikfiSETLRRMEEEERLAE 1354
Cdd:pfam02029 88 EFDPTIADEK----------ESVAERKENNEEEENSSWEKEEKRDSRlGRYKEEETEIRE-----KEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1355 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELE-AQELQRRMQEEVARREEAAVDAQqqkrsiqEELQHLRQSSEA 1433
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvKYESKVFLDQKRGHPEVKSQNGE-------EEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1434 EIQAKAQQVEAAERSRMRIEEEIRvvrlqLETTERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1512
Cdd:pfam02029 226 RQGGLSQSQEREEEAEVFLEAEQK-----LEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 254675119 1513 RQAEAElalRVKAEAEaarEKQRALQALDelRLQAEEAERRLRQAE 1558
Cdd:pfam02029 301 KQEEAE---RKLREEE---EKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3351-3386 |
3.97e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 3.97e-05
10 20 30
....*....|....*....|....*....|....*.
gi 254675119 3351 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3386
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1271-1602 |
4.04e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.01 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1271 QKFAKQYINAIKDYelqlitYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1349
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1350 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ----------ELQRRMQE-EVARREEAAVDAQQQKR 1418
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1419 SIQEELQHLRQSSEAEiQAKAQQVEAAERSRMRIEEEIR---------VVRLQLETTE------RQRGGAEGELQALRAR 1483
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEAKrradaklkeAVEKNVATSEqdkpkrRAKRGVLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1484 AEEAEAQKRQAQEEAerlrrqVQDESQR--KRQAEAElalRVKAEAEAAREKQR-------ALQALDELRLQAEEAERRL 1554
Cdd:NF033838 280 ENDAKSSDSSVGEET------LPSPSLKpeKKVAEAE---KKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKV 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1555 RQAEA----ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1602
Cdd:NF033838 351 KEAELelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2271-2430 |
4.05e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2271 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2350
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2351 DKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2430
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1372-1592 |
4.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1372 EKQRQLAEAHAQ-AKAQAELEAqeLQR---RMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER 1447
Cdd:COG3883 20 AKQKELSELQAElEAAQAELDA--LQAeleELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1448 SRMR------------IEEEIRvvrlQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1515
Cdd:COG3883 98 SGGSvsyldvllgsesFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1516 EAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1592
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1635-1821 |
4.33e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1635 RWQLKANEALRLRLQAE----EVAQQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQR 1710
Cdd:pfam15709 335 RDRLRAERAEMRRLEVErkrrEQEEQRRLQQEQLERAEKM---------REELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1711 LAAEQELiRLRAETEQGEQQRQLLEEELARLQHE--------ATAATQKRQELEAELA---KVRAEMevllASKARAEEE 1779
Cdd:pfam15709 406 EERKQRL-QLQAAQERARQQQEEFRRKLQELQRKkqqeeaerAEAEKQRQKELEMQLAeeqKRLMEM----AEEERLEYQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254675119 1780 SRSTSEKSKQRLEAEAGRFRElaEEAARLraLAEEAKRQRQL 1821
Cdd:pfam15709 481 RQKQEAEEKARLEAEERRQKE--EEAARL--ALEEAMKQAQE 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2168-2578 |
4.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2168 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSVRVQMEE 2241
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2242 LGKLKARIEAENRALI--LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2319
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2320 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRMAEM 2394
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2395 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL-KQEAKL 2470
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2471 LQLKSE----------------EMQTVQQE--------------------QILQETQALQKSFLSEKDS---LLQRERFI 2511
Cdd:PRK03918 542 KSLKKElekleelkkklaelekKLDELEEElaellkeleelgfesveeleERLKELEPFYNEYLELKDAekeLEREEKEL 621
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 2512 EQEKAKLEQLFqDEVAKAKQLREEQQRQQQQMEQEKQELmaSMEEARRRQREAEEGVRRKQEELQHL 2578
Cdd:PRK03918 622 KKLEEELDKAF-EELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEEL 685
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4137-4165 |
4.47e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.47e-05
10 20
....*....|....*....|....*....
gi 254675119 4137 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4165
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1344-1517 |
4.51e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQaeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1423
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRL-----EEERQRQEEEERKQRLQLQAAQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1424 LQHLRQsseaEIQAKAQQVE---AAERSRMRIEEEIRVVrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaer 1500
Cdd:pfam15709 428 FRRKLQ----ELQRKKQQEEaerAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE--- 496
|
170
....*....|....*..
gi 254675119 1501 lRRQVQDESQRKRQAEA 1517
Cdd:pfam15709 497 -RRQKEEEAARLALEEA 512
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1783-2062 |
4.76e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.15 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1783 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA-EIALKEK 1861
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1862 EAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKvsfEKAAA 1941
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE---AEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1942 GKAELELELGRIRSNAEDTMRSKEQAElEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-V 2020
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 254675119 2021 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQ 2062
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2253-2615 |
4.78e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2253 NRALILRDKDNTQRflEEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2327
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2328 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLkLRMAE 2393
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2394 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQL 2473
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2474 KSEEMQTVQQEQILQEtqalqksfLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEqqrqqqqmeqekqelmas 2553
Cdd:COG3096 505 RSQQALAQRLQQLRAQ--------LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL------------------ 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 2554 MEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSE 2615
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQ 626
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1665-2022 |
4.86e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1665 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1744
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1745 ATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAE 1823
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1824 EDAARQR---AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQL 1900
Cdd:COG4372 169 LEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1901 RKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAE 1980
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 254675119 1981 EEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEE 2022
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1478-1716 |
4.86e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1478 QALRARAEEAEAQKRQAQEEAERLRRQVqDESQRKRQA--EAELALRVKAEAEAAREKQRALQA-LDELRLQAEEAERRL 1554
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1555 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREeaerraqqqaeaerareeaerele 1634
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA------------------------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1635 rwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELA--EQELEKQRQLAEGTAQQRLA 1712
Cdd:COG3206 299 --QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEE 376
|
....
gi 254675119 1713 AEQE 1716
Cdd:COG3206 377 ARLA 380
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1936-2495 |
5.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1936 FEKAAAGKAELELELGRIRSNAEDTMRSKEQAElEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKvalEEVER 2015
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2016 LKAKVEEARRLRERAEQEsARQLQLAQEAAQKRLqAEEKAHAFVVQQREEELQQTLQQEQNMLdRLRSEAEAARRAAEEA 2095
Cdd:PRK03918 236 LKEEIEELEKELESLEGS-KRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2096 EEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2175
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2176 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLK----------AEVTEAARQR--SQVEEELFSVRVQMEELG 2243
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKEllEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2244 KLKARIEAENRAL-ILRDKDNTQRFLEEEAEKMKQVAEE-----AARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2317
Cdd:PRK03918 473 EKERKLRKELRELeKVLKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2318 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQlEMSAEAERLKLRMAEMSRA 2397
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK-ELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2398 Q---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL------------VQTLEIQRQQSDHDAERLREAIAELEREKE 2462
Cdd:PRK03918 632 FeelAETEKRLEELRKELEELEKKYSEEEYEELREEYLelsrelaglraeLEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590
....*....|....*....|....*....|...
gi 254675119 2463 KLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2495
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1430-1665 |
5.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1430 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1507
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1508 -ESQRKRQAEAELAL------------RVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAErARQVQVALETAQR 1574
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1575 saevELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1654
Cdd:COG3883 172 ----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
250
....*....|.
gi 254675119 1655 QQKSLAQADAE 1665
Cdd:COG3883 248 GAGAAGAAGAA 258
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1445-1564 |
5.29e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.57 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1445 AERSRMRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvK 1524
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQER-----LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---K 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 254675119 1525 AEAEAAREKQRALQALDELRLQAEEAERRLRQaEAERARQ 1564
Cdd:pfam05672 81 AEEEAEEREQREQEEQERLQKQKEEAEAKARE-EAERQRQ 119
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1464-1715 |
5.45e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1464 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDEL 1543
Cdd:TIGR02794 25 HSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1544 RlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaqlreEAERRAQQQAEAE 1623
Cdd:TIGR02794 105 K-QAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA---------AEAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1624 RAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaEREARRRGKAEEQAVRQRELAEQELEKQRQla 1703
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAA---AAAAEAERKADEAELGDIFGLASGSNAEKQ-- 249
|
250
....*....|..
gi 254675119 1704 EGTAQQRLAAEQ 1715
Cdd:TIGR02794 250 GGARGAAAGSEV 261
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2259-2414 |
5.83e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2259 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2335
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2336 QQKELAQEQARRLQEDKE---QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRaqaRAEEDAQRF---- 2408
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 254675119 2409 -RKQAEE 2414
Cdd:pfam15709 512 aMKQAQE 518
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1348-2066 |
6.91e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1348 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1423
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1424 LQHLR-QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQ-----LETTERQRGGAEGELQALRARAEEAEAQKRQAQEE 1497
Cdd:PRK04863 378 QEENEaRAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1498 AERLRRQVQDESQRKRQAE--AELALRVKAEAEAAREKQRALQALDELRLQAEEAER----RLRQAEAERARQVQVALET 1571
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1572 AQRSAEVELQSK--RASFAEK-TAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWqLKANEALRlRL 1648
Cdd:PRK04863 538 LLAEFCKRLGKNldDEDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA-RL 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1649 QAEEVAQQKSLAQADAEKQKEEAERearrrgKAEEQAVRQRELAEQELEKQ-RQLaegtaQQRLAAEQELIRLRAETEQG 1727
Cdd:PRK04863 616 REQSGEEFEDSQDVTEYMQQLLERE------RELTVERDELAARKQALDEEiERL-----SQPGGSEDPRLNALAERFGG 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1728 EQQRQL-----LEEE------LARLQH--------EATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK 1788
Cdd:PRK04863 685 VLLSEIyddvsLEDApyfsalYGPARHaivvpdlsDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIA 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1789 QRlEAEAGRFRE--LAEEAARlRALAEEAKRQRQLAEEDAARQRAEAERVLT-----EKLAAISEATRLKTEAEIALKEK 1861
Cdd:PRK04863 765 DR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDVQKLQRlhqafSRFIGSHLAVAFEADPEAELRQL 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1862 EAE-NERLRRLAEDEAfqrrrLEEQAALHKADIEERLAQLRK-ASESELerqkgLVEDTLRQR-RQVEEEIMALkvsfEK 1938
Cdd:PRK04863 843 NRRrVELERALADHES-----QEQQQRSQLEQAKEGLSALNRlLPRLNL-----LADETLADRvEEIREQLDEA----EE 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1939 AAA-----GKA--ELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQrsLAAEEEAARQRKVAlE 2011
Cdd:PRK04863 909 AKRfvqqhGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAH--FSYEDAAEMLAKNS-D 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2012 EVERLKAKVEEARRLRERA-EQESARQLQLAQ-------------------EAAQKRLQ---------AEEKA------- 2055
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRArEQLRQAQAQLAQynqvlaslkssydakrqmlQELKQELQdlgvpadsgAEERArarrdel 1065
|
810
....*....|...
gi 254675119 2056 HAFVV--QQREEE 2066
Cdd:PRK04863 1066 HARLSanRSRRNQ 1078
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1368-1868 |
7.19e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.28 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1368 EAALEKQRQLAEAhAQAKAQAELeAQELQRRMQEeVARREEAAVDAQQQKRSIQE---ELQHLRQSSEAEiqakaqqvea 1444
Cdd:PRK10929 25 EKQITQELEQAKA-AKTPAQAEI-VEALQSALNW-LEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1445 aersrmriEEEIRVVRLQLETterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRRQVQDESQ-RKRQAEAELALrv 1523
Cdd:PRK10929 92 --------RDEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAREISDSLSQlPQQQTEARRQL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1524 kAEAEaarekqRALQALDELRLQAEEAERRLRQAEAerarqvqvaletAQRSAEVElqskrasfaektaqlertlqeehv 1603
Cdd:PRK10929 154 -NEIE------RRLQTLGTPNTPLAQAQLTALQAES------------AALKALVD------------------------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1604 tvaqlreeaerraqqqaeaerareeaerELERWQLKAN---EALRLRLqaeEVAQQKSlAQADAEKQKEeaerearrrgK 1680
Cdd:PRK10929 191 ----------------------------ELELAQLSANnrqELARLRS---ELAKKRS-QQLDAYLQAL----------R 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1681 AEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQHEATAATQK-RQELEA-- 1757
Cdd:PRK10929 229 NQLNSQRQRE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlr 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1758 ----ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRA 1831
Cdd:PRK10929 307 eqsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTA 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1832 EAERVLTEKLAA---------------ISEATRLK---TEAEIALKE-KEAENERL 1868
Cdd:PRK10929 376 EQNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1466-2068 |
7.23e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1466 TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ--VQDESQRKRQA--EAELALRVKAEAEAARE--------- 1532
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLdeLQQEASRRQQAlqQALAAEEKAQPQLAALSlaqparqlr 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1533 -----KQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTL---QEEHVT 1604
Cdd:PRK10246 294 phwerIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLAEHDRFRqwnNELAGW 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1605 VAQLREEAERRAQQQAEAERAREEaereleRWQLKANEALRLRLQAEEVAQqkslAQADAEKQKEEAEREARRRGKAEEQ 1684
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQQLTHA------EQKLNALPAITLTLTADEVAA----ALAQHAEQRPLRQRLVALHGQIVPQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1685 AVRQRELAE------QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgEQQRQLLEEELARLQ------------HEAT 1746
Cdd:PRK10246 439 QKRLAQLQVaiqnvtQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ-EARIKDLEAQRAQLQagqpcplcgstsHPAV 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1747 AATQ---------KRQELEAELAK-------VRAEMEVLLASKARAEEESRSTSEKSK------QRLEAEAGRFRELAEE 1804
Cdd:PRK10246 518 EAYQalepgvnqsRLDALEKEVKKlgeegaaLRGQLDALTKQLQRDESEAQSLRQEEQaltqqwQAVCASLNITLQPQDD 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1805 AARLRALAEEAKRQ-RQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIA-----LKEKEAENERLRRLAEDEAFQ 1878
Cdd:PRK10246 598 IQPWLDAQEEHERQlRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltLPQEDEEASWLATRQQEAQSW 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1879 RRRLEEQAALhkadiEERLAQLRKASESELERQKGLVED---TLRQRRQVEEEIMALKvsfEKAAAGKAELELELGRIrs 1955
Cdd:PRK10246 678 QQRQNELTAL-----QNRIQQLTPLLETLPQSDDLPHSEetvALDNWRQVHEQCLSLH---SQLQTLQQQDVLEAQRL-- 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1956 naedtmrSKEQAELEAARQrqlaaeeeqrrREAEERVQRSLAA-EEEAARQRKVALEEveRLKAKVEEARRLRERAEQES 2034
Cdd:PRK10246 748 -------QKAQAQFDTALQ-----------ASVFDDQQAFLAAlLDEETLTQLEQLKQ--NLENQRQQAQTLVTQTAQAL 807
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 254675119 2035 ARQLQLAQEAAQKRLQAE--EKAHAFVVQQ------REEELQ 2068
Cdd:PRK10246 808 AQHQQHRPDGLDLTVTVEqiQQELAQLAQQlrenttRQGEIR 849
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1540-2006 |
7.59e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 49.25 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1540 LDELRLQAEEAERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQ 1618
Cdd:COG3903 470 LETVREYAAERLAEAGERAAARRRHADYYLALAERaAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1619 QAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEkqkeeaeREARRRGKAEEQAVRQRELAEQELEK 1698
Cdd:COG3903 550 ALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAAR-------AAAAAAAAAAAAAAAAAAAAAAAAAA 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1699 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEE 1778
Cdd:COG3903 623 LLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAA 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1779 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIAL 1858
Cdd:COG3903 703 LAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1859 KEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEK 1938
Cdd:COG3903 783 AAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAA 862
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1939 AAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR 2006
Cdd:COG3903 863 AAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAA 930
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3798-3834 |
8.05e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.05e-05
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 3798 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3834
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2159-2377 |
8.17e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2159 LKQKQAA-DAEMEKHKKFAE-QTLRQ-KAQVEQELTTLRLQLEETDHQksildeelqrlkAEVTEAARQRSQVEEELFSV 2235
Cdd:NF012221 1551 AKQDDAAqNALADKERAEADrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2236 RVQMEELGKlkaRIEA----------------ENRALILRDK-----DNTQRFLEEEAEKMKQ--------VAEEAARLS 2286
Cdd:NF012221 1619 TKELTTLAQ---GLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSE 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2287 VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlveETQGF 2366
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAKGA 1772
|
250
....*....|.
gi 254675119 2367 QRTLEAERQRQ 2377
Cdd:NF012221 1773 KQDESDKPNRQ 1783
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
41-145 |
8.48e-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: 44.95 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 41 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHR 118
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAK 84
|
90 100
....*....|....*....|....*..
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2692-2730 |
8.72e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 42.31 E-value: 8.72e-05
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 2692 YLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALIL 2730
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
44-156 |
8.86e-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: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 44 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDY 114
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNS 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 254675119 115 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 156
Cdd:cd21323 104 ASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2181-2612 |
9.89e-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: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2181 RQKAQVEQELTTLRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2257
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2258 LRDKDNTQRFLEEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2336
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2337 QKELAQEQARRLQEDKEQMAQQLVEE--TQGFQ----RTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRK 2410
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERmsAKGLQmelsRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2411 QAEEIG----------EKLHRTELATQEKVTLVQTleiqRQQSDHDAERLREAIAELEREKEKLKQEAKLL--------- 2471
Cdd:pfam07111 427 AVARIPslsnrlsyavRKVHTIKGLMARKVALAQL----RQESCPPPPPAPPVDADLSLELEQLREERNRLdaelqlsah 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2472 -----------QLKSEEMQTV----QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQ-LFQDEVAKAKQLREE 2535
Cdd:pfam07111 503 liqqevgrareQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2536 QQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQ----EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAL 2611
Cdd:pfam07111 583 VAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLML 662
|
.
gi 254675119 2612 A 2612
Cdd:pfam07111 663 A 663
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3685-3721 |
1.04e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.04e-04
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 3685 RYLYGTGAVAGVYLPGSRQTLTIYQALKKGLLSAEVA 3721
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
186-263 |
1.09e-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: 44.22 E-value: 1.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 186 DNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 263
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1796-2042 |
1.09e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1796 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1875
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1876 AFQRRRLEEQAALHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELE 1949
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1950 LGRIRSNAEDTMRSKEQAELEAARQRQLaaeeeQRRREAEERVQRSLAAEEEAARQRKVALEE-VERLKAKVEEARRLRE 2028
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQK-----LTTAHRKEAENEALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 254675119 2029 RAEQESAR-QLQLAQ 2042
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
44-157 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 44 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIAL 112
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 254675119 113 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 157
Cdd:cd21325 102 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2181-2385 |
1.16e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2181 RQKAQVEQELTTLRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIl 2258
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2259 rDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQEATRLKAEAELLQQQK 2338
Cdd:COG3206 261 -QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEAELEALQAREASLQAQL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254675119 2339 ELAQEQARRLQEdKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAE 2385
Cdd:COG3206 337 AQLEARLAELPE-LEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1481-1751 |
1.19e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1481 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaeaELALRVKAEAEAAREKQRAlqaldELRLQAE----EAERRLRQ 1556
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKA-----EERREAEtaraEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1557 AEAERARQVQVALETAQRSAEVELQSKRAsfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeaerelerw 1636
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEA--------------------------------------------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1637 qlkanealrLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTAQQRLAAeqe 1716
Cdd:COG2268 300 ---------EREEAELEADVRKPAEAEKQAAE-------------------AEAEAEAEAIRAKGLAEAEGKRALAE--- 348
|
250 260 270
....*....|....*....|....*....|....*.
gi 254675119 1717 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQK 1751
Cdd:COG2268 349 -----AWNKLGDAAILLmLIEKLPEIAEAAAKPLEK 379
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1360-1581 |
1.21e-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: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.45 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1360 ERERLAEVEAALEKQRQLAEAHAQAKAQAE---LEAQELQRRMQEEVarreeaavdaqqqkRSIQEELQHLRQSSEAEIQ 1436
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQqlrTELQELEAQQQEEA--------------ESSREQLQELEEQLATERS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1437 AKaqqvEAAERSRMRIEEEIRVVRLQLETTERQRggaegelqalraraeeaEAQKRQAQEEAERLRRQVQDESQRKRQaE 1516
Cdd:pfam09787 108 AR----REAEAELERLQEELRYLEEELRRSKATL-----------------QSRIKDREAEIEKLRNQLTSKSQSSSS-Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1517 AELALRVKAEAEAAREKQRALQAL----DELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1581
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALstekNSLVLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLR 234
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2330-2615 |
1.22e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2330 EAELLQQQKELAQEQA----RRLQEDKEQMAQQLVEETQGfQRTLEAERQRQLEMS-----AEAERLKLRMAEMSRAQAR 2400
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2401 AEEDAQRFRKQAEEI-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDhdaERLREAIAELEREKEKLKQEAKLLQLKSEEM 2478
Cdd:pfam17380 346 RERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2479 QTVQQEQILQETQALQKsflsekdslLQRERFIEQEKAKLEQLfqdevakakqlreeqqRqqqqmEQEKQELMASMEEAR 2558
Cdd:pfam17380 423 EQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E-----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2559 RRQREAEEGVRRKQ----EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSE 2615
Cdd:pfam17380 473 KRKKLELEKEKRDRkraeEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2183-2610 |
1.24e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2183 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEaENRALILRDK 2261
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2262 DNTQRFLEEEAEKMKQVAEEAARLSVAAQEAArLRQLAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQQQ 2337
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2338 KELAQEQARRLQEDkeqmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2417
Cdd:PRK02224 351 ADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2418 KLH--RTELAT-QEKVTLVQTL-----------EIQRQQSDHDAERLREAIAELEREKEKLKQ-----EAKLLQLKSEEM 2478
Cdd:PRK02224 427 REAelEATLRTaRERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEeveevEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2479 QTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQ---EKAKLEQLFQD--EVAKAKQLREEQQRQQQQMEQEKQELMAS 2553
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEElreRAAELEAEAEEkrEAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2554 MEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQR---LEEEHRAA 2610
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERkreLEAEFDEA 646
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2159-2461 |
1.25e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.75 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2159 LKQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSVRVQ 2238
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2239 MEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2317
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2318 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRT---LEAERQRQLEMSAEAERLKLRMAEM 2394
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 2395 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLREaiaELEREK 2461
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1679-2057 |
1.32e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.09 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1679 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQHEATAATQK 1751
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1752 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1826
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1827 ARQRAEAERvlteklaaiSEATRL---KTEAEIALKE-KEAENERLRRLAED-----EAFQRRRLEEQAALHKADIEERL 1897
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAEEEaKRRADAKLKEAVEKnvatsEQDKPKRRAKRGVLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1898 AQLRKASESELERQKgLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAE------------LELELgrirsnAEDTMRSKE 1965
Cdd:NF033838 280 ENDAKSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEI------AESDVKVKE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1966 qAELEAARQRqlaaeeeqrrreaeervqrslAAEEEAARQRKVALEEVERLKA---KVEEARRLRERAEQESARQLQLAQ 2042
Cdd:NF033838 353 -AELELVKEE---------------------AKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEED 410
|
410
....*....|....*
gi 254675119 2043 EAAQKRLQAEEKAHA 2057
Cdd:NF033838 411 KVKEKPAEQPQPAPA 425
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3967-4001 |
1.33e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.33e-04
10 20 30
....*....|....*....|....*....|....*
gi 254675119 3967 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4001
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1353-1467 |
1.34e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1353 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ---AKAQAELEAQELQRRM---------QEEVARREEAAVDAQQQKRSI 1420
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 254675119 1421 QEELQHLRQSSEAEiqakaQQVEAAERSRMRIEEEIRVVRLQLETTE 1467
Cdd:COG1566 168 QAQLAQAQAGLREE-----EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2160-2472 |
1.56e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 KQKQAADAE---MEKHKKFAEQTLRQKAqVEQEL-----------TTLRLQlEETDHQKSILDEELQRLKAE---VTEAA 2222
Cdd:COG3096 297 ARRQLAEEQyrlVEMARELEELSARESD-LEQDYqaasdhlnlvqTALRQQ-EKIERYQEDLEELTERLEEQeevVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2223 RQRSQVEEELFSVRVQMEELGK-----LKARIEAENRAL----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA 2293
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSqladyQQALDVQQTRAIqyqqAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2294 RLR-----QLAEEDLAQQR-----ALAEKMLKE--KMQAVQEATRL-------KAEAELLQQ---------QKELAQEQA 2345
Cdd:COG3096 455 EEVleleqKLSVADAARRQfekayELVCKIAGEveRSQAWQTARELlrryrsqQALAQRLQQlraqlaeleQRLRQQQNA 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2346 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE---EIGEKLHRT 2422
Cdd:COG3096 535 ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPawlAAQDALERL 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2423 ELATQEKVTLVQTLEIQRQQSdhdAERLREAIAE---LEREKEKLKQEAKLLQ 2472
Cdd:COG3096 615 REQSGEALADSQEVTAAMQQL---LEREREATVErdeLAARKQALESQIERLS 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2160-2607 |
1.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETdhqKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2239
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2240 EELGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2314
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSN-----IPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2315 ------KEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQED-----------------KEQMAQQL----VEETQ 2364
Cdd:COG4913 489 ltllvpPEHYAAALRWvnrLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcVDSPE 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2365 GFQRT--------------------------------LEAERQRQ-LEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2411
Cdd:COG4913 569 ELRRHpraitragqvkgngtrhekddrrrirsryvlgFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERRE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2412 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---SDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQ 2488
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2489 ETQALQK--SFLSEKDSLLQRERFIEQekakLEQLFQDEVAKAKQLREEqqrqqqqmeqekqelmASMEEARRRQREAEE 2566
Cdd:COG4913 728 ELDELQDrlEAAEDLARLELRALLEER----FAAALGDAVERELRENLE----------------ERIDALRARLNRAEE 787
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 254675119 2567 GVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2607
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3761-3797 |
1.65e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.65e-04
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 3761 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPAEEA 3797
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2187-2416 |
1.66e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2187 EQELTTLRLQLEE----TDHQKSILDEELQRLKAEVTEAARQRS-----QVEEELFSVRVQMEELGKLKARI-EAENRal 2256
Cdd:COG3096 450 EQQATEEVLELEQklsvADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRLQQLRAQLaELEQR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2257 iLRDKDNTQRFLEEEAEKMKQVAEEAARLsvaaqeaarlrqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2336
Cdd:COG3096 528 -LRQQQNAERLLEEFCQRIGQQLDAAEEL--------------EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2337 Q-KEL---------AQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQ 2406
Cdd:COG3096 593 RiKELaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
250
....*....|
gi 254675119 2407 RFRKQAEEIG 2416
Cdd:COG3096 673 RLLALAERLG 682
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2163-2619 |
1.81e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2163 QAADAEMEKHKKFAEQTLRQKAQVEQElTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEEL 2242
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2243 GKLKARIEAEnralilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2322
Cdd:TIGR00618 427 AHAKKQQELQ------------QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2323 EATRLKAEAELLQQQkELAQEQAR----------RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2392
Cdd:TIGR00618 495 RLLELQEEPCPLCGS-CIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2393 EMSRAQARAEEDAQRFRKQAEEIgekLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2472
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2473 LKSEEMQ----------TVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQ 2542
Cdd:TIGR00618 651 LQLTLTQervrehalsiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2543 MEQEKQELMA---SMEEARRRQRE-----AEEGVRRKQE---------ELQHLEQQRQQQEKLLAEENQRLRErlqrLEE 2605
Cdd:TIGR00618 731 GSDLAAREDAlnqSLKELMHQARTvlkarTEAHFNNNEEvtaalqtgaELSHLAAEIQFFNRLREEDTHLLKT----LEA 806
|
490
....*....|....
gi 254675119 2606 EHRAALAHSEIATT 2619
Cdd:TIGR00618 807 EIGQEIPSDEDILN 820
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4276-4309 |
1.85e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.85e-04
10 20 30
....*....|....*....|....*....|....
gi 254675119 4276 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4309
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1375-1744 |
1.95e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.22 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1375 RQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQ---QQKRSIQEELQHLRQSSEAEIQAKAQQVEA-AERSRM 1450
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMmeeERERALEEEEEKEEERKEERKRYRQELEEQiEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1451 RIEEEirvvrlqlettERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1530
Cdd:pfam13868 89 RQEEY-----------EEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1531 REKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQrsaevelqskrasfAEKTAQLERTLQEEHvtvaqlre 1610
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK--------------AERDELRAKLYQEEQ-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1611 eaerraqqQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1690
Cdd:pfam13868 216 --------ERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1691 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1744
Cdd:pfam13868 288 RLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1382-1863 |
2.00e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1382 AQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrl 1461
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1462 QLETTERQRGGAEgelqalRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALD 1541
Cdd:COG3064 78 KLAEAEKAAAEAE------KKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1542 ELRLQAEEAERRlrqAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAE 1621
Cdd:COG3064 152 AEAEAARAAAAA---AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1622 AERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1701
Cdd:COG3064 229 SREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1702 LAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1781
Cdd:COG3064 309 GAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1782 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1861
Cdd:COG3064 389 AGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKA 468
|
..
gi 254675119 1862 EA 1863
Cdd:COG3064 469 VA 470
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2163-2323 |
2.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2163 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQmEEL 2242
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2243 GKLKARIEAENRALILRDKDnTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2322
Cdd:COG1579 92 EALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
.
gi 254675119 2323 E 2323
Cdd:COG1579 171 K 171
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1474-1608 |
2.14e-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: 462900 [Multi-domain] Cd Length: 305 Bit Score: 46.67 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1474 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERR 1553
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1554 LRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVTVAQL 1608
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1392-1564 |
2.17e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.15 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1392 AQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqSSEAEIQAKAQQVeaaersrmrieeeirvvrlqlETTERQRG 1471
Cdd:COG3524 175 REDAVRFAEEEVERAEERLRDAREALLAFRNRNGIL--DPEATAEALLQLI---------------------ATLEGQLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1472 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeaarekQRALQALDELRLQAEEAE 1551
Cdd:COG3524 232 ELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSL------------ASLLAEYERLELEREFAE 299
|
170
....*....|....*
gi 254675119 1552 RRLRQAEA--ERARQ 1564
Cdd:COG3524 300 KAYTSALAalEQARI 314
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
39-152 |
2.33e-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: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 39 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQ 109
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCN 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 254675119 110 IALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21329 73 YAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2174-2622 |
2.51e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2174 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAEN 2253
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2254 RALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2333
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2334 LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2413
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2414 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2493
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2494 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQE 2573
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 254675119 2574 ELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAA 2622
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2179-2411 |
2.67e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2179 TLRQKAQVEQELTTLRLQleetdhQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIL 2258
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2259 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2332
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 2333 LLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2411
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1781-1929 |
2.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1781 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1859
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675119 1860 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1929
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1016-1509 |
2.76e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1016 DPARECAQRIAEQQKAQAE-VEGLGKGVARLSAEAEKV-LALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLK-- 1091
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIkMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNka 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1092 --TISLVIR----STQGAEEVLKTHEEQLKEAQavpatlQELEATKASLKKLRAQAEAQQPVFNTLRDELrgaqevgERL 1165
Cdd:pfam05483 344 kaAHSFVVTefeaTTCSLEELLRTEQQRLEKNE------DQLKIITMELQKKSSELEEMTKFKNNKEVEL-------EEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1166 QQRHGERDV---EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQL-------RYYRESADPLSAWLQDAKRRQEQI 1235
Cdd:pfam05483 411 KKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1236 QAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK------KPKVQS 1309
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1310 GSESVIQEYVDLRTRYSELTTLTS------QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHA 1382
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKlELELASAKQ 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1383 QAKA-----QAELEAQEL-QRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRmriEEEI 1456
Cdd:pfam05483 651 KFEEiidnyQKEIEDKKIsEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1457 RVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1509
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1655-1801 |
2.76e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.97 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1655 QQKSLAQA--DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQR 1731
Cdd:pfam17045 101 QRKQLKEAreEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1732 QLLEEELARLQH-----EATAATQKRQELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1801
Cdd:pfam17045 181 QCLEASQSEIQRlrsklERAQDSLCAQELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1771-1970 |
2.94e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1771 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLTEKLAAISEATRL 1850
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1851 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIM 1930
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254675119 1931 ALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1970
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1800-2035 |
3.11e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1800 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAeneRLRRLAEDEAFQR 1879
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1880 RRLEEQaalhKADIEERLAQLRKASE-------------SELERQKGLVEDTLRQRRqveEEIMALKVSFEKAAAGKAEL 1946
Cdd:COG4942 97 AELEAQ----KEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1947 ELELGRIRSNAEDtmRSKEQAELEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVAL-EEVERLKAKVEEARR 2025
Cdd:COG4942 170 EAERAELEALLAE--LEEERAALEALKAER-------------QKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
|
250
....*....|
gi 254675119 2026 LRERAEQESA 2035
Cdd:COG4942 235 EAAAAAERTP 244
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1680-1903 |
3.21e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1751
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1752 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE-EAKRQRQLAEEDAARQR 1830
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARaKAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1831 AEAERVLTEKL-AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAlhKADIEERLAQLRKA 1903
Cdd:PRK05035 607 VAEVDPKKAAVaAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQ--ANAEPEEAEDPKKA 678
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2160-2364 |
3.59e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 KQKQAaDAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR----------S 2226
Cdd:PRK11281 50 KQKLL-EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslrqleS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2227 QVEE-------------------------------ELFSVRVQMEELGKLKARIEAENRALI--LRDKDNT-QRFLEEEA 2272
Cdd:PRK11281 129 RLAQtldqlqnaqndlaeynsqlvslqtqperaqaALYANSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAeQALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2273 EKMKQVAEEAARLSVAAQE-----AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAElLQQQKELAQEQARR 2347
Cdd:PRK11281 209 DLQRKSLEGNTQLQDLLQKqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAAR-IQANPLVAQELEIN 287
|
250
....*....|....*..
gi 254675119 2348 LqedkeQMAQQLVEETQ 2364
Cdd:PRK11281 288 L-----QLSQRLLKATE 299
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1413-1614 |
3.72e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1413 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmRIEEEIRVVRLqletteRQRGGAEGELQALRARAEEAEAQKR 1492
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ---RAAEQARQKEL------EQRAAAEKAAKQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1493 QAQEEAErlrrqvQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERrlrQAEAERArqvqvALETA 1572
Cdd:TIGR02794 120 QAEEAKA------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK---KAEAEAK-----AKAEA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254675119 1573 QRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAER 1614
Cdd:TIGR02794 186 EAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1423-1571 |
3.84e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQA-------- 1494
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1495 -QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALET 1571
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1704-2053 |
3.94e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1704 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1783
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1784 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEA 1863
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1864 ENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGK 1943
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1944 AELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEA 2023
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350
....*....|....*....|....*....|
gi 254675119 2024 RRLRERAEQESARQLQLAQEAAQKRLQAEE 2053
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAE 462
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1327-1566 |
3.95e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 46.90 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1327 ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAELeaQELQRRMQE-EVAR 1405
Cdd:pfam13779 517 ELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEM-TQQDLQRMLDRIEELARSGRRAEAQQML--SQLQQMLENlQAGQ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1406 REEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAL 1480
Cdd:pfam13779 594 PQQQQQQGQSEMQQAMDELGDLLReqqqlLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEAL 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1481 RARAEEAEAQKRQAQEEAERLRRQVQ-DESQRKRQA-----EAELALRVKAEAEAAREKQRALQALdelrlqaEEAERRL 1554
Cdd:pfam13779 674 GDLAERQQALRRRLEELQDELKELGGkEPGQALGDAgramrDAEEALGQGDLAGAVDAQGRALEAL-------RKGAQQL 746
|
250
....*....|..
gi 254675119 1555 RQAEAERARQVQ 1566
Cdd:pfam13779 747 AEAMQQQQGQGQ 758
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1687-1977 |
4.13e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1687 RQREL------AEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqheataatqkrQELEAelA 1760
Cdd:COG0497 142 AQRELldafagLEELLEEYREAY----RAWRALKKELEELRADEAERARELDLLRFQL--------------EELEA--A 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1761 KVRAEMEVLLaskaraEEEsrstseksKQRLEAeAGRFRELAEEAarLRALAEEakrqrqlaEEDAARQRAEAERVLtEK 1840
Cdd:COG0497 202 ALQPGEEEEL------EEE--------RRRLSN-AEKLREALQEA--LEALSGG--------EGGALDLLGQALRAL-ER 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1841 LAAISE-----ATRLkTEAEIALKEKEAEnerLRRLAEDEAFQRRRLEEqaalhkadIEERLAQLRKaseseLERQKGL- 1914
Cdd:COG0497 256 LAEYDPslaelAERL-ESALIELEEAASE---LRRYLDSLEFDPERLEE--------VEERLALLRR-----LARKYGVt 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 1915 VEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAED--TMRSKEQAELEAARQRQL 1977
Cdd:COG0497 319 VEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKlsAARKKAAKKLEKAVTAEL 383
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1552-1873 |
4.38e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1552 RRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvtvaQLREEAERRAQQQAEAERAREEAER 1631
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEE------QIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1632 ELERWQLkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRL 1711
Cdd:pfam13868 106 IVERIQE---EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER--EEIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1712 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRsTSEKSKQRL 1791
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER-RLAEEAERE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1792 EAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRL 1871
Cdd:pfam13868 260 EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
..
gi 254675119 1872 AE 1873
Cdd:pfam13868 340 KE 341
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1018-1710 |
4.39e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1018 ARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSaiyleklktislvi 1097
Cdd:PRK10246 256 QQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALA-------------- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1098 RSTQGAEEV----LKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAqqpvFNTLRDELRG-----AQEVGERLQQR 1168
Cdd:PRK10246 308 HTRQQIEEVntrlQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDR----FRQWNNELAGwraqfSQQTSDREQLR 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1169 hgerdveveRWRERVTQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLSAWLQDAKRRQEQIQAvpiANC 1243
Cdd:PRK10246 384 ---------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1244 QAAREQLRQEKALLEEIERHGEKVEE-------CQKFAKqyinaIKDYElqliTYKAQLEPvASPAkkPKVQSGSESVIQ 1316
Cdd:PRK10246 451 NVTQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLE----AQRAQLQA-GQPC--PLCGSTSHPAVE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1317 EYVDLRtryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQaelEAQELQ 1396
Cdd:PRK10246 519 AYQALE----------------PGVNQSRLDALEKEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQ---EEQALT 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1397 RRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ----SSEAEIQAkaqQVEAAERSRMRIEEEIRVVRLQLETTERQrgg 1472
Cdd:PRK10246 579 QQWQAVCASLNITLQPQDDIQPWLDAQEEHERQlrllSQRHELQG---QIAAHNQQIIQYQQQIEQRQQQLLTALAG--- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1473 aegelQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA-LRVKAEAEAAREKQRALQALDELR------- 1544
Cdd:PRK10246 653 -----YALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTpLLETLPQSDDLPHSEETVALDNWRqvheqcl 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1545 -LQAE-EAERRLRQAEAERARQVQVALETAqrsaeveLQSKRasFAEKTAQLERTLQEEhvTVAQLREEAERRAQQQAEA 1622
Cdd:PRK10246 728 sLHSQlQTLQQQDVLEAQRLQKAQAQFDTA-------LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQA 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1623 ERAREEAERELERWQLKANEALRLRLQAEEVAQQksLAQadaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQL 1702
Cdd:PRK10246 797 QTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQE--LAQ---------------LAQQLRENTTRQGEIRQQ----LKQD 855
|
....*...
gi 254675119 1703 AEGTAQQR 1710
Cdd:PRK10246 856 ADNRQQQQ 863
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2183-2367 |
4.67e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2183 KAQVEQELTTLRLQLEETDHQKsiLDEELQRLKAEVTEAarqrsqVEEELFSV----RVQMEELGKLKARIEAENRALIl 2258
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKR--CQALLQELSAPLEEK------ISQGSYSVpggyQLYLEDREKLVEKYRQVPRKGV- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2259 RDKDNTQRFLEEEA--------------EKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKM 2318
Cdd:cd16269 167 KAEEVLQEFLQSKEaeaeailqadqaltEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKM 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254675119 2319 QavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLVEETQGFQ 2367
Cdd:cd16269 247 E--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3387-3422 |
4.72e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.72e-04
10 20 30
....*....|....*....|....*....|....*.
gi 254675119 3387 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3422
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2730-2763 |
4.76e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.76e-04
10 20 30
....*....|....*....|....*....|....
gi 254675119 2730 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2763
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1342-1518 |
4.78e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1342 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---------LAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD 1412
Cdd:PRK12678 45 GMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRaaraaaaarQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1413 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKR 1492
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREER 196
|
170 180
....*....|....*....|....*.
gi 254675119 1493 QAQEEAERLRRQVQDESQRKRQAEAE 1518
Cdd:PRK12678 197 GRDGDDRDRRDRREQGDRREERGRRD 222
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1395-2028 |
5.12e-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: 46.25 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1395 LQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAE 1474
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1475 gELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElaLRVKAEaeaarekqralQALDELRLQAEEAERRL 1554
Cdd:pfam05483 159 -LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1555 RQAEAERARQV-----QVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVTVAQLREEAERRAQQQAEAERAREEA 1629
Cdd:pfam05483 225 QHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1630 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegTAQQ 1709
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR----TEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1710 RLaaeqelirlraetEQGEQQRQLLEEELARLQHEATAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESRSTSE 1785
Cdd:pfam05483 371 RL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1786 KSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeialkekeaEN 1865
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------EN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1866 ERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEIMALKVS 1935
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1936 FEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE--------AARQRQLAAEEEQRRREAEERVQRSLAAEE------E 2001
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEiidnyqK 661
|
650 660 670
....*....|....*....|....*....|.
gi 254675119 2002 AARQRKVA----LEEVERLKAKVEEARRLRE 2028
Cdd:pfam05483 662 EIEDKKISeeklLEEVEKAKAIADEAVKLQK 692
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1068-1284 |
5.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1068 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATKASLkklraqaEAQQPV 1147
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1148 FNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLSAWLQD 1227
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1228 AKRRQEQIQAVPiancQAAREQLRQE-KALLEEIERHGEKVEEC-QKFAKQYINAIKDY 1284
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3018-3055 |
5.20e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.20e-04
10 20 30
....*....|....*....|....*....|....*...
gi 254675119 3018 RQALRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVA 3055
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1068-1602 |
5.25e-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: 46.50 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1068 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKthEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPV 1147
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE--EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1148 FNTLRDELRgaQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ-LGRQLRYYRESADPLSAWLQ 1226
Cdd:pfam02463 472 DLLKETQLV--KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1227 DAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEecQKFAKQYINAIKDYE-LQLITYKAQLEPVASPAK-- 1303
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL--KSIAVLEIDPILNLAqLDKATLEADEDDKRAKVVeg 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1304 ------------KPKVQSGSESVIQEYVDLRTRYSELTTLTS---QYIKFISETLRRMEEEERLAE-----------QQR 1357
Cdd:pfam02463 628 ilkdteltklkeSAKAKESGLRKGVSLEEGLAEKSEVKASLSeltKELLEIQELQEKAESELAKEEilrrqleikkkEQR 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1358 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQA 1437
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1438 KAQQVEAAERS------RMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDES 1509
Cdd:pfam02463 788 VEEEKEEKLKAqeeelrALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEE 867
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1510 QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1589
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
570
....*....|...
gi 254675119 1590 KTAQLERTLQEEH 1602
Cdd:pfam02463 948 KEKEENNKEEEEE 960
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2691-2727 |
5.26e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.26e-04
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 2691 RYLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTA 2727
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1680-1823 |
5.28e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEATAATQKRQELEAE 1758
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1759 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALAE-EAKRQRQLAE 1823
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNElEIAKAKELADiEATKFERIVE 795
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1703-2199 |
5.34e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.39 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1703 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV----------RAEMEVLLAS 1772
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1773 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKT 1852
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1853 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAL 1932
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1933 KVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE 2012
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2013 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAA 2092
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2093 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2172
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 254675119 2173 KKFAEQTLRQKAQVEQELTTLRLQLEE 2199
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
965-1393 |
5.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 965 RHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEAcetrtvhrlrlpldkdpARECAQRIAEQQKAQAEVEGLGKGVAR 1044
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEK-----------------LLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1045 LSAEAEKVLALPEpspAAPTLRSELELTLGKLEQVRSLSAiyLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQavpatl 1124
Cdd:COG4717 151 LEERLEELRELEE---ELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQ------ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1125 QELEATKASLKKLRAQAEAQQPvFNTLRDELRGAQEVGERL-----QQRHGERDVEV------------------ERWRE 1181
Cdd:COG4717 220 EELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALLallglGGSLLSLILTIagvlflvlgllallflllAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1182 RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRE-SADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQE-KALLEE 1259
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1260 IerHGEKVEECQKFAKQYiNAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFI 1339
Cdd:COG4717 379 A--GVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1340 SET---LRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ 1393
Cdd:COG4717 456 AELeaeLEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1337-1596 |
5.41e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1337 KFISETLR----RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQR-RMQEEVARREEAAV 1411
Cdd:pfam05667 250 KRIAEQLRsaalAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAaTSSPPTKVETEEEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1412 DAQQQK--RSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaegelQALRARA-EEAE 1488
Cdd:pfam05667 330 QQQREEelEELQEQLEDL----ESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ--------YKVKKKTlDLLP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1489 aqkrQAQEEAERLRRQVQDESQRKrqaeAELAlrvkAEAEAAR----EKQRALQalDELRLQAEEAERRLRQAEAERaRQ 1564
Cdd:pfam05667 398 ----DAEENIAKLQALVDASAQRL----VELA----GQWEKHRvpliEEYRALK--EAKSNKEDESQRKLEEIKELR-EK 462
|
250 260 270
....*....|....*....|....*....|..
gi 254675119 1565 VQVALEtaqrsaevELQSKRASFAEKTAQLER 1596
Cdd:pfam05667 463 IKEVAE--------EAKQKEELYKQLVAEYER 486
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1451-1596 |
5.62e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1451 RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1530
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1531 REKQRAL-----QALDELRLQAEEAERRLRQAEAERaRQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1596
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKK-DTLKARAKAAKAQEKVNEALSGIDSDDATSALER 169
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2247-2615 |
5.65e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2247 ARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLS-------VAAQEAARLRQLAEEDLAQQRAL--AEKMLKEK 2317
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNeaesdleQDYQAASDHLNLVQTALRQQEKIerYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2318 MQAVQEATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLklrMAEMS 2395
Cdd:PRK04863 361 EERLEEQNEVVEEA---DEQQEENEARAEAAEEEVDELKSQLADYQQALdvQQTRAIQYQQAVQALERAKQL---CGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2396 RAQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVQTLeiqRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKS 2475
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEEL----LSLEQKLSVAQAA---HSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2476 EEMQTVQQEQILQETQALQKSFLSEKDSllqrERFIEQEKAKLEQLFQDEvakakqlreeqqRQQQQMEQEKQELMASME 2555
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDE------------DELEQLQEELEARLESLS 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2556 EARRRQREAEEGVRRKQEelqhleqqrqQQEKLLAEENQR------LRERLQRLEEEHRAALAHSE 2615
Cdd:PRK04863 572 ESVSEARERRMALRQQLE----------QLQARIQRLAARapawlaAQDALARLREQSGEEFEDSQ 627
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2446-2574 |
5.68e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2446 DAERLREAIAELEREKEKLKQEAKLLqlkseemqtvqqEQILQETQALQKSFLSEKDSLLQRErfiEQEKAKLEQLFQDE 2525
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2526 VAKAKQLREEQQRQQQQMEQEKQELMAS--MEEARRRQREAEEGVRRKQEE 2574
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAheLIEARKRLNKANEKKEKKKKK 629
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1433-1566 |
5.71e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.05 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1433 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1512
Cdd:PRK12678 53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1513 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQ 1566
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAE 186
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3686-3724 |
6.10e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.00 E-value: 6.10e-04
10 20 30
....*....|....*....|....*....|....*....
gi 254675119 3686 YLYGTGAVAGVYLPGSRQTLTIYQALKKGLLSAEVARLL 3724
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
44-156 |
6.43e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 43.07 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 44 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIAL 112
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 254675119 113 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 156
Cdd:cd21324 102 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1680-2060 |
7.09e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 KAEEQAVRQRELAEQElekQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEElarlqheataATQKRQELEAEL 1759
Cdd:COG3064 9 AAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE----------AEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1760 AKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTE 1839
Cdd:COG3064 76 AKKLAE-----AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1840 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTL 1919
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1920 RQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAE 1999
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2000 EEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVV 2060
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2174-2341 |
7.13e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.23 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2174 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSVRVQMEEL----------- 2242
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALrsylspnspqv 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2243 GKLKARIEAenralilrdkdntqrfLEeeaekmKQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAV 2321
Cdd:COG3524 252 RQLRRRIAA----------------LE------KQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAAL 309
|
170 180
....*....|....*....|
gi 254675119 2322 QEAtrlKAEAEllQQQKELA 2341
Cdd:COG3524 310 EQA---RIEAA--RQQRYLA 324
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1683-1878 |
7.26e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1683 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1759
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1760 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAE-AGRFRELAEEAARLRALAEEAKRQRQLAE 1823
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQiAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 1824 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1878
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1265-1548 |
7.47e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1265 EKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLR 1344
Cdd:PRK10929 58 EERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1345 RMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAeleaqelqrrMQEEVARReEAAVDaqqqkrsiQE 1422
Cdd:PRK10929 132 AREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA----------LQAESAAL-KALVD--------EL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ELQHLRQSSEAEIqakaqqveaaerSRMRIeeeirvvrlqlETTERQRGGAEGELQALRAR--------AEEAEAQKRQA 1494
Cdd:PRK10929 193 ELAQLSANNRQEL------------ARLRS-----------ELAKKRSQQLDAYLQALRNQlnsqrqreAERALESTELL 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1495 QEEAERLRRQVQDESQRKRQAEAEL---ALRVKAEA----EAAREKQRALQALDELRLQAE 1548
Cdd:PRK10929 250 AEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQALNTLREQSQ 310
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2297-2527 |
7.61e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 45.32 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2297 QLAEEDLAQQRALAEKMLKEKmqavqeatrlkaEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2376
Cdd:COG4487 18 SLYADIVKQRRAEFEKELAER------------LADAAKREAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2377 QLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtLVQTLEIQRQQsdhdaerlreaiaE 2456
Cdd:COG4487 86 ALAVAEEKEK---ELAALQEALAEKDAKLAELQAKELELLKKERELEDAKRE---AELTVEKERDE-------------E 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2457 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQetqalqksflsekdsllQRERFIEQEKAKLEQLFQDEVA 2527
Cdd:COG4487 147 LDELKEKLKKEEEEKQLAEKSLKVAEYEKQLK-----------------DMQEQIEELKRKKEQGSTQLQG 200
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1485-1564 |
7.77e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1485 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL----RVKAE--AEAAREKQRALQA-LDELRLQAEEAERRLRQA 1557
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAqqqeLVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 254675119 1558 EAERARQ 1564
Cdd:PRK11448 218 RKEITDQ 224
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1709-1864 |
7.90e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1709 QRLAAEQELIRlRAETEQGEQQRQLlEEELARLQHEATAATQKRQELEAELAkvraEMEVLLASKARAEEESRSTSEKSK 1788
Cdd:PRK00409 495 KRLGLPENIIE-EAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1789 QRLEAEAgrfrelaeEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1864
Cdd:PRK00409 569 EEAEKEA--------QQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1513-1855 |
8.01e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1513 RQAEAELALRVKAEAEAAREKQR--ALQAldelRLQAEEAERRLRQAEAERARQVQValETAQRSAEVELQSKRASFAEK 1590
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAREARHKKAAEARAAKD--KDAVAAALARVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1591 TAQLERTLQEEHVTVAQLREEaerraqqqaeaerareeaerelerwqlkanealrlRLQAEEVAQQKSLAQADAEKQKEE 1670
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREAR-----------------------------------KAQARARQAEKQAAAAADPKKAAV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1671 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqqrlaaeqelirlRAETEQGEQQrqlleeelarlqHEATAATQ 1750
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIA-------------RAKAKKAAQQ------------AASAEPEE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1751 KRQELEAELAKVRAEMEVLLASKARAEEESRSTSEkskqrleaeagrfrelaeEAARLRALAEE---AKRQRQLAEEDAA 1827
Cdd:PRK05035 606 QVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP------------------VDPRKAAVAAAiarAKARKAAQQQANA 667
|
330 340
....*....|....*....|....*...
gi 254675119 1828 RQRAEAERVLTEKLAAISEATRLKTEAE 1855
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1794-1903 |
8.04e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1794 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLTEKLAAISEATRLKTEAEIA-LKEKEAE 1864
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 254675119 1865 NERLRRLaedeafQRRRLEEQAAlHKADIEERL------AQLRKA 1903
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAA-KRLELSEEEtrilidQQLRKA 247
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1354-1457 |
8.24e-04 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 44.79 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1354 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAqelqrRMQEEVARREEAAVDAQQQKRS-IQEELQHLRQSSE 1432
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAA-----AAAEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675119 1433 ----------------AEIQAkaqQVEAAERSRMRIEEEIR 1457
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1354-1455 |
8.38e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.88 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1354 EQQRAEERERLAEVEAALEKQRQLAEAHAQAkaqaelEAQELQRRMQEEVARREEaaVDAQQQKRSIQEELQHLRQSSEA 1433
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 254675119 1434 EIQAKAQQVEAAERSRMRIEEE 1455
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1495-1819 |
9.06e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1495 QEEAERLRRQVQDESQRKRQAEAELALRV---------KAEAEAAREKQRALQALDEL-----RLQAEEAERRLRQAEAE 1560
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVtesvepnehNSYEEDSELKPSGQGGLDEEeafldRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1561 RaRQVQVALETAQRSAEVELQSKRASFAEKT-AQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1639
Cdd:pfam02029 84 E-RQKEFDPTIADEKESVAERKENNEEEENSsWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1640 ANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL-I 1718
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAeV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1719 RLRAETEQGEQQRQLLEEElarlQHEATAATQKRQELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEAGRf 1798
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKE----SEEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLREEEEK- 315
|
330 340
....*....|....*....|.
gi 254675119 1799 RELAEEAARLRALAEEaKRQR 1819
Cdd:pfam02029 316 RRMKEEIERRRAEAAE-KRQK 335
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1344-1600 |
9.09e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAELEaqelqrrmqeevarREEAAVDAQQQKRSIQE 1422
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1423 ELQhLRQSSEAEIQAKAQQVEAAERSR----MRI--------------EEEIRVVRLQLETTERQ---RGGAEGEL-QAL 1480
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARvdleAKIeslkeelaflkknhEEEVRELQAQVSDTQVNvemDAARKLDLtSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1481 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA-LDELRLQAEEAERRLRQAEA 1559
Cdd:pfam00038 173 AEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIeLQSLKKQKASLERQLAETEE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 254675119 1560 ERARQvqvaLETAQRSaeveLQSKRASFAEKTAQLERTLQE 1600
Cdd:pfam00038 253 RYELQ----LADYQEL----ISELEAELQETRQEMARQLRE 285
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1414-1583 |
9.37e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.39 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1414 QQQKRSIQEELQHLRQSSEAEIQAKAQQVE-----AAERSRM--RIE-EEIRVVRLQLETTerqrgGAEGELQAlRARAE 1485
Cdd:PTZ00491 647 DSLQKSVQLAIEITTKSQEAAARHQAELLEqeargRLERQKMhdKAKaEEQRTKLLELQAE-----SAAVESSG-QSRAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1486 -EAEAQKRQAQEEAErlrrqVQDESQRKRqaeaelALRVKAEAEAAREKQRALQALDELRLQAE---EAERRLRQAEAER 1561
Cdd:PTZ00491 721 aLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATK 789
|
170 180
....*....|....*....|....*.
gi 254675119 1562 ARQVQVAL--ET--AQRSAEVELQSK 1583
Cdd:PTZ00491 790 FERIVEALgrETliAIARAGPELQAK 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2347-2626 |
9.63e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2347 RLQEDKEQMAQQLVEETQGFQRT--LEAERQRQLE-MSAEAERlklrmAEMSRAQARAEEDAQR--FRKQAEEIGEKLHR 2421
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLedILNELERQLKsLERQAEK-----AERYKELKAELRELELalLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2422 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ-----LKSEEMQTVQQEQILQETQALQKS 2496
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAneisrLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2497 FLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQ 2576
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 254675119 2577 HLEQQRQQQEKLLAEENQRLRERLQRLeEEHRAALAHSEIATTQAASTKA 2626
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKL-EEAELKELQAELEELEEELEEL 452
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2281-2506 |
9.87e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2281 EAARLsvAAQEAARLRQLAEE--DLAQQRALAEKMLKE---KMQAVQEATRLKAEAELLQQQKELA-------------- 2341
Cdd:PRK10929 120 EKSRQ--AQQEQDRAREISDSlsQLPQQQTEARRQLNEierRLQTLGTPNTPLAQAQLTALQAESAalkalvdelelaql 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2342 -----QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARA----EEDAQRFRKQ 2411
Cdd:PRK10929 198 sannrQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2412 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ------SDHDAERLREAIA---------ELERE-----------KEKLK 2465
Cdd:PRK10929 278 AQRMDLIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVArlpempkpqQLDTEmaqlrvqrlryEDLLN 357
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 254675119 2466 QEAKLLQLKSEEMQ--TVQQEQILQETQALQKSFLSekdSLLQ 2506
Cdd:PRK10929 358 KQPQLRQIRQADGQplTAEQNRILDAQLRTQRELLN---SLLS 397
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1097-1782 |
1.00e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1097 IRSTQGAEEVLKTHEEQLKEAQAVPATLQE-LEATKASLKKLRAQAEAQqpvFNTLRDELRGAQEVG-ERLQQRHGERDV 1174
Cdd:pfam12128 250 FNTLESAELRLSHLHFGYKSDETLIASRQEeRQETSAELNQLLRTLDDQ---WKEKRDELNGELSAAdAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1175 EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEK 1254
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1255 AL-LEEIERHGEKVE-ECQKFAKQYINAIKDYELQLITYKAQL-----EPVASPAKKPKVQSGSESVIQEYVDLRTRYSE 1327
Cdd:pfam12128 407 DRqLAVAEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELklrlnQATATPELLLQLENFDERIERAREEQEAANAE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1328 LTTLTSQYIKFIS---ETLRRMEEEERLAEQQRaeerERLAEVEAALEKQRqlAEAHAQAKAQAELEAQELQRRMQEEVA 1404
Cdd:pfam12128 487 VERLQSELRQARKrrdQASEALRQASRRLEERQ----SALDELELQLFPQA--GTLLHFLRKEAPDWEQSIGKVISPELL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1405 RREEaaVDAQQQKRSIQEELQ------HLRQ-------SSEAEIQAKAQQVE----AAERSRMRIEEEIRVVRLQLETTE 1467
Cdd:pfam12128 561 HRTD--LDPEVWDGSVGGELNlygvklDLKRidvpewaASEEELRERLDKAEealqSAREKQAAAEEQLVQANGELEKAS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1468 RQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRalQALDELRLQA 1547
Cdd:pfam12128 639 REETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK--EQKREARTEK 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1548 EEAERRLRQAEAERARQVQVALETAQRSAEVELQS----------KRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQ 1617
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAletwykrdlaSLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1618 QQAEAErareeaerelERWQLkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1697
Cdd:pfam12128 797 YFDWYQ----------ETWLQ---RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1698 KQRQLAEGTAQQRLAAEQElirlRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAE 1777
Cdd:pfam12128 864 GLRCEMSKLATLKEDANSE----QAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREE 938
|
....*
gi 254675119 1778 EESRS 1782
Cdd:pfam12128 939 DHYQN 943
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2114-2435 |
1.01e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2114 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQ-TLRQKAQVEQELTT 2192
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETgIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2193 LRLQLEETDHQKSILDEElqrlkaevteaaRQRSQVEEELFSVRVQMEElgkLKARIEAENRALilrdKDNTQRFLEEEA 2272
Cdd:COG5185 352 LTENLEAIKEEIENIVGE------------VELSKSSEELDSFKDTIES---TKESLDEIPQNQ----RGYAQEILATLE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2273 EKMKQVAEEAARLSVAaqeaarLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqARRLQE 2350
Cdd:COG5185 413 DTLKAADRQIEELQRQ------IEQATSSNEEVSKLLneLISELNKVMREADEESQSRLEEAYDEINRSVRSK-KEDLNE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2351 DKEQMAQQLVEETQGFQrTLEAERQRQLE-----MSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2425
Cdd:COG5185 486 ELTQIESRVSTLKATLE-KLRAKLERQLEgvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAAN 564
|
330
....*....|
gi 254675119 2426 TQEKVTLVQT 2435
Cdd:COG5185 565 LRTAVIDELT 574
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3058-3091 |
1.03e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....
gi 254675119 3058 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPE 3091
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1684-2595 |
1.09e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1684 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVR 1763
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1764 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1835
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1836 VLTEKLAAISEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---ALHKADIEERLAQLRKASESELERQK 1912
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1913 GLVEDTLRQRRQVEEEIMALKVSFEK----AAAGKAELELELGRIRSNAeDTMRSKEQAELEAARQRQLAAEEEQRRREA 1988
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKElqqlEGSSDRILELDQELRKAER-ELSKAEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1989 EERvqrSLAAEEEAARQRKVALEEVERL-KAKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAF-----VVQQ 2062
Cdd:TIGR00606 516 KLR---KLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKskeinQTRD 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2063 REEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRK 2142
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2143 EAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA 2222
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK-STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2223 RQRSQVEEELFSVRVQMEELGKLKARIEAENRA--LILRDKDNTQRFLEEEAEKMKQVAEEAARL-----SVAAQEAARL 2295
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2296 RQLAEEDL---AQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQedkeQMAQQLVEETQGFQRTLEA 2372
Cdd:TIGR00606 831 KQEKQHELdtvVSKIELNRKLIQDQQEQIQH---LKSKTNELKSEKLQIGTNLQRRQ----QFEEQLVELSTEVQSLIRE 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2373 ERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQT-LEIQRQQSDHDAERLR 2451
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVN 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2452 EAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQETQALQKsfLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAKQ 2531
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRK--RENELKEVEEEL-----KQHLKEMGQMQVLQMKQ 1054
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 2532 LReeqqrqqqqmeqekQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQR 2595
Cdd:TIGR00606 1055 EH--------------QKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1345-1532 |
1.12e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1345 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEEL 1424
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1425 QHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRqaQEEAERLRRQ 1504
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEALKAKD-------------------------HKAFDLKQESKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 254675119 1505 VQDESQR-KRQAEAElalrVKAEAEAARE 1532
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2160-2467 |
1.14e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2160 KQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2239
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2240 EELGKLKArieaenralILRDKdntqrFLEEEAEKmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2319
Cdd:pfam15905 132 LELTRVNE---------LLKAK-----FSEDGTQK---------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2320 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQA 2399
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 2400 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQE 2467
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1347-1530 |
1.18e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1347 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1426
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1427 LRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAErlrrqv 1505
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*
gi 254675119 1506 QDESQRKRQAEAELAlRVKAEAEAA 1530
Cdd:PRK05035 671 EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1334-1512 |
1.23e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1334 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR---REEAA 1410
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKarqRQELQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1411 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLeTTERQRGGAEGELQALRARAEEAEAQ 1490
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH-RRELEKQIEEREEQRAAEREEELEEG 317
|
170 180
....*....|....*....|..
gi 254675119 1491 KRQAQEEAERLRRqVQDESQRK 1512
Cdd:pfam13868 318 ERLREEEAERRER-IEEERQKK 338
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1723-1855 |
1.29e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1723 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1802
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1803 EEAARLRA-------------LAEEAKRQRQLAEEDAARQRAEAERVlTEKLAAISEATRLKTEAE 1855
Cdd:pfam05262 287 QIEIKKNDeealkakdhkafdLKQESKASEKEAEDKELEAQKKREPV-AEDLQKTKPQVEAQPTSL 351
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1622-2051 |
1.36e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1622 AERAREEAERELERWQLKANEALRLRLQAEevaqqkSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1701
Cdd:COG3903 487 RAAARRRHADYYLALAERAAAELRGPDQLA------WLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1702 LAEGT--AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1779
Cdd:COG3903 561 LREGRrwLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1780 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1859
Cdd:COG3903 641 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAA 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1860 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKA 1939
Cdd:COG3903 721 AAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1940 AAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2019
Cdd:COG3903 801 AAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAA 880
|
410 420 430
....*....|....*....|....*....|..
gi 254675119 2020 VEEARRLRERAEQESARQLQLAQEAAQKRLQA 2051
Cdd:COG3903 881 AAALLAAAAAAAAAAAAAAAAAAALAAAAAAA 912
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1334-1528 |
1.37e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1334 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarreeaavda 1413
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKE------------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1414 QQQKRSIQEELQHLRQSSEAEIQAKAQQvEAAERSRMRIEEEiRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1493
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 254675119 1494 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1528
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1697-1972 |
1.39e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 44.46 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1697 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK 1773
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1774 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1833
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1834 ErvLTEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLEE-QAALHK-ADIEERLAQLRKASES 1906
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIERaEKERAAsAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1907 ELERQKGLVEDTLRQRrqVEEEIMAlkvsfekaaagKAELELELGRIRSNAEDTmrSKEQAELEAA 1972
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEETEDA-----------KNKLEWQLKKTLQEIAEL--EKNIEALEKA 287
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2327-2620 |
1.47e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2327 LKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRTLEAERqrqlEMSAEAERLKLRMAEmsraqaraeedaq 2406
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAA------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2407 rfRKQaeEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqqEQI 2486
Cdd:pfam01576 69 --RKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLE----EDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2487 LqetqalqksFLSEKDSLLQRER-FIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQmeqekqelMASMEEARRRQ---R 2562
Cdd:pfam01576 141 L---------LLEDQNSKLSKERkLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM--------ISDLEERLKKEekgR 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 2563 EAEEGVRRKQEELQHLEQQRQQQEKLLAEEnqrLRERLQRLEEEHRAALAHSEIATTQ 2620
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAE---LRAQLAKKEEELQAALARLEEETAQ 258
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2238-2536 |
1.51e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2238 QMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2317
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2318 MQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMS 2395
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2396 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQlks 2475
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--- 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2476 EEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQ 2536
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1792-1916 |
1.52e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1792 EAEAGRFRELA-EEAARLRALAEEAKRQ----RQLAEEDAA--------RQRAEAERVLTEKLAAISEAtrlKTEAEIAL 1858
Cdd:COG2268 205 EAEAERETEIAiAQANREAEEAELEQEReietARIAEAEAElakkkaeeRREAETARAEAEAAYEIAEA---NAEREVQR 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1859 KEKEAENERLRRLAEDEAfQRRRLEEQAALHK-ADIEERLAQLRKASESELERQKGLVE 1916
Cdd:COG2268 282 QLEIAEREREIELQEKEA-EREEAELEADVRKpAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1679-1860 |
1.54e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1679 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEATAATQKRQELEA 1757
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1758 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDaarqrAEAERV 1836
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 254675119 1837 LTEKLAAISEATRLKTEAEIALKE 1860
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1477-1566 |
1.54e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1477 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEaarekQRALQALDELRLQAEEAERRLRQ 1556
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 254675119 1557 AEAERARQVQ 1566
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1889-2306 |
1.54e-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: 44.73 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1889 HKADIEERLAQlRKASESELERQKGLVEDTLRQ---RRQVEEEIMALKVSFEKAAAGKAELElelgrirsnaedTMRSKE 1965
Cdd:pfam17380 280 HQKAVSERQQQ-EKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRQAAIYAEQE------------RMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1966 QAELEAARQRQLAAeeeqrrreaeervqrslaaEEEAARQRKVALE-----EVERLKAKvEEARRLRERAEQESARQLQL 2040
Cdd:pfam17380 347 ERELERIRQEERKR-------------------ELERIRQEEIAMEisrmrELERLQME-RQQKNERVRQELEAARKVKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2041 AQEAAQKRLQAEEKAHAFVvqqreeelqqtlqqeqnmldrlrseaeaarraaeeaeeareqaereaaqsRKQVEEAERlk 2120
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQI--------------------------------------------------RAEQEEARQ-- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2121 qsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQaadaEMEKHKKFAEQTLRQKAQVEQElttLRLQLEET 2200
Cdd:pfam17380 435 -----------------REVRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEERKRKKLELEKE---KRDRKRAE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2201 DHQKSILDEELQRLKAEVTEAARQRSQVEEElfsvrvqMEELGKlkaRIEAENRALILRDKDNTQRFLEEE---AEKMKQ 2277
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKE-------MEERQK---AIYEEERRREAEEERRKQQEMEERrriQEQMRK 560
|
410 420
....*....|....*....|....*....
gi 254675119 2278 VAEEAARLSVAAQEAARLRQLAEEDLAQQ 2306
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2209-2417 |
1.55e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2209 EELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKM-----KQVAEEAA 2283
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2284 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLV 2360
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 2361 EETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2417
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2183-2560 |
1.58e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2183 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2262
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2263 NTQRFLEEE---AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmQAVQEATRLKAEAELLQQQKE 2339
Cdd:pfam07888 127 HEARIRELEediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ----QTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2340 LAQEQARRLQEDKEQMAQQLveeTQGFQRTLEAER--------QRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRK 2410
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKL---TTAHRKEAENEAlleelrslQERLNASERkVEGLGEELSSMAAQRDRTQAELHQARL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2411 QAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAkllqlkseemqtvqqeqilQE 2489
Cdd:pfam07888 280 QAAQLTLQLADASLALREgRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER-------------------ME 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2490 TQALQKSFLSEKDS----LLQRERFIEQEKAKLeQLFQDEvakakqlreeqqrqQQQMEQEKQELMASMEEARRR 2560
Cdd:pfam07888 341 REKLEVELGREKDCnrvqLSESRRELQELKASL-RVAQKE--------------KEQLQAEKQELLEYIRQLEQR 400
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1641-1863 |
1.60e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.85 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1641 NEALRLRLQ-AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--LAEGTAQQRLAAEQEl 1717
Cdd:COG5283 9 DKPFKSALEsAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQalDQAGIDTRQLSAAQR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1718 iRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVRAEME-----VLLASKARAEEESRSTSEKSKQRLE 1792
Cdd:COG5283 88 -RLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQR-LAGAGAAAAaigaaLAASVKPAIDFEDAMADVAATVDLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1793 AEAGRFRELAEEA----ARLRALAEE-AKRQRQLAEEDAARQRAEAervLTEKLAAISEATRLKTE--AEIALKEKEA 1863
Cdd:COG5283 166 KSSEQFKALGKQArelsAQTPQSADDiAAGQAALAQAGVSAEDILA---FTPTAAKLATAFDTDAEeaAEIAAKILNA 240
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1722-1849 |
1.62e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1722 AETEQGEQQRQLLEEELARLQHEATAATQKR-QELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQRLEAEAGRFRE 1800
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1801 LAEEAARLRALAEEAKRQRQLA--EEDAAR-------------QRAEAERVLT-------------EKLAAISEATR 1849
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEvtEEDIAEvvsrwtgipvgklLEGEREKLLNleeelhervigqdEAVEAVADAIR 566
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2211-2424 |
1.68e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2211 LQRLKAEVTEAARQRSQVEEElfsvrvQMEELGKLKARIEAENRALilrdkdNTQRFLEEEAEKMkqvAEEAARLSVAAQ 2290
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL------EKERLAAQEQKKQ---AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2291 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLVEETQGFQRT 2369
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2370 LEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2424
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1647-1817 |
1.76e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1647 RLQAEEVAQQKSLA-QADAE-KQKEEAEREARRRGkaEEQAVRQRELA---------EQELEKQRQLAEGTAQQRLAAEQ 1715
Cdd:PRK11637 114 KLEQQQAAQERLLAaQLDAAfRQGEHTGLQLILSG--EESQRGERILAyfgylnqarQETIAELKQTREELAAQKAELEE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1716 ELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEkskqrleaea 1795
Cdd:PRK11637 192 KQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAE---------- 261
|
170 180
....*....|....*....|..
gi 254675119 1796 grfRElAEEAARLRALAEEAKR 1817
Cdd:PRK11637 262 ---RE-AREAARVRDKQKQAKR 279
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1401-1885 |
1.77e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.62 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1401 EEVARREEAAVDAQQQK--RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG-EL 1477
Cdd:NF033838 53 NESQKEHAKEVESHLEKilSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQfKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1478 QALRARAEEAEAQK------RQAQEEAERLRRQVQDESQRKRQAE-AELALRVKaEAEAAREKQRALQALDELRLQAEEA 1550
Cdd:NF033838 133 DTLEPGKKVAEATKkveeaeKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1551 ERRLRQAEAERARQVQVALETAQRSAEvelqskrasfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeae 1630
Cdd:NF033838 212 KVESKKAEATRLEKIKTDREKAEEEAK----------------------------------------------------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1631 relERWQLKANEALRLRLQAEEVAQQKSLAQADAeKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1710
Cdd:NF033838 239 ---RRADAKLKEAVEKNVATSEQDKPKRRAKRGV-LGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE--AEKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1711 LAAEQElirlRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQR 1790
Cdd:NF033838 313 VEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAK-------EPRNEEKIKQAKAKVESK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1791 LeAEAGRFrelaeeaarlralaEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 1870
Cdd:NF033838 382 K-AEATRL--------------EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEK 446
|
490
....*....|....*..
gi 254675119 1871 LAEDEAFQ--RRRLEEQ 1885
Cdd:NF033838 447 PADQQAEEdyARRSEEE 463
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1354-1461 |
1.79e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1354 EQQRAEERERLAEVEAAL-----------EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVA------RREEAAVDAQQQ 1416
Cdd:PRK00409 526 EELERELEQKAEEAEALLkeaeklkeeleEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 254675119 1417 KRSIQEELQHLRQSSeaEIQAKAQQVEAAERSRMRIEEEIRVVRL 1461
Cdd:PRK00409 606 AHELIEARKRLNKAN--EKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2176-2354 |
1.81e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2176 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAarQRSQVEEELFSVRVQME-ELGKLKARIEAENR 2254
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2255 ALilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2334
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|
gi 254675119 2335 QQQKELAQEQARRLQEDKEQ 2354
Cdd:COG3206 364 RELYESLLQRLEEARLAEAL 383
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2180-2477 |
1.83e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2180 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIeaenralil 2258
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2259 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2338
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2339 ELAQEQARRLQEDKEQMAQQLVEET--QGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIG 2416
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2417 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2464
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 254675119 2465 KQEAKllQLKSEE 2477
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1344-1425 |
1.91e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.53 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAELEAQELQRR-----MQEEVARREEAAVDAQ 1414
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEalaeaQAEAQASKEKARREIE 111
|
90
....*....|.
gi 254675119 1415 QQKRSIQEELQ 1425
Cdd:PRK07353 112 QQKQAALAQLE 122
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2176-2424 |
1.92e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2176 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSVRVQMEELGK 2244
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2245 LKARIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedlaQQRALAEKMlkEKMQAVQ 2322
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPL------QYDCWWEKV--ENLQDLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2323 EATRLKAE--AELLQQQKELaqeqarrlqEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2400
Cdd:PLN02939 310 DRATNQVEkaALVLDQNQDL---------RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQL 380
|
250 260
....*....|....*....|....
gi 254675119 2401 AEEDAQRFRKQAEEIGEKLHRTEL 2424
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESKKRSL 404
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2168-2576 |
1.94e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2168 EMEKHKKFAEQTLRQKAQVEQELttlRLQLEETDHQ----KSILDEELQRLKAEVTEAAR---QRSQVEEELFSVRVQME 2240
Cdd:pfam15921 121 EMQMERDAMADIRRRESQSQEDL---RNQLQNTVHEleaaKCLKEDMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2241 E-----------LGKLKARIEAENRALILRDKDNTQRFL-------EEEAEKMKQVAEEAARLsVAAQEAARLRQLAEED 2302
Cdd:pfam15921 198 EasgkkiyehdsMSTMHFRSLGSAISKILRELDTEISYLkgrifpvEDQLEALKSESQNKIEL-LLQQHQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2303 LAQQRALAEKmlkekmqavqeATRLKAEAELLQQQKELAQEQARrlQEDKEQMAQ-QLVEETQGFQRTLEAERQRQLEMS 2381
Cdd:pfam15921 277 EVEITGLTEK-----------ASSARSQANSIQSQLEIIQEQAR--NQNSMYMRQlSDLESTVSQLRSELREAKRMYEDK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2382 AEAERLKLRMAEMSRAQARAEEDaqRFRKQAEEIGEKLHR--TELATQEKvtlvqTLEIQRQQSDHDAERLRE---AIAE 2456
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERD--QFSQESGNLDDQLQKllADLHKREK-----ELSLEKEQNKRLWDRDTGnsiTIDH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2457 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQ-KSFLSEKDSLLQRErfIEQEKAKLEQLFQDEVAKaKQLREE 2535
Cdd:pfam15921 417 LRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgKNESLEKVSSLTAQ--LESTKEMLRKVVEELTAK-KMTLES 493
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 254675119 2536 QQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQ 2576
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2165-2622 |
1.97e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2165 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSildEELQRLKAEVTEAARQR-SQVEEELFSVRVQMEELg 2243
Cdd:NF041483 209 AEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAES---DQARRQAAELSRAAEQRmQEAEEALREARAEAEKV- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2244 kLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEeaarlsvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQE 2323
Cdd:NF041483 285 -VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGE-------ATKEAEALKAEAEQALADARAEAEKLVAEAAEKART 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2324 ATRLKAEAELLQQQKElAQEQARRLQEDKEQMAQQLVEEtqgfqrtleAERQRQlEMSAEAERLKLRMAEMS-RAQARAE 2402
Cdd:NF041483 357 VAAEDTAAQLAKAART-AEEVLTKASEDAKATTRAAAEE---------AERIRR-EAEAEADRLRGEAADQAeQLKGAAK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2403 EDAQRFRKQAEEIGEKLHRTElatqekvtlvqtleiqrqqsdHDAERLR-EAIAELEREKEKLKQEAkllqLKSEEMQTV 2481
Cdd:NF041483 426 DDTKEYRAKTVELQEEARRLR---------------------GEAEQLRaEAVAEGERIRGEARREA----VQQIEEAAR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2482 QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQ 2561
Cdd:NF041483 481 TAEELLTKAKADADELRSTATAESERVRTEAIERATTLRR-QAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELR 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2562 REAEEGVRRKQEELqhleqqrqqqekllAEENQRLR----ERLQRLEEEHRAALAHSEIATTQAA 2622
Cdd:NF041483 560 EETERAIAARQAEA--------------AEELTRLHteaeERLTAAEEALADARAEAERIRREAA 610
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1826-2048 |
1.98e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1826 AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEErLAQLRKASE 1905
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1906 SELERQKGLVEDTLRQR-RQVEEEIMALKVSFEKAAAGKAELEL--ELGRIRSNAEDTMRsKEQAELEAARQRQLAAEEE 1982
Cdd:COG4942 97 AELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELR-ADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1983 QRRREAEERVQRSLAAEEEAARQRKVALEEvERLKAKVEEARRLRERAEQESARQLQLAQEAAQKR 2048
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLE-KELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1420-1755 |
2.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1420 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1499
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1500 RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVE 1579
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1580 LQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1659
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1660 AQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1739
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*.
gi 254675119 1740 RLQHEATAATQKRQEL 1755
Cdd:COG4372 324 LAKKLELALAILLAEL 339
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
71-146 |
2.06e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.28 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 71 LYEDLRDGHNLISLLEvlsgDSLP-------------REKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 137
Cdd:cd21294 38 LFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113
|
....*....
gi 254675119 138 TLGLIWTII 146
Cdd:cd21294 114 ILGLIWQII 122
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1680-1820 |
2.09e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 43.43 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA-- 1757
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 1758 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1820
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1683-1826 |
2.12e-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: 44.22 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1683 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1762
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675119 1763 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1826
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2767-2803 |
2.12e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|....*..
gi 254675119 2767 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2803
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1344-1514 |
2.16e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.12 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1344 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1423
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPE-AAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1424 LQHLRQSSEAEIQAKAQQVEAAERSRMRieeeiRVVRLQLETTERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRR 1503
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 254675119 1504 QVQDESQRKRQ 1514
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2275-2474 |
2.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2275 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE- 2353
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2354 ----QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2429
Cdd:COG4717 128 lplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254675119 2430 vtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLK 2474
Cdd:COG4717 208 ---LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1477-1576 |
2.20e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1477 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEsQRKRQAEAElALRVKAEAEAAREKQRALQALDelrlqaEEAERR 1553
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 254675119 1554 LRQAEAERARQVQVALETAQRSA 1576
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
44-146 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 44 QKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALD 113
Cdd:cd21292 25 EKVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALN 102
|
90 100 110
....*....|....*....|....*....|...
gi 254675119 114 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 146
Cdd:cd21292 103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2268-2406 |
2.47e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2268 LEEEA------EKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQ 2337
Cdd:PTZ00491 675 LEQEArgrlerQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAE 751
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 2338 KELAQEQARRLQEDKEQmaQQLVEetqgfqrtLEAERQRQLeMSAEAERLKLRMAEMSR----AQARAEEDAQ 2406
Cdd:PTZ00491 752 AELEKLRKRQELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2401-2525 |
2.65e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2401 AEEDAQRFRKQAEEigeklhRTELATQEKVTLVQTlEIQRQQSDHDAErLREAIAELEREKEKLKQEAKLLQLKSEEMQt 2480
Cdd:PRK12704 36 AEEEAKRILEEAKK------EAEAIKKEALLEAKE-EIHKLRNEFEKE-LRERRNELQKLEKRLLQKEENLDRKLELLE- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 254675119 2481 vQQEQILQEtqalqksflsEKDSLLQRERFIEQEKAKLEQLFQDE 2525
Cdd:PRK12704 107 -KREEELEK----------KEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1633-1895 |
2.66e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1633 LERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR-----RGKAEEQAVRQRELAEQELEKQRQLAEGTA 1707
Cdd:pfam13868 65 EERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERiqeedQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1708 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsEKS 1787
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE-----RKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1788 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLT------EKLAAISEATRLKTEAEIALKEK 1861
Cdd:pfam13868 220 RQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRkqaedeEIEQEEAEKRRMKRLEHRRELEK 297
|
250 260 270
....*....|....*....|....*....|....*.
gi 254675119 1862 EAENERLRRLAEDEAF--QRRRLEEQAALHKADIEE 1895
Cdd:pfam13868 298 QIEEREEQRAAEREEEleEGERLREEEAERRERIEE 333
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1690-1886 |
2.94e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.21 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1690 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEV 1768
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1769 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAER----VLTEK 1840
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKlrnqLTSKS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254675119 1841 LAAISEA---TRLKTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQA 1886
Cdd:pfam09787 160 QSSSSQSeleNRLHQLTE-TLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1372-1503 |
2.95e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1372 EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKAQQVEAAERSR 1449
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1450 MRIEEEIRVVRLQLETTERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1503
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
524-618 |
2.97e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 524 LRYLQDLLAWVEENQRRIDSAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQL---SPATRGAYRDCLGRLD 600
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 254675119 601 LQYAKLLNSSKARLRSLE 618
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2258-2431 |
3.47e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2258 LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2337
Cdd:pfam05262 177 ISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2338 KELAQEQAR--------RLQEDKEQMAQQLVEETQgfQRTLEAERQRQlemsAEAERLKLRMAEMSRAQARAEEDAQRFR 2409
Cdd:pfam05262 257 AKNLPKPADtsspkedkQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|..
gi 254675119 2410 kqaEEIGEKLHRTELATQEKVT 2431
Cdd:pfam05262 331 ---EPVAEDLQKTKPQVEAQPT 349
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2161-2434 |
3.57e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2161 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVR 2236
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2237 VQMEELGKL-----KARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRAL 2309
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2310 AEKMLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDK--EQMAQQLVEETQGFQRTLEAERQRQLEMSAEAER 2386
Cdd:pfam13868 213 EEQERKERQKEREEAeKKARQRQELQQAREEQIELKERRLAEEAerEEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 254675119 2387 LKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2434
Cdd:pfam13868 293 RELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2240-2357 |
3.70e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2240 EELGKLKARIEAENRALILRDKDNTQrfLEEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2319
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675119 2320 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2357
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2295-2469 |
3.72e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2295 LRQLAEEDLAQQRALAEKMLKEkmqavqeatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAER 2374
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2375 QRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAI 2454
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEA 171
|
170
....*....|....*.
gi 254675119 2455 AELEREKEKL-KQEAK 2469
Cdd:PRK12704 172 AVLIKEIEEEaKEEAD 187
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1462-1925 |
3.78e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1462 QLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR--VKAEAEAAREKQRALQA 1539
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1540 LDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehVTVAQLREEAERRAQQQ 1619
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA--RAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1620 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1699
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1700 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1779
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1780 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1859
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1860 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 1925
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1339-1440 |
3.89e-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: 42.67 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1339 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAKA-----QAELEAQELQRRMQE-----EV 1403
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEVakiqmQQKIMEKEAEKKISEiedemHL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675119 1404 ArREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAQ 1440
Cdd:cd03406 237 A-REKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1341-1468 |
3.92e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQEL-QRRMQEEVARREEAAVDAQQQKR 1418
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675119 1419 SIQEELQHLRQSSEAeiqAKAQQVEAAErsRMRIEEEIRVVRLQLETTER 1468
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAE--RQRQEREKIMQQEEQERLER 135
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1685-2042 |
3.97e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1685 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--HEATAATQKRQELEA 1757
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1758 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLR--------ALAEEAKRQRQLAEEDAARQ 1829
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKsqladyqqALDVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1830 RAE------------AERVLTEKLAAISEATRLKTEAEIALKEKEAENER-------LRRLAED----EAFQR-----RR 1881
Cdd:PRK04863 425 RAKqlcglpdltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlVRKIAGEvsrsEAWDVarellRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1882 LEEQAALhkadiEERLAQLRkASESELERQkglvedtLRQRRQVEEeimaLKVSFEKAAAGKAELELELGRIRSNAEDTM 1961
Cdd:PRK04863 505 LREQRHL-----AEQLQQLR-MRLSELEQR-------LRQQQRAER----LLAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1962 RSKEQaELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE-------------------VERLKAKVEE 2022
Cdd:PRK04863 568 ESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeefedsqdvteymqqlLERERELTVE 646
|
410 420
....*....|....*....|
gi 254675119 2023 ARRLRERAEQESARQLQLAQ 2042
Cdd:PRK04863 647 RDELAARKQALDEEIERLSQ 666
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3021-3058 |
4.03e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.69 E-value: 4.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 254675119 3021 LRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVAVAL 3058
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1430-1564 |
4.05e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1430 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDES 1509
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 1510 QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1564
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1228-1556 |
4.16e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1228 AKRRQEQIQAVpIANCQAAREQLRQE-KALLEEIERHGEKVEECQKfakQYINAIKdyelQLITYKAQLEPVASPAkkpk 1306
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELKD---KYRELRK----TLLANRFSYGPAIDEL---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1307 vqsgsESVIQEYVDLRTRYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1385
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1386 AQ--------AELEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKA----------QQVEAAE 1446
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKKyveknlpeieDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1447 RSRMRIEEEIRVV----RLQLETTERQRgGAEGELQALRARAEEAE---AQKRQA----QEEAERLRRQVQD-ESQRKRQ 1514
Cdd:pfam06160 305 EQNKELKEELERVqqsyTLNENELERVR-GLEKQLEELEKRYDEIVerlEEKEVAyselQEELEEILEQLEEiEEEQEEF 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 254675119 1515 AEAELALRvkaeaeaaREKQRALQALDELRLQAEEAERRLRQ 1556
Cdd:pfam06160 384 KESLQSLR--------KDELEAREKLDEFKLELREIKRLVEK 417
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1680-1837 |
4.16e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1680 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEATAATQKRQELEA 1757
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1758 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1833
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....
gi 254675119 1834 ERVL 1837
Cdd:COG1842 207 EDEL 210
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1391-1529 |
4.28e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1391 EAQELQRRMqEEVARREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1470
Cdd:COG0542 412 ELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1471 GGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEAELALRVKAEAEA 1529
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1341-1525 |
4.28e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEEER---LAEQQRAEererLAEVEAALEKQRQlaEAHAQAKAQAELE-----AQELQRRMQEEVARREEAAVD 1412
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE----LDASRALAEKQKH--ELDTEKRCAEELKeamqmAMEGHARMLEQYADLEEKHIQ 1125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1413 AQQQKRSIQEELQHLRQSSE------AE---IQAKAQQVEA----AERSRMRIEEEIRVVRLQLETTER--QRGG----- 1472
Cdd:PLN03188 1126 LLARHRRIQEGIDDVKKAAAragvrgAEskfINALAAEISAlkveREKERRYLRDENKSLQAQLRDTAEavQAAGellvr 1205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1473 ---AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1525
Cdd:PLN03188 1206 lkeAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1378-1566 |
4.33e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1378 AEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIR 1457
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1458 vvRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAE-AELALRVKAEAEAAREKQRA 1536
Cdd:PRK12678 147 --EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG--RREERGRDGDdRDRRDRREQGDRREERGRRD 222
|
170 180 190
....*....|....*....|....*....|
gi 254675119 1537 LQALDELRLQAEEAERRLRQAEAERARQVQ 1566
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1026-1555 |
4.41e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1026 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRSTQGAEE 1105
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1106 VLKTHEEQLKEAQAVPATLQELEATKASLkklraQAEAQQpVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQ 1185
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1186 LLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLSAWLQDAKRRQEQiqavpIANCQAAREQLRQEKALLEE 1259
Cdd:pfam05557 144 LKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELAR-----IPELEKELERLREHNKHLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1260 IERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSEL---------- 1328
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDLSRRIEQLqqreivlkee 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1329 -TTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL----------------------AEAHAQA 1384
Cdd:pfam05557 299 nSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgyrailesydkeltMSNYSPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1385 KAQAELEAQELQRRMQ---EEVARR----EEAAVDAQQQKRSIQEELQHLRQ--------SSEAEIQAKAQQVEAAERSR 1449
Cdd:pfam05557 378 LLERIEEAEDMTQKMQahnEEMEAQlsvaEEELGGYKQQAQTLERELQALRQqesladpsYSKEEVDSLRRKLETLELER 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1450 MRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DESQRKRQAEAELALRVKAEA 1527
Cdd:pfam05557 458 QRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKRLLKKLEDDLEQVLRLPETT 537
|
570 580
....*....|....*....|....*...
gi 254675119 1528 EAAREKQralqaLDELRLQAEEAERRLR 1555
Cdd:pfam05557 538 STMNFKE-----VLDLRKELESAELKNQ 560
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1386-1765 |
4.48e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1386 AQAELEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQl 1463
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1464 ETTERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREkqralqalDEL 1543
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS--------TEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1544 RLQAEEAErrlrqaeaerarqvqvalETAQRSAEVELQSKRASFAEKTaQLERTLQEEHVTVAQLREEAERRAQQQAEAE 1623
Cdd:pfam02029 150 RQAEEEGE------------------EEEDKSEEAEEVPTENFAKEEV-KDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1624 RAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQadaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQla 1703
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ------------------KLEELRRRRQEKESEEFEKLRQ-- 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 1704 egtAQQRLAAEQELIRLRAEteqgEQQRQLLEEELARLQHEATAATQKRQE---LEAELAKVRAE 1765
Cdd:pfam02029 271 ---KQQEAELELEELKKKRE----ERRKLLEEEEQRRKQEEAERKLREEEEkrrMKEEIERRRAE 328
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1151-1519 |
4.63e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1151 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLgrqLRYYRESADPLSAWLQDAKR 1230
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1231 RQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKV-------EECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK 1303
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1304 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSqyiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAH 1381
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQ---KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1382 AQAKAQAELEAQELQrrMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEiRVVRL 1461
Cdd:pfam07888 266 QRDRTQAELHQARLQ--AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675119 1462 QLETT-ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1519
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2293-2468 |
4.89e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2293 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLVEETQG 2365
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2366 FQRTLEAERQRQLemsaeAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2445
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 254675119 2446 DAERLREAIAELEREKEKLKQEA 2468
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2234-2414 |
5.03e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2234 SVRVQMEE----LGKLKARIEAENRA-LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEED 2302
Cdd:PRK11637 62 SVRQQQQQraslLAQLKKQEEAISQAsRKLRETQNTLNQLNKQIDELNasiaklEQQQAAQERLLAAQLDAAFRQGEHTG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2303 LAQQRALAEKMLKEKMQA----VQEAtRLKAEAELLQQQKELAQEqaRRLQEDKEQMAQQLVEETQGFQRTLE---AERQ 2375
Cdd:PRK11637 142 LQLILSGEESQRGERILAyfgyLNQA-RQETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEqarNERK 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675119 2376 RQL---------------EMSAEAERLKLRMAEMSR-AQARAEE---DAQRFRKQAEE 2414
Cdd:PRK11637 219 KTLtglesslqkdqqqlsELRANESRLRDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3426-3457 |
5.10e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.10e-03
10 20 30
....*....|....*....|....*....|..
gi 254675119 3426 KLLSAEKAVTGYKDPYSGNTISLFQAMKKGLV 3457
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2265-2477 |
5.21e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2265 QRFleeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQ 2344
Cdd:PRK05035 453 ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAARE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2345 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQR-------QLEMSAEAE-----RLKLRMAEMSRAQAR-AEEDAQRFRKQ 2411
Cdd:PRK05035 525 ARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaQQAANAEAEeevdpKKAAVAAAIARAKAKkAAQQAASAEPE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 2412 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEE 2477
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1341-1445 |
5.36e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1341 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDA----- 1413
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVlqewe 148
|
90 100 110
....*....|....*....|....*....|....*
gi 254675119 1414 ---QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA 1445
Cdd:pfam13904 149 rkkLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1474-1667 |
5.72e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1474 EGELQALRARAEEAEAQKRQAQEEAERLRRQvqdESQRKRQAEAELALRVKAEAEAAREKQRAlqaldELRLQAEEAERR 1553
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQERLKQLEKERLAAQ---EQKKQAEEAAKQAALKQKQAEEAAAKAAA-----AAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1554 LrqaeAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAReeaerel 1633
Cdd:PRK09510 156 A----AAAAKK---AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA------- 221
|
170 180 190
....*....|....*....|....*....|....
gi 254675119 1634 ERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQ 1667
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2439-2661 |
5.83e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2439 QRQQSDH----DAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQEtqalQKSFLSEKDSLLQRERfIEQE 2514
Cdd:pfam17380 286 ERQQQEKfekmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAE----QERMAMERERELERIR-QEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2515 KAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQ 2594
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 2595 RLRE----RLQRLEEEHRAALAHSEIATTQAASTKALPNGRDApdgpsvEAEPEYTFEGLRQKVPAQQLQE 2661
Cdd:pfam17380 439 RLEEerarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEK------EKRDRKRAEEQRRKILEKELEE 503
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2335-2469 |
6.13e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2335 QQQKELAQEQARRLQEDKEQMAQQLVEETQgfQRTLEAERQRQLEMSAEAERLKLRMAEMSR------AQARAEEDAQRF 2408
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2409 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLKQEAK 2469
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1814-1975 |
6.70e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1814 EAKRQRQLAEEDAARQRAEAERvLTEKlaAISEATRLKTEAEIA-------LKEKEAENERLRRLAEdeafQRRRLEEQA 1886
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAEAER-ETEI--AIAQANREAEEAELEqereietARIAEAEAELAKKKAE----ERREAETAR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1887 ALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELElgrirsnaedtmrskEQ 1966
Cdd:COG2268 262 AEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE---------------AE 326
|
....*....
gi 254675119 1967 AELEAARQR 1975
Cdd:COG2268 327 AEAEAIRAK 335
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1358-1533 |
6.76e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1358 AEERERLAEVEAalekQRQLAEAHAQAKA---QAELEAQELQRRMQEEvarreeaavdAQQQKRSIQEELQHLrqssEAE 1434
Cdd:PRK12704 29 AEAKIKEAEEEA----KRILEEAKKEAEAikkEALLEAKEEIHKLRNE----------FEKELRERRNELQKL----EKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1435 IQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERqrggaegELQALRARAEEAEAQKRQA--------QEEA-ERLRRQV 1505
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKV 163
|
170 180
....*....|....*....|....*...
gi 254675119 1506 QDEsqrkrqAEAELALRVKAEAEAAREK 1533
Cdd:PRK12704 164 EEE------ARHEAAVLIKEIEEEAKEE 185
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
50-145 |
6.77e-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: 39.20 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 50 KWVNKHLikhWRAEAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN- 124
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYf 91
|
90 100
....*....|....*....|.
gi 254675119 125 IRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21218 92 LTPEDIVSGNPRLNLAFVATL 112
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1443-1560 |
6.87e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1443 EAAERSRMRIE---EEIRVVRLQLETTERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDESQRKRQAEAel 1519
Cdd:COG0542 397 EAAARVRMEIDskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA-- 461
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675119 1520 alRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAE 1560
Cdd:COG0542 462 --RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1485-1602 |
6.88e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1485 EEAeaqKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1564
Cdd:PRK00409 505 EEA---KKLIGEDKEKLNELIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110
....*....|....*....|....*....|....*....
gi 254675119 1565 VQVALETAQRSAEVELQSKRASFAEKTAQL-ERTLQEEH 1602
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVkAHELIEAR 613
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2342-2530 |
6.89e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.18 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2342 QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigEKLHR 2421
Cdd:pfam15665 13 EAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE--RELKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2422 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKL-LQLKSEEMQTVQQEQ---ILQETQALQKSF 2497
Cdd:pfam15665 91 EAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAkHRQEIQELLTTQRAQsasSLAEQEKLEELH 170
|
170 180 190
....*....|....*....|....*....|...
gi 254675119 2498 LSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAK 2530
Cdd:pfam15665 171 KAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQ 203
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1355-1549 |
7.10e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1355 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE 1434
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1435 IQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKR 1513
Cdd:PRK07735 156 EEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSgDEDA 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 254675119 1514 QAEAELALRVKAEAeAAREKQRALQALDELRLQAEE 1549
Cdd:PRK07735 236 KAKAIAAAKAKAAA-AARAKTKGAEGKKEEEPKQEE 270
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1347-1608 |
7.16e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1347 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEE-------VARREEAAVDAQQQKRS 1419
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1420 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEI--RVVRLQLETTE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1496
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1497 EAERLRRQV-QDESQRKRQAEAELALRVKAEAEAAREK-------QRALQALDELRLQAEEAERRLRQAEAERARQVQVa 1568
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVF- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 254675119 1569 LETAQRSAEVElQSKRASFAEKTAQLERTLQEEHVTVAQL 1608
Cdd:pfam02029 244 LEAEQKLEELR-RRRQEKESEEFEKLRQKQQEAELELEEL 282
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1886-2062 |
7.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1886 AALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKE 1965
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1966 QAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL-----------EEVERLKAKVEEARRLRERAEQES 2034
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAER 173
|
170 180 190
....*....|....*....|....*....|
gi 254675119 2035 ARQLQL--AQEAAQKRLQAEEKAHAFVVQQ 2062
Cdd:COG4942 174 AELEALlaELEEERAALEALKAERQKLLAR 203
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2181-2507 |
7.58e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.59 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2181 RQKAQVEQELTTLRLQ-LEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVrVQMEE---LGKLKARIEAEN-RA 2255
Cdd:pfam15964 285 QHEAVLAQTHTNVHMQtIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQA-VQMTEeanFEKTKALIQCEQlKS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2256 LILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELL 2334
Cdd:pfam15964 364 ELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2335 QQQKELAQEQAR-RLQEDKEQMAQqlvEETQGFQRTLEAERQRQLEMS-AEAERLKL-------RMAEMSRAQARAEEDA 2405
Cdd:pfam15964 442 SQEMDVTKVCGEmRYQLNQTKMKK---DEAEKEHREYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREEC 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2406 QRFrkqAEEIGEKLHRTELATQEKVTLVQ--------------------TLEIQRQQSDHDaERLREAIAELEREK---E 2462
Cdd:pfam15964 519 LKL---TELLGESEHQLHLTRLEKESIQQsfsneakaqalqaqqreqelTQKMQQMEAQHD-KTVNEQYSLLTSQNtfiA 594
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 254675119 2463 KLKQEAKLLQLKSEEMQTVQQEQILQETQalQKSFLSEKDSLLQR 2507
Cdd:pfam15964 595 KLKEECCTLAKKLEEITQKSRSEVEQLSQ--EKEYLQDRLEKLQK 637
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1209-1421 |
7.84e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1209 RQLRYYRESADPLSAWLQD-AKRRQEQIQAVpiancQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINA---IKDY 1284
Cdd:COG3206 164 QNLELRREEARKALEFLEEqLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1285 ELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQR 1357
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675119 1358 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEE-------VARREEAAVDAQQQKRSIQ 1421
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
43-149 |
8.00e-03 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 39.32 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 43 VQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHR 118
Cdd:cd21306 16 VVKKSLITFVNKHLNK-----LNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDA 90
|
90 100 110
....*....|....*....|....*....|.
gi 254675119 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21306 91 GLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1428-1607 |
8.03e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1428 RQSSEAEIQAKAQQVEA-AERSRMRIE-EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1505
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1506 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSK-- 1583
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTei 212
|
170 180
....*....|....*....|....
gi 254675119 1584 RASFAEKTAQLERTLQEEHVTVAQ 1607
Cdd:pfam00529 213 RAPVDGTVAFLSVTVDGGTVSAGL 236
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2159-2623 |
8.09e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2159 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTtlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVE-----EELF 2233
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2234 SVRVQMEELgklKARIEAENRALILRDkDNTQRFLE---EEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2310
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLEmlqSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2311 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLVEETQGFQRTLEaerqrqLEMSAEAERLKlr 2390
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQMLKTNGL------LHTEDREEEIK-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2391 maemsraQARAEEDAQRFRK-QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAK 2469
Cdd:pfam10174 276 -------QMEVYKSHSKFMKnKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2470 LLQLKSEEMQTV-----QQEQILQETQALQKSFLSE-KDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQM 2543
Cdd:pfam10174 349 ALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2544 EQEKQE--LMASMEEARRrqrEAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLE----EEHRAALAHSEIA 2617
Cdd:pfam10174 429 TDSSNTdtALTTLEEALS---EKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQpeltEKESSLIDLKEHA 505
|
....*.
gi 254675119 2618 TTQAAS 2623
Cdd:pfam10174 506 SSLASS 511
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1530-1584 |
8.37e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675119 1530 AREKQRALQaldelRLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1584
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1320-1592 |
8.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1320 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELE---AQELQ 1396
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1397 RRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSS----------EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETT 1466
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRkqleaqiaelQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1467 ERQRggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQ 1546
Cdd:COG4372 177 SEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 254675119 1547 AEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1592
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1753-1938 |
8.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1753 QELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1832
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDE------------------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1833 AERvLTEKLAAISEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQK 1912
Cdd:COG1579 75 IKK-YEEQLGNVRNNKEYE-----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....*.
gi 254675119 1913 GLVEDTLRQRRQVEEEIMALKVSFEK 1938
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1786-1934 |
8.88e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1786 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LTEKLAAisEATRLKTE 1853
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1854 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALK 1933
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
.
gi 254675119 1934 V 1934
Cdd:PRK12705 181 I 181
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1432-1770 |
8.94e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1432 EAEIQAKaQQVEAAERSRMR--IEEEIRVVRLQLETTERQRGGAEGELqalraraeeaeaqkRQAQEEAERLRRQVQDES 1509
Cdd:pfam00038 31 ETKISEL-RQKKGAEPSRLYslYEKEIEDLRRQLDTLTVERARLQLEL--------------DNLRLAAEDFRQKYEDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1510 QRKRQAEAELAL--RVKAEAEAAR-EKQRALQAL-DELRLqaeeaerrLRQAEAERARQVQVALETAQRSAEVElqskra 1585
Cdd:pfam00038 96 NLRTSAENDLVGlrKDLDEATLARvDLEAKIESLkEELAF--------LKKNHEEEVRELQAQVSDTQVNVEMD------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1586 sfAEKTAQLERTLQEehvtvaqlreeaerraqqqaeaerareeaerelerwqlkanealrLRLQAEEVAQqKSLAQAdae 1665
Cdd:pfam00038 162 --AARKLDLTSALAE---------------------------------------------IRAQYEEIAA-KNREEA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1666 kqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA----RL 1741
Cdd:pfam00038 191 ----------------EEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAeteeRY 254
|
330 340
....*....|....*....|....*....
gi 254675119 1742 QHEATAATQKRQELEAELAKVRAEMEVLL 1770
Cdd:pfam00038 255 ELQLADYQELISELEAELQETRQEMARQL 283
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1183-1460 |
8.94e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1183 VTQLLERWQAVLAQTDVRQRELEQLGRQLryyrESADplsAWLQDAkrrQEQIQAVPIANCQAAREQLrqEKALLEEIER 1262
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQL----AQAP---AKLRQA---QAELEALKDDNDEETRETL--STLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1263 hgeKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFISET 1342
Cdd:PRK11281 129 ---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1343 LR-RMEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAELEAQELQ------RRMQ-EEVARREEAAV 1411
Cdd:PRK11281 193 QRvLLQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQeainskRLTLsEKTVQEAQSQD 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675119 1412 DAQQQKRS--IQEELQHLRQSSEAEIQAKA-------------QQVEAAERSRMRIEEEIRVVR 1460
Cdd:PRK11281 270 EAARIQANplVAQELEINLQLSQRLLKATEklntltqqnlrvkNWLDRLTQSERNIKEQISVLK 333
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1681-1781 |
9.16e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1681 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1760
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 254675119 1761 KvRAEMEVLLaskarAEEESR 1781
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2181-2359 |
9.20e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2181 RQKAQVEQELTTlRLQLEETDHQKSIlDEELQRLKAEVTEAARQRSQVEeelfsVRVQMEELGKLKARIEAENRALILR- 2259
Cdd:COG2268 201 ARIAEAEAERET-EIAIAQANREAEE-AELEQEREIETARIAEAEAELA-----KKKAEERREAETARAEAEAAYEIAEa 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2260 --DKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA-RLRQLAEEDLAQQRALAE-KMLKEKMQAVQEATRLKAEAELLQ 2335
Cdd:COG2268 274 naEREVQRQLEIAEREREIELQEKEAEREEAELEADvRKPAEAEKQAAEAEAEAEaEAIRAKGLAEAEGKRALAEAWNKL 353
|
170 180
....*....|....*....|....
gi 254675119 2336 QQKELAQEQARRLQEDKEQMAQQL 2359
Cdd:COG2268 354 GDAAILLMLIEKLPEIAEAAAKPL 377
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1411-1557 |
9.32e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1411 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ 1490
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675119 1491 KRQAQEEAERLRRQVQdesqrkrQAEAElalrvkaeaEAAREKQRALQALDELRLqaEEAERR------LRQA 1557
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4282-4312 |
9.50e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.50e-03
10 20 30
....*....|....*....|....*....|.
gi 254675119 4282 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4312
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1371-1535 |
9.59e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1371 LEKQRQLAEAHAQAKAQAELEAQELQRRMQEEvaRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrm 1450
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 1451 rieeeirvvrlqLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE---SQRKRQAEAELALRVKAEA 1527
Cdd:PRK12705 100 ------------LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKlllKLLDAELEEEKAQRVKKIE 167
|
....*...
gi 254675119 1528 EAAREKQR 1535
Cdd:PRK12705 168 EEADLEAE 175
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2350-2486 |
9.80e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675119 2350 EDKEQMAQQLVEETQgfqRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigeklhrtELAT--- 2426
Cdd:COG1842 22 EDPEKMLDQAIRDME---EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE--------DLAReal 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675119 2427 QEKVTL---VQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLL--QLKSEEMQTVQQEQI 2486
Cdd:COG1842 91 ERKAELeaqAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEAL 155
|
|
| |
