|
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 ... |
41-145 |
3.93e-76 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 248.47 E-value: 3.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 41 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 120
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1920237974 121 RNDDIADGNPKLTLGLIWTIILHFQ 145
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
38-156 |
1.58e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 241.47 E-value: 1.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 117
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237974 118 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 156
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
34-154 |
9.86e-73 |
|
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: 239.50 E-value: 9.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 34 EGKKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHR 113
Cdd:cd21236 8 ERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237974 114 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 154
Cdd:cd21236 88 QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
158-263 |
1.08e-69 |
|
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: 229.91 E-value: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 158 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1920237974 238 PEDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
159-263 |
3.69e-64 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 214.18 E-value: 3.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1920237974 239 EDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
38-155 |
3.76e-63 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 211.81 E-value: 3.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 117
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237974 118 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 155
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
159-263 |
1.43e-56 |
|
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: 192.51 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1920237974 239 EDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
43-146 |
1.19e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 175.65 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 43 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 121
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1920237974 122 NDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
157-263 |
6.25e-50 |
|
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: 173.30 E-value: 6.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 157 DMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 236
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1920237974 237 DPEDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
38-142 |
1.78e-47 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 166.77 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1920237974 117 LVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
159-259 |
6.66e-45 |
|
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: 159.11 E-value: 6.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1920237974 239 EDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
42-370 |
1.15e-44 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 174.36 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 42 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGCQ-GLRCDNFTTSWRDGRLFNAII 197
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 198 HRHKPTLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 264
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 265 VPDVQDGVKANElQLRwQEYRELVLLLLQWIRAHTAGFEERRFPSSFEEIEILWCQFLKFKETE--LPAKEAD-KNRSKG 341
Cdd:COG5069 245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
|
330 340
....*....|....*....|....*....
gi 1920237974 342 IYQSLEgAVQAGQLKVPPGYHPLDVEKEW 370
Cdd:COG5069 323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
39-146 |
3.47e-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: 3.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 114
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1920237974 115 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
37-142 |
8.60e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 156.30 E-value: 8.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 37 KDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLrHRQV 115
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 1920237974 116 KLVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
39-146 |
1.08e-43 |
|
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: 155.81 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 111
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237974 112 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
159-259 |
4.63e-43 |
|
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: 153.71 E-value: 4.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237974 239 EDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
158-263 |
5.51e-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: 5.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 158 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1920237974 238 PEDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
146-261 |
8.63e-40 |
|
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: 144.81 E-value: 8.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237974 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
38-142 |
9.69e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 145.55 E-value: 9.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 1920237974 117 LVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
37-142 |
1.06e-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: 142.50 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 37 KDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQV 115
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKV 104
|
90 100
....*....|....*....|....*..
gi 1920237974 116 KLVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21317 105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
41-142 |
1.12e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 141.37 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 41 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 119
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1920237974 120 IRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
39-146 |
1.65e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 141.12 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1920237974 117 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
43-144 |
1.89e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 43 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 120
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1920237974 121 RNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1302-1877 |
1.14e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 156.64 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1302 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEErERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1381
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-AELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1382 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQA 1461
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1462 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1541
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1542 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaEAERARAEAERELERWQLK 1621
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--------AGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1622 ANEALRLRLQAeevAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1701
Cdd:COG1196 536 YEAALEAALAA---ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1702 LRAETEQGEqqrqLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1781
Cdd:COG1196 613 ARYYVLGDT----LLGRTLVAARLEAALRR--AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1782 ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1861
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|....*.
gi 1920237974 1862 RLLEEQAAQHKADIEA 1877
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
155-259 |
2.06e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 138.27 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 155 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 234
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1920237974 235 LLDPEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
155-259 |
4.47e-37 |
|
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: 137.06 E-value: 4.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 155 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 234
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1920237974 235 LLDPEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
38-146 |
9.87e-37 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 135.82 E-value: 9.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1920237974 117 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1330-2035 |
1.03e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.53 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1330 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiqEELQHL 1409
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1410 RQSSEAEIQAKARQVEAAERSRlRIEEEIRVVRLQlEATERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1489
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1490 ETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF 1569
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1570 AEKTAQ-LERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAlrlRLQAEEVAQQKSLTQaeaek 1648
Cdd:PTZ00121 1327 AKKKADaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA---KKKAEEKKKADEAKK----- 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1649 qkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQLLE-----EELAR 1722
Cdd:PTZ00121 1399 -------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEeakkaEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1723 LQREAAAATQKRRELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAK 1798
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1799 RQRQLAEEDAVRQRAEAERvlAEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1878
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1879 LAQLRKASESELERQKGLVEDTLRQRrqveEEILALKGSFEKAAAGKAELELELGRIRGT-----AEDTLRSKEQA--EQ 1951
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakkAEEDKKKAEEAkkAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1952 EAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQEAA 2027
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
....*...
gi 1920237974 2028 QKRLQAEE 2035
Cdd:PTZ00121 1765 EEEKKAEE 1772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1335-1936 |
1.65e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.78 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1335 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAQGLQrrmqeevarreevaveAQEQKRSIQEELQHLRQSs 1413
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELK----------------EELKELEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1414 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR 1493
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1494 KRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEAELQSEHASFAEKT 1573
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1574 AQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEA 1653
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1654 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR------LRAETEQGEQQRQLLEEELARLQREA 1727
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavlIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1728 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1807
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1808 AVRQRAEAERVLAEKLAA--ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKA 1885
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1886 SESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1936
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
158-259 |
1.12e-35 |
|
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: 132.68 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 158 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1920237974 238 PEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1462-2062 |
3.64e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.55 E-value: 3.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1462 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQR---KRQAE-AELALRVQAEAEAaREKQRALQALEELRLQAEEAER 1534
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLeplERQAEkAERYRELKEELKE-LEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1535 RLRQAEAERARqvqvaLETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERE 1614
Cdd:COG1196 247 ELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1615 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1694
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---------AELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1695 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1774
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1775 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA----AISEATRLKTEAEIALKEKEAENERL 1850
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1851 RRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELEL 1930
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1931 ELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2010
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2011 RAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLER 2062
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
162-263 |
1.22e-34 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 129.47 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 162 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237974 241 VDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
143-259 |
1.53e-34 |
|
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: 130.56 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 143 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQA 222
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237974 223 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1665-2233 |
2.81e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.46 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1744
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1745 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLA 1824
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1825 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKgLVEDTLRQR 1904
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1905 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 1984
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1985 ARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQEQSV 2059
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2060 LERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQA 2139
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2140 ALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV 2219
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570
....*....|....
gi 1920237974 2220 QMEELGKLKARIEA 2233
Cdd:COG1196 765 LERELERLEREIEA 778
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
42-147 |
8.79e-34 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 127.95 E-value: 8.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 118
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
43-146 |
6.89e-33 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 124.71 E-value: 6.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 43 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 120
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1920237974 121 RNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
43-146 |
1.71e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 123.58 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 43 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 121
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1920237974 122 NDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
159-259 |
5.65e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 122.13 E-value: 5.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237974 239 EDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
38-142 |
6.89e-32 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 123.62 E-value: 6.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 1920237974 117 LVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
158-256 |
3.98e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 119.84 E-value: 3.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 158 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1920237974 238 PEDVDVPQPDEKSIITYVS 256
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1323-1927 |
1.19e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.50 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQRAE------------ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1390
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEavkkaeeakkdaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1391 V--AVEAQ--EQKRSIQEELQHLRQSSEAEiQAKARQVEA---AERSRLRIEEEirvvRLQLEATERQRGGAEGELQALR 1463
Cdd:PTZ00121 1289 KkkADEAKkaEEKKKADEAKKKAEEAKKAD-EAKKKAEEAkkkADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1464 ARAEEAEAQKRQAQEEAERLRRQVQ-----DETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRlQAEEAERRLRQ 1538
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1539 A--------EAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLR--EEATRRAQQQAEAERAR 1608
Cdd:PTZ00121 1443 AkkadeakkKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1609 AEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKQKEEAEREARRRgKAEEqavrQRELAEQELEKQRQLAEGT 1688
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKK----AEEKKKADELKKAEELKKAEEKKKAEEAK-KAEE----DKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1689 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1768
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1769 SKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEedaVRQRAEAERVLAEKLAAISEATRLKteAEIALKEKEAENE 1848
Cdd:PTZ00121 1674 KKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEE---LKKKEAEEKKKAEELKKAEEENKIK--AEEAKKEAEEDKK 1744
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1849 RLRRLAEDEAFQRRLleeqaAQHKADIEARLAQLRKASESELErqKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAE 1927
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKI-----AHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
146-261 |
1.60e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.40 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 146 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237974 226 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 261
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
158-256 |
1.64e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 158 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1920237974 238 PEDVDVPQPDEKSIITYVS 256
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
162-263 |
1.80e-30 |
|
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: 117.75 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 162 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237974 241 VDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1323-1955 |
1.85e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.11 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAEREAQGLQR----------RMQEEVARREE 1390
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedakkaeavKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1391 VAVEAQEQKRSIQ-EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRAR-AEE 1468
Cdd:PTZ00121 1241 EAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1469 AEAQKRQAQEEAERLRRQVQdETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAERRlrqaeAERARQV 1547
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK-----AEEKKKA 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1548 QVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARaeaerelerwqlKANEALR 1627
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------------EAKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1628 LRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELiRLRAETE 1707
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-KKADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1708 QGEQQR---QLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaEAGRFRELA 1784
Cdd:PTZ00121 1541 KAEEKKkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAK 1619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1785 EEAARLRALAEEAKRQRQLAEEDA--------VRQRAEAERVLAEKLAAISEATrlKTEAEIALKEKEAENERLRRLAED 1856
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKE 1697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1857 EAFQRRLleEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVeEEILALKGSFEKAAAGKAELELELGRIR 1936
Cdd:PTZ00121 1698 AEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
650
....*....|....*....
gi 1920237974 1937 GTAEDTLRSKEQAEQEAAR 1955
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRR 1793
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
39-148 |
2.48e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.68 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 114
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1920237974 115 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 148
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
878-955 |
4.18e-30 |
|
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: 115.78 E-value: 4.18e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 878 LAWQSLGRDMQLIRSWSLATFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 955
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
42-144 |
5.92e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 116.43 E-value: 5.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1732-2443 |
1.30e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.44 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1732 QKRRELEAELAKVRAEMEvllaskaRAEEEsrsTSEKSKQ--RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedav 1809
Cdd:COG1196 172 ERKEEAERKLEATEENLE-------RLEDI---LGELERQlePLERQA----EKAERYRELKEELKELEAELLLLK---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1810 RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadiEARLAQLRKASESE 1889
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL------LAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1890 LERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1969
Cdd:COG1196 308 EERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1970 AEERVQKSLAAEEEAARQRKAALEEVERLKAkvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQEL 2049
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2050 QQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2129
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2130 AARRAQAEQAALRQKQAAdaemekhkqfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRgq 2209
Cdd:COG1196 542 AALAAALQNIVVEDDEVA----------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2210 vEEELFSLRVQMEELGklkarieaenRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2289
Cdd:COG1196 610 -EADARYYVLGDTLLG----------RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2290 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERL 2369
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2370 RLRVAEMSRAQARAEEDARRFRK-------QAEDIGERLyrTELATQekvmlVQTLETQRqqsdrdaERLREAIAELEHE 2442
Cdd:COG1196 759 PPDLEELERELERLEREIEALGPvnllaieEYEELEERY--DFLSEQ-----REDLEEAR-------ETLEEAIEEIDRE 824
|
.
gi 1920237974 2443 K 2443
Cdd:COG1196 825 T 825
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
162-264 |
3.04e-29 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 114.64 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 162 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 239
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1920237974 240 DVDVPQPDEKSIITYVSSLYDAMPR 264
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
164-259 |
3.44e-29 |
|
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: 113.98 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 164 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 242
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1920237974 243 VPQPDEKSIITYVSSLY 259
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
144-261 |
3.56e-28 |
|
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: 112.10 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 144 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAF 223
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237974 224 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1178-1796 |
3.71e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1178 QTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVpLANSQAVREQLRQEKALLED-IERHGEKveecqrfa 1256
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELeLEEAQAE-------- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1257 kqyinaikdyELQLVTYKAQLEPVASPAKkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAE 1336
Cdd:COG1196 290 ----------EYELLAELARLEQDIARLE--------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1337 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqglqrrmqeEVARREEVAVEAQEQKRSIQEELQHLRQSSEAE 1416
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---------EALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1417 IQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRqvQDETQRKRQ 1496
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA--RLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1497 AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE----K 1572
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflplD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1573 TAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEE 1652
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1653 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1732
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1733 KRRELEAELAKVRAEMEvllaskaraEEESRSTSEKSKQRLEAEAGRF--------RELAEEAARLRALAEE 1796
Cdd:COG1196 741 LLEEEELLEEEALEELP---------EPPDLEELERELERLEREIEALgpvnllaiEEYEELEERYDFLSEQ 803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1492-2207 |
4.08e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1492 QRKRQAEAELAlrvQAEAEAAR--------EKQralqaLEELRLQAEEAERRLRQAEAERARQVQVALetaqrsaeAELQ 1563
Cdd:COG1196 172 ERKEEAERKLE---ATEENLERledilgelERQ-----LEPLERQAEKAERYRELKEELKELEAELLL--------LKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1564 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkanEALRLRLQAEEvaqqksltq 1643
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAEL--------------------------EELRLELEELE--------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1644 aeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1723
Cdd:COG1196 281 ------------------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1724 QREAAAATQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1803
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1804 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLR 1883
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1884 KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEE 1963
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1964 ERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2043
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2044 QKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLR 2123
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2124 KEAEQEAARRAQAEQAALRQKQAADAEMEKHKqfAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLK-- 2197
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELER--LEREIEALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEea 817
|
730
....*....|.
gi 1920237974 2198 -AEVTEAARQR 2207
Cdd:COG1196 818 iEEIDRETRER 828
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
42-144 |
3.03e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 108.73 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1706-2596 |
1.01e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.79 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1706 TEQGEQQRQLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1783
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1784 AEEAARlralAEEAKRQrqlAEEdaVRQRAEAERvlAEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDeafQR 1861
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAED---AK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1862 RLLEEQAAqhkadIEARLA-QLRKASESelerqkglvedtlrqrRQVEEeilalkgsfekaaAGKAELELELGRIRgTAE 1940
Cdd:PTZ00121 1177 KAEAARKA-----EEVRKAeELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAE 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1941 DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQL 2020
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKA 1298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2021 QLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERlrseaeaarraaeeaeaareraereaaqsRRQVEEAER 2100
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAK 1349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2101 LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQaLRQKAQVEQELTALRLQLE 2180
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAE 1428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2181 ETDHQksildEELQRLKAEVTEAARQRGQVEEelfslRVQMEELGKlkaRIEAENRALVLRDKDSAQRLLQE---EAEKM 2257
Cdd:PTZ00121 1429 EKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEA 1495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2258 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2333
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2334 KeQMAQQLAQETQgfqktlETERQRQLEMSAEAERLRLRVAEmsraQARAEEDARrfrKQAEDIGErlyrtelaTQEKVM 2413
Cdd:PTZ00121 1576 K-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAK---IKAEELKK--------AEEEKK 1633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2414 LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsflsekdslLQRErci 2493
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------------LKKE--- 1697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2494 EQEKAKLEQL---FQDEVAKAQALREEQQRQQQqmqqekqqlaaSMEEARRRQHE----AEEgVRRQQEELQRLAQQQQQ 2566
Cdd:PTZ00121 1698 AEEAKKAEELkkkEAEEKKKAEELKKAEEENKI-----------KAEEAKKEAEEdkkkAEE-AKKDEEEKKKIAHLKKE 1765
|
890 900 910
....*....|....*....|....*....|....
gi 1920237974 2567 QEKLLAEENQR----LRERLQHLEEERRAALARS 2596
Cdd:PTZ00121 1766 EEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKK 1799
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
162-261 |
1.11e-26 |
|
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: 106.99 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 162 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 240
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1920237974 241 VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
146-261 |
1.65e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 107.09 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237974 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
42-147 |
1.72e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.04 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
146-261 |
8.06e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 105.19 E-value: 8.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237974 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1872-2600 |
1.13e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 118.32 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1872 KADIEARLAQLRKASESELERQKGLVEDTlRQRRQVEEEilalKGSFE---KAAAGKAELELELGRIRGTAEDTLRSKE- 1947
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDN-RADEATEEA----FGKAEeakKTETGKAEEARKAEEAKKKAEDARKAEEa 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1948 -QAE-----QEAARQRQLAAEEERRRREAEERVQKSLAAEE----EAARQ----RKAA----LEEVERLKA--KVEEARR 2007
Cdd:PTZ00121 1134 rKAEdarkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDakkaEAARKaeevRKAEelrkAEDARKAEAarKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2008 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAERE 2087
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2088 AAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA--EMEKHKQFAEQALRQK 2165
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2166 AQVEQELTALRLQLEETDHQksildEELQRLKAEVTEAARQRGQVEEElfslrvqmeelgKLKARiEAENRALVLRDKDS 2245
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAA------------KKKAD-EAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2246 AQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQlAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2323
Cdd:PTZ00121 1436 AKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKK-ADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2324 QEqARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQA--RAEEDARRFRKQAEDigerL 2401
Cdd:PTZ00121 1513 DE-AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKAEEakKAEEDKNMALRKAEE----A 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2402 YRTELATQEKVM-LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFL 2480
Cdd:PTZ00121 1587 KKAEEARIEEVMkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2481 SEKDsllqrerciEQEKAKLEQLFQDEVAKAQAlrEEQQRQQQQMQQEKQQLAASMEEARRRQHE---AEEGVRRQQEEL 2557
Cdd:PTZ00121 1667 AKKA---------EEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAKKAEELKKKEAEEKKKAEElkkAEEENKIKAEEA 1735
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237974 2558 QRLAQQ-QQQQEKLLAEENQrlRERLQHL--EEERRAALARSEEIA 2600
Cdd:PTZ00121 1736 KKEAEEdKKKAEEAKKDEEE--KKKIAHLkkEEEKKAEEIRKEKEA 1779
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
37-146 |
1.38e-25 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 104.45 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 37 KDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHR 113
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTK 93
|
90 100 110
....*....|....*....|....*....|....
gi 1920237974 114 -QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21247 94 vPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1398-2200 |
1.61e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1398 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEaEAQKRQAQ 1477
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE-ARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1478 EEAERLR-----RQVQD--ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE----AERARQ 1546
Cdd:PTZ00121 1122 KKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEelrkAEDARK 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1547 VQVAletaqRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1626
Cdd:PTZ00121 1202 AEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1627 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGTAQQrlaAEQEliRLRAET 1706
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKK---AEEA--KKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1707 EQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEmEVLLA--SKARAEEESRSTSEKSKQrlEAEAGRFRELA 1784
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKAdeAKKKAEEDKKKADELKKA--AAAKKKADEAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1785 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1864
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1865 EEQAAQHKADiEARLAQLRKASEsELERQKglvedtlrQRRQVEEeilaLKGSFEKAAAGKAELELELGRirgtAEDTlR 1944
Cdd:PTZ00121 1504 KAAEAKKKAD-EAKKAEEAKKAD-EAKKAE--------EAKKADE----AKKAEEKKKADELKKAEELKK----AEEK-K 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1945 SKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRlrerAEQESARQLQLaq 2024
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK----AEEEKKKVEQL-- 1638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2025 eaaqKRLQAEEKAHAFAVQQKEQELQQTLqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQs 2104
Cdd:PTZ00121 1639 ----KKKEAEEKKKAEELKKAEEENKIKA-------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2105 aeeQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADaemEKHKQFAEQALRQKAQVEQELTALRLQLEETDH 2184
Cdd:PTZ00121 1707 ---LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
810
....*....|....*.
gi 1920237974 2185 QKSILDEELQRLKAEV 2200
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEV 1796
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
46-143 |
2.18e-25 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 103.16 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 46 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 121
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1920237974 122 NDDIADGnPKLTLGLIWTIILH 143
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1335-2546 |
1.61e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 114.15 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1335 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAEREAQGLQRRMQ--EEVARREEvAVEAQEQKRSIQEELQHLRQ 1411
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQQldQELAERRQ-TVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1412 SSEA-----EIQAKARQVEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERLRRQ 1486
Cdd:NF041483 162 ESQArrlldESRAEAEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1487 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQaeEAERRLRQAEAERARQVQVALETA-QRSAEAELQSE 1565
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAaKQLASAESANE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1566 hasfaektaQLERTLKEEhvaVVQLREEATRRAQQQAEAERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQA 1644
Cdd:NF041483 305 ---------QRTRTAKEE---IARLVGEATKEAEALKAEAEQALADARAEAEKLVaEAAEKARTVAAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1645 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARL 1723
Cdd:NF041483 373 AEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1724 QREAAaatQKRRELEAELAKVRAEmevllaskARAEeesrstsekSKQRLEAEAGRFRELAEEAarlRALAEEAKRQrql 1803
Cdd:NF041483 446 RGEAE---QLRAEAVAEGERIRGE--------ARRE---------AVQQIEEAARTAEELLTKA---KADADELRST--- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1804 aeedavrQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA-QHKADIEARLAQL 1882
Cdd:NF041483 500 -------ATAESERVRTE---AIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArELREETERAIAAR 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1883 RKASESELERQKGLVEdtlrQRRQVEEEilALKGSFEKAAAGKAELELELGRIRGTAEDTLRS-KEQAEQEAARQRqlaa 1961
Cdd:NF041483 570 QAEAAEELTRLHTEAE----ERLTAAEE--ALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLR---- 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1962 eeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLR-------ERAEQESARQLQLAQ-EAAQKRLQ 2032
Cdd:NF041483 640 -----TEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQEsADRVRaeaaaaaERVGTEAAEALAAAQeEAARRRRE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2033 AEE---KAHAFAVQQKEQELQQTLQQEQSVLERLrseaeaarraaeeaeaareraEREAAQSRRQVEEAERlkqsaeeqa 2109
Cdd:NF041483 715 AEEtlgSARAEADQERERAREQSEELLASARKRV---------------------EEAQAEAQRLVEEADR--------- 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2110 qaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-DHQKSI 2188
Cdd:NF041483 765 --------------------------------RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAaERTRTE 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2189 LDEELQRLKAEvteAARQRGQVEEELFSLRVQ-MEELGKLKARIEAEnralVLRDKDSAQRLLQEEAEKMKQVAEEAA-R 2266
Cdd:NF041483 813 AQEEADRVRSD---AYAERERASEDANRLRREaQEETEAAKALAERT----VSEAIAEAERLRSDASEYAQRVRTEASdT 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2267 LSVAAQEAARLRQLAEEDLAQQRALA---EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAq 2343
Cdd:NF041483 886 LASAEQDAARTRADAREDANRIRSDAaaqADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIA- 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2344 etqgfqktleterqrqlEMSAEAERLRLRVAE-MSRAQARAE---EDARRFRKQAEDIGERLyRTELATQEKVMLVQTLE 2419
Cdd:NF041483 965 -----------------EATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERL-RTEAREEADRTLDEARK 1026
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2420 TQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLL----QETQALQQSFLSEKDSLLQRERcieq 2495
Cdd:NF041483 1027 DANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVgaarKEAERIVAEATVEGNSLVEKAR---- 1102
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 2496 ekAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLaasMEEARRRQHEA 2546
Cdd:NF041483 1103 --TDADELLVGARRDATAIRERAEELRDRITGEIEEL---HERARRESAEQ 1148
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
43-146 |
2.34e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 43 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 118
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
146-261 |
2.35e-24 |
|
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: 100.92 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237974 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
164-259 |
6.10e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 99.15 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 164 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 242
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1920237974 243 VPQPDEKSIITYVSSLY 259
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
158-264 |
6.94e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 6.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 158 MTAKEKLLLWSQRMVEGC-QGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 234
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1920237974 235 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 264
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1372-2232 |
9.96e-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: 111.30 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1372 REAQGLQRRMQEEVARREEVAVEAQEQKRSIQ------EELQHLR-QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1444
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKaELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1445 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1524
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1525 LRLQAEEAERRLrqaeaerarqvqvaletaqrsaeAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaea 1604
Cdd:TIGR02168 335 LAEELAELEEKL-----------------------EELKEELESLEAELEELEAELEELESRLEELEEQLE--------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1605 eraraeaerelerwQLKANEALRLRLQAEEVAQQKSLTQAEaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQL 1684
Cdd:TIGR02168 383 --------------TLRSKVAQLELQIASLNNEIERLEARL-------------------ERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1685 AEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS 1764
Cdd:TIGR02168 430 LE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1765 TSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaeEDAVRQRAEAERVLAEKLAAiSEATRLKTEAEIALKE 1842
Cdd:TIGR02168 508 VKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL---QAVVVENLNAAKKAIAFLKQ-NELGRVTFLPLDSIKG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1843 KEAENERLRRLAEDEAFQRRL--LEEQAAQHKADIEARLAQLRKASEselerqkglVEDTLRQRRQVEEEIL-------- 1912
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRivtldgdl 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1913 -----ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerRRREAEERVQKSLAAEEEAARQ 1987
Cdd:TIGR02168 655 vrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1988 RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLERLRSEA 2067
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2068 EAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAA 2147
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2148 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK---AEVTEAARQRGQVEEELFSLRVQMEEL 2224
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*...
gi 1920237974 2225 GKLKARIE 2232
Cdd:TIGR02168 966 DEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1298-2034 |
6.55e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1298 QEYVDLRTRYSELS-TLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAL--------EKQRQLAEA------ 1362
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlevsELEEEIEELqkelya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1363 HAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE------ELQHLRQSSEAEIQAKARQVEAAERSRLRIEE 1436
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1437 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQ 1516
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1517 RALQALEELRLQAEEAERRLRQAEAERarqvqvaletaqRSAEAELQsEHASFAEKTAQLERTLKEEHVAVVQLREEAtr 1596
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQAL------------DAAERELA-QLQARLDSLERLQENLEGFSEGVKALLKNQ-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1597 raQQQAEAERARAEAERELERWQLKANEALRLRLQA---EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1673
Cdd:TIGR02168 516 --SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1674 AEQELEKQRQLA---EGTAQQRLAAEQELIRLR-AETEQG--EQQRQLLEEELA------------RLQREAAAATQKRR 1735
Cdd:TIGR02168 594 LKNIEGFLGVAKdlvKFDPKLRKALSYLLGGVLvVDDLDNalELAKKLRPGYRIvtldgdlvrpggVITGGSAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1736 ELEAELAKVRAEMEvLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA 1815
Cdd:TIGR02168 674 ERRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1816 ERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED-----EAFQRRLLEEQAAQHKADIEARLAQLRKAS-ESE 1889
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLLNEEAANLRERLESlERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1890 LERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1969
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1970 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERA--EQESARQLQLAQEAAQKRLQAE 2034
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYslTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1690-2482 |
7.50e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1690 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKS 1769
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKA-ERYKELKAELRELELA---LLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1770 KQRLEAEagrFRELAEEAARLRALAEEAKRQRQLAEEDAvrqrAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENER 1849
Cdd:TIGR02168 248 LKEAEEE---LEELTAELQELEEKLEELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1850 LRRLAEDEAFQRRLLEEQAAQHKADIEaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFekaaagkAELE 1929
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1930 LELGRIRGTAEDTLRSKEQAEQEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL 2008
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2009 RERAEQESARQLQLAQE--AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2086
Cdd:TIGR02168 473 AEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2087 EAAQSRRQVEEAerLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAaDAEMEKHKQFAeqaLRQKA 2166
Cdd:TIGR02168 553 ENLNAAKKAIAF--LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF-DPKLRKALSYL---LGGVL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2167 QVEQELTALRLQlEETDHQKSI--LDEELQRLKAEVTEAARQRGQVeeeLFSLRVQMEELGKLKARIEAENRAL--VLRD 2242
Cdd:TIGR02168 627 VVDDLDNALELA-KKLRPGYRIvtLDGDLVRPGGVITGGSAKTNSS---ILERRREIEELEEKIEELEEKIAELekALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2243 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-----------KMQAVQEATRLKA 2311
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleerLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2312 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRAQARAEEDARRFR 2391
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2392 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTvRQEQLLQE 2471
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVR 937
|
810
....*....|.
gi 1920237974 2472 TQALQQSFLSE 2482
Cdd:TIGR02168 938 IDNLQERLSEE 948
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1326-2037 |
9.45e-23 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 108.37 E-value: 9.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1326 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQE 1404
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIAR---LVGEATKEAEALKA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1405 ELQHLRQSSEAEiqAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLR 1484
Cdd:NF041483 331 EAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATTRAAAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1485 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRLQaEEAeRRLRqAEAERARqvqvaletaqrsaeaelqs 1564
Cdd:NF041483 400 REAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLR------------------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1565 ehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELErwqlkANEALRLRLQAEEVAqqKSLTQA 1644
Cdd:NF041483 454 -----AEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTA-----TAESERVRTEAIERA--TTLRRQ 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1645 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAETEQ----GEQQRQLLEEE 1719
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEErltaAEEALADARAE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1720 LARLQREAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALA 1794
Cdd:NF041483 602 AERIRREAAEETERLRTEAAErirtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEA------AAEAERLKSEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1795 EE-AKRQRQLAEEDAVRQRAEAERVLAeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrllEEQAAQHKA 1873
Cdd:NF041483 676 QEsADRVRAEAAAAAERVGTEAAEALA---AAQEEAARRRREAEETLGSARAEADQERERAREQS------EELLASARK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1874 DIEARLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEILALKGSFEKAAA-GKAELELELGRIRGtaeD 1941
Cdd:NF041483 747 RVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS---D 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1942 TLRSKEQAEQEAARQRQlaaeeerrrreaeERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERAeqeSARQL 2020
Cdd:NF041483 824 AYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEA---SDTLA 887
|
730
....*....|....*..
gi 1920237974 2021 QLAQEAAQKRLQAEEKA 2037
Cdd:NF041483 888 SAEQDAARTRADAREDA 904
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
160-259 |
9.49e-23 |
|
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: 95.71 E-value: 9.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 160 AKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 239
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1920237974 240 D-VDVPQPDEKSIITYVSSLY 259
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1861-2502 |
1.20e-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: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1861 RRLLEEQA--AQHKADIEARLAQLRKASE---------SELERQKglveDTLRQRRQVEEEILALKGSFEKAaagkaELE 1929
Cdd:COG1196 158 RAIIEEAAgiSKYKERKEEAERKLEATEEnlerledilGELERQL----EPLERQAEKAERYRELKEELKEL-----EAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1930 LELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2009
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2010 ERAEQESARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAA 2089
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELE-----------------------EELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2090 QSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2169
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2170 QELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenrALVLRDKDSAQRL 2249
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG---VKAALLLAGLRGL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2250 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2329
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2330 LQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQ 2409
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2410 EKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQR 2489
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
650
....*....|...
gi 1920237974 2490 ERcIEQEKAKLEQ 2502
Cdd:COG1196 763 EE-LERELERLER 774
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
162-262 |
1.69e-22 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 94.84 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 162 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 241
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1920237974 242 DVPQPDEKSIITYVSSLYDAM 262
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1322-2038 |
1.79e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 107.22 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1322 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAEREAQGLQRRMQEEVAR-REEV 1391
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1392 AVEAQEQKRSIQEELQHLRqsSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLE-ATERQRGGAEGELQALRARAEE-- 1468
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1469 --AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE--LALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEAER 1543
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLRTEAAEriRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRsEAAAEA 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1544 ARQVQVALETAQRsaeaeLQSEHASFAEKTAQlertlkeehvavvqlreeatrraqqqaeaeraraeaerelerwqlKAN 1623
Cdd:NF041483 669 ERLKSEAQESADR-----VRAEAAAAAERVGT---------------------------------------------EAA 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1624 EALrlrlqaeevaqqksltqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI--- 1700
Cdd:NF041483 699 EAL----------------------------------AAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasa 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1701 RLRAETEQGEQQRqLLEEELARLQREAAAATQKRRELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAE 1776
Cdd:NF041483 745 RKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSD 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1777 AGRFRELA-EEAARLRALA-EEAKRQRQLAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLA 1854
Cdd:NF041483 824 AYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADA 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1855 EDEAFQRRllEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAElelelgR 1934
Cdd:NF041483 901 REDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------R 972
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1935 IRGTAEDTLRSkeqAEQEAARQRQLAAEEERRrreaeervqkslaAEEEAARQRKAALEEVERL--KAKVEEARRLRERA 2012
Cdd:NF041483 973 LRAEAAETVGS---AQQHAERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAA 1036
|
730 740
....*....|....*....|....*.
gi 1920237974 2013 EQESARQLQLAQEAAQKRLQAEEKAH 2038
Cdd:NF041483 1037 EQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
159-257 |
2.08e-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: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1920237974 238 PEDVDVPQPDEKSIITYVSS 257
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1669-2439 |
2.25e-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: 107.06 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1669 RQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETeqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEM 1748
Cdd:TIGR02168 207 RQAEKAERYKELKAELRE--------LELALLVLRLEE---------LREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1749 EVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1828
Cdd:TIGR02168 270 EELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1829 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQH---KADIEARLAQLRKASeSELERQKGLVEDTLRQRR 1905
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLN-NEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1906 QVEEEILALKGSFEKAAagKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRrreaeervQKSLAAEEEAA 1985
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1986 RQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQK 2045
Cdd:TIGR02168 488 QARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2046 EQELQQTLQQEQSVLER-LRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQA 2117
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRI 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2118 AAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK 2197
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2198 AEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ----- 2272
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2273 ------------EAARLRQLAEEDLAQQRALAEKML----KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2336
Cdd:TIGR02168 805 ldelraeltllnEEAANLRERLESLERRIAATERRLedleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2337 MAQQLAQ---ETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDigerLYRTELATQEKvm 2413
Cdd:TIGR02168 885 LEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE----EYSLTLEEAEA-- 958
|
810 820
....*....|....*....|....*.
gi 1920237974 2414 LVQTLETQRQQSDRDAERLREAIAEL 2439
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
159-259 |
2.97e-22 |
|
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: 94.41 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1920237974 239 EDVDVPQ-PDEKSIITYVSSLY 259
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1976-2591 |
4.33e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1976 KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQ 2055
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2056 EQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQ 2135
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2136 AEQAALRQKQAADAEMEKHKQFAEQALRQkaqvEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2215
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2216 SLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2295
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2296 LKEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRV 2373
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2374 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2453
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2454 QLKSEEMQTVRQEQLLQETQALQQsflsekdsLLQRERCIEQEKAKLEQlfqdevakaqalreeqqrqqqqmqqekqqlA 2533
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAE--------EEEERELAEAEEERLEE------------------------------E 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 2534 ASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA 2591
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1773-2588 |
6.14e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1773 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAVR------------QRAEAERVLAEKLAAISEATRlKTEAE 1837
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1838 IALKEKEAENERLRRLAEDEAFQRRLLEEQAAQhKADIEARLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILAL 1914
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1915 KGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1994
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1995 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ-QKEQELQQTLQQEQSVLERLRSEAEAAR 2071
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2072 RAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQaeqaaLRQKQAADAEM 2151
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-----LSELISVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2152 EKHKQFAEQALRQKAQVEQELTALRLQleetDHQKsilDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARI 2231
Cdd:TIGR02168 536 EAAIEAALGGRLQAVVVENLNAAKKAI----AFLK---QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2232 EAENRA-----------LVLRDKDSAQRLLQEEAEKMKQVAEEAARLS---VAAQEAARLRQLAeedLAQQRALAEkmLK 2297
Cdd:TIGR02168 609 KFDPKLrkalsyllggvLVVDDLDNALELAKKLRPGYRIVTLDGDLVRpggVITGGSAKTNSSI---LERRREIEE--LE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2298 EKMQAVQEAtrlkaEAELLQQQKELAQEQarrlqedkeqmaQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMS 2377
Cdd:TIGR02168 684 EKIEELEEK-----IAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2378 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS 2457
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2458 EEMQTvRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASME 2537
Cdd:TIGR02168 827 ESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 2538 EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2588
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1000-1564 |
6.24e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1000 ARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1079
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1080 RSTQEAEEVLRAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVE 1159
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1160 RWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL 1239
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1240 EDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1319
Cdd:COG1196 477 AALAE-----------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1320 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA----HAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1395
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1475
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1476 AQEEAERLRRQvqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA-LETA 1554
Cdd:COG1196 692 ELELEEALLAE---EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEeLERE 768
|
570
....*....|
gi 1920237974 1555 QRSAEAELQS 1564
Cdd:COG1196 769 LERLEREIEA 778
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
42-147 |
6.34e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.38 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
159-263 |
7.12e-22 |
|
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: 93.32 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGcQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21245 3 KAIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1920237974 239 EDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
42-147 |
7.30e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.00 E-value: 7.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1469-2603 |
4.76e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.60 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1469 AEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE--AEAAREKQRALQALEELRLQAE-EAERRLRQAEAERAR 1545
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1546 QVQVA---LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVvqlREEATRRAQQQAEAERARAEAERELERWQLKA 1622
Cdd:NF041483 161 TESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1623 NEALRLRLQAE-EVAQQKSltqaeaekqkeeaereaRRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrlAAEQELIR 1701
Cdd:NF041483 238 AEQLRSSTAAEsDQARRQA-----------------AELSRAAEQRMQE---AEEALREARAEAEKVVAE--AKEAAAKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1702 LRAETEQGEQQRQLLEEELARLQREAAA-ATQKRRELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSKQRLEAEA 1777
Cdd:NF041483 296 LASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1778 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAI---------------SEATRLKTEAEIALKE 1842
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1843 KEAENERLRRLAEDEAFQR-----RLLEEQAAQHKADIEarlaQLRKASESELERQKG-LVEDTLRQRRQVEEeilALKG 1916
Cdd:NF041483 456 AVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADAD----ELRSTATAESERVRTeAIERATTLRRQAEE---TLER 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1917 SFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ------LAAEEERRRREAEERVQKSLAAEEEAARQRKA 1990
Cdd:NF041483 529 TRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQaeaaeeLTRLHTEAEERLTAAEEALADARAEAERIRRE 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1991 ALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEKAHAFAVqqkeqelqqtlqqeqsvleRLRSEAEa 2069
Cdd:NF041483 609 AAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAV-------------------RLRSEAA- 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2070 arraaeeaeaareraereaaqsrrqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaada 2149
Cdd:NF041483 666 --------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQ---- 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2150 emekhkqfaEQALRQKAQVEQELTALRLQLEEtdhqksildeelqrlkaevtEAARQRGQVEEELFSLRVQMEELGKLKA 2229
Cdd:NF041483 706 ---------EEAARRRREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAEAQ 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2230 RI--EAENRA--LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA-RLRQLAEEDLAQQRALAekmLKEKMQAVQ 2304
Cdd:NF041483 757 RLveEADRRAteLVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAeRTRTEAQEEADRVRSDA---YAERERASE 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2305 EATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLemsAEAERlrlrvaEMSRAQARAE 2384
Cdd:NF041483 834 DANRLRREA---QEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTL---ASAEQ------DAARTRADAR 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2385 EDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREaiaelehEKDKLKQEAQLLQLKSEEMQTVR 2464
Cdd:NF041483 902 EDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERV-------RADAAAQAEQLIAEATGEAERLR 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2465 QEQLLQETQALQQSflsekdsllqrerciEQEKAKLEQLFQDEVAKAQALReeqqrqqqqmqqekqqlAASMEEARRRQH 2544
Cdd:NF041483 975 AEAAETVGSAQQHA---------------ERIRTEAERVKAEAAAEAERLR-----------------TEAREEADRTLD 1022
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2545 EAeegvrrQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPSR 2603
Cdd:NF041483 1023 EA------RKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTM 1075
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1081-1885 |
1.28e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.29 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1081 STQEAEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1160
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1161 WRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLE 1240
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1241 DIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQyirf 1320
Cdd:TIGR02168 401 EIER-----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE---- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1321 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQE-EVARREEVAVEAQ--- 1396
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAAlgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1397 -------EQKRSIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR 1463
Cdd:TIGR02168 546 rlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1464 ARAEEAEAQKRQAQEEAERLR-------------------RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1524
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1525 LRLQAEEAERRLRQAEAERARQVqvaleTAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaea 1604
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE----- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1605 eraraeaerelerwQLKANEALRLRLQAeEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELaEQELEKQRQL 1684
Cdd:TIGR02168 776 --------------ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL-ERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1685 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE---EE 1761
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrelEE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1762 SRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAVRQRAEAERvLAEKLAAISEATRLkteaeiAL 1840
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AI 992
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1920237974 1841 KEKEAENERLRRLaedeafqrrlleeqaAQHKADIEARLAQLRKA 1885
Cdd:TIGR02168 993 EEYEELKERYDFL---------------TAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1982-2601 |
2.89e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1982 EEAARQRKAALEEVERLKAKVEEARR----LRERAEQ-ESARQLQlaqeAAQKRLQAEEKAHAFAVQQKEqelqqtlqqe 2056
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERqlepLERQAEKaERYRELK----EELKELEAELLLLKLRELEAE---------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2057 qsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQA 2136
Cdd:COG1196 241 ---LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------------EAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2137 EQAALRQKQAADAEMEKHKQfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2216
Cdd:COG1196 305 ARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2217 LRVQMEELgklkARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2296
Cdd:COG1196 384 LAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2297 KEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAER---LRLRV 2373
Cdd:COG1196 460 ALL-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveAAYEA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2374 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2453
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2454 Q--LKSEEMQTVRQEQLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQlfqdEVAKAQALREEQQRQQQQMQQE 2528
Cdd:COG1196 619 GdtLLGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLTGGSRRELLA----ALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 2529 KQQLAASMEEARRRQHEAEEGVRRQQEELQRLAqqqqqqEKLLAEENQRLRERLQHLEEERRAALARSEEIAP 2601
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALE------EQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1852 |
7.86e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.59 E-value: 7.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1083 QEAEEVLRAHEEQLKEAQAVpatlpeLEATKAALKKLRAQAEAQQPvFDALRDELRgaqevgerlqqrHGERDVEVERWR 1162
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI------LNELERQLKSLERQAEKAER-YKELKAELR------------ELELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1163 ErvtlLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVRE---QLRQEKALL 1239
Cdd:TIGR02168 236 E----LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1240 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPV-----ASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLT 1314
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1315 SQYIRFISETLRRMEEE-ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAV 1393
Cdd:TIGR02168 392 ELQIASLNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1394 EAQEQKRSIQEELQHLR------QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALR 1463
Cdd:TIGR02168 472 EAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1464 ARAEEAEAQKRQAQEEAERLRR----------QVQDETQRKRQAEAELALRVQAEAEAAREK-QRALQALEELRLQAEEA 1532
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1533 ERRLRQAEAERARQVQVALE---------TAQRSAEAEL-----QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRA 1598
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDgdlvrpggvITGGSAKTNSsilerRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1599 QQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL 1678
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1679 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARA 1758
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1759 EEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE------DAVRQRAEAERVLAEKLAAISEATRL 1832
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNLQERLSEEYSL 951
|
810 820
....*....|....*....|.
gi 1920237974 1833 KTEAEIALKEK-EAENERLRR 1852
Cdd:TIGR02168 952 TLEEAEALENKiEDDEEEARR 972
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1329-2065 |
1.40e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.97 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1329 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQh 1408
Cdd:NF041483 560 EETERAIAARQAEAAEELTRLHTEAEERLTAAE---EALADARAEAERIRREAAEETER---LRTEAAERIRTLQAQAE- 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1409 lrqsSEAEiqaKARQVEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1487
Cdd:NF041483 633 ----QEAE---RLRTEAAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1488 QDETQRKRQAEAELAlrvQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQVqvalETAQRSAeaelqSEHA 1567
Cdd:NF041483 706 EEAARRRREAEETLG---SARAEADQERERAREQSEEL---LASARKRVEEAQAEAQRLV----EEADRRA-----TELV 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1568 SFAEKTAQLERTlkeehvAVVQLREEATRraqqqaeaeraraeaerelerwqlkanEALRLRLQAEEVAQQksLTQAEAE 1647
Cdd:NF041483 771 SAAEQTAQQVRD------SVAGLQEQAEE---------------------------EIAGLRSAAEHAAER--TRTEAQE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1648 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ--------------- 1712
Cdd:NF041483 816 EADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqd 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1713 ----RQLLEEELARLQREAAA-----ATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrel 1783
Cdd:NF041483 893 aartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA------ 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1784 AEEAARLRALAEEAKRQrqlAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEialkekeAENERLRRLAEDEAFQRR- 1862
Cdd:NF041483 967 TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR-------EEADRTLDEARKDANKRRs 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1863 ---------LLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1933
Cdd:NF041483 1034 eaaeqadtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELLVGAR 1113
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1934 R----IRGTAEDtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK--------AK 2001
Cdd:NF041483 1114 RdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvriAA 1192
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2002 VEEARRLRERAEQESARQLQLAQ------EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2065
Cdd:NF041483 1193 VKKAEGLLKEAEQKKAELVREAEkikaeaEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALES 1262
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
163-260 |
1.91e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 86.63 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 163 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 241
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237974 242 DVPQPDEKSIITYVSSLYD 260
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
44-144 |
1.31e-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: 83.79 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 44 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 119
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1920237974 120 IRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
159-258 |
1.40e-18 |
|
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: 83.68 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237974 239 ED-VDVPQPDEKSIITYVSSL 258
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
777-843 |
3.39e-18 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 81.15 E-value: 3.39e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 777 QLKPRSpaHPMRGRVPLLAVCDYKQVEVTVHKGDECQMVGPAQPFYWKVLGSSCSEAAMPSVCFLVP 843
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
45-142 |
4.00e-18 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 82.39 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 45 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 120
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1920237974 121 RNDDI-ADGNPKLTLGLIWTIIL 142
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
159-259 |
4.07e-18 |
|
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: 82.78 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1920237974 239 EDVDV--PQPDEKSIITYVSSLY 259
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
155-260 |
4.14e-18 |
|
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: 82.69 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 155 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 234
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1920237974 235 LLDPEDV-DVPQPDEKSIITYVSSLYD 260
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
162-258 |
4.61e-18 |
|
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: 82.36 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 162 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 237
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1920237974 238 PEDVDVPQPDEKSIITYVSSL 258
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1323-1911 |
5.00e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 92.67 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AQGLQRRMQEEVARREEVAVEA 1395
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1453
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1454 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELrLQAEEAE 1533
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1534 RRLRQAeAERarqvqvALETAQRSaeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAER 1613
Cdd:COG4913 474 ERWRGA-IER------VLGGFALT----LLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1614 ELERWQLKANEALRLR---LQAEEVAQ----QKSLTQAEAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEK- 1680
Cdd:COG4913 543 KPHPFRAWLEAELGRRfdyVCVDSPEElrrhPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEl 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1681 QRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLLASKA 1756
Cdd:COG4913 623 EEELAEAEERlEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1757 RAEEESRSTSEKsKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRlKTEA 1836
Cdd:COG4913 703 ELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID-ALRA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1837 EIALKEKEAENERLRRLAEDEAFQ-------------RRLLEEQAAQHKADIEARLAQLRKasESELERQKGLVEDTLRQ 1903
Cdd:COG4913 781 RLNRAEEELERAMRAFNREWPAETadldadleslpeyLALLDRLEEDGLPEYEERFKELLN--ENSIEFVADLLSKLRRA 858
|
....*...
gi 1920237974 1904 RRQVEEEI 1911
Cdd:COG4913 859 IREIKERI 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1321-1892 |
2.11e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.48 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1321 ISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAEREAQGLQRRMQEEVARREE 1390
Cdd:PRK02224 218 LDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1391 vaveaqeqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1467
Cdd:PRK02224 291 -----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1468 EAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQAEAErarqv 1547
Cdd:PRK02224 360 ELREEAAELESELEEAREAV--EDRREEIEELEEEIEELRERFGDAPVDL--GNAEDFLEELREERDELREREAE----- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1548 qvaLETAQRSAEAELQSEHASFAE-KTAQLERTLKE-EHVAVVQLREEatrraqqqaeaeraraeaerelerwQLKANEA 1625
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEAgKCPECGQPVEGsPHVETIEEDRE-------------------------RVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1626 LRLRLQAEEVAQQKSLTQAEAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1702
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1703 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1782
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRER 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1783 LAEEAARLRALAEEAKRQRqLAEEDAVRQRAEA--ERVlAEKLAAISEAtRLKTEAEIALKEKEAEN-ERLR-RLAEDEA 1858
Cdd:PRK02224 629 LAEKRERKRELEAEFDEAR-IEEAREDKERAEEylEQV-EEKLDELREE-RDDLQAEIGAVENELEElEELReRREALEN 705
|
570 580 590
....*....|....*....|....*....|....*.
gi 1920237974 1859 FQRRL--LEEQAAQHKADIEARLAQLRKASESELER 1892
Cdd:PRK02224 706 RVEALeaLYDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1381-2286 |
4.76e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 89.26 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1381 MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlriEEEIRVVRLQLEATERQRGGAEGELQ 1460
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-----KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1461 ALRARAEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE 1540
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1541 AERARQVQVALETAQRSAEAELQSEHASFAEKtaqleRTLKEEHVAVVQLREEatrraqqqaeaeraraeaerelerwql 1620
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEE--------------------------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1621 kANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1700
Cdd:pfam02463 357 -EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1701 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA----- 1775
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvllal 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1776 -EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1854
Cdd:pfam02463 516 iKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1855 EDEAFQRRLLeeqAAQHKADIEARLAQ---------LRKASESELERQKGLVEDTLRQRRQVEEEILALKG---SFEKAA 1922
Cdd:pfam02463 596 VLEIDPILNL---AQLDKATLEADEDDkrakvvegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEvkaSLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1923 AGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV 2002
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2003 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARE 2082
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK---VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2083 RAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaadAEMEKHKQFAEQAL 2162
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE---EKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2163 RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEvteaarQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRD 2242
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE------EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1920237974 2243 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLA 2286
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
950-1859 |
5.49e-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: 89.36 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 950 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSA 1029
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1030 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL---------KTISLVIRSTQEAEEVLRAHEEQLKEAQ 1100
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1101 AVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERvtlllerwqavlaqT 1179
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--------------L 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1180 DVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAvplansqavreqlrqekalleDIERHGEKVEECQRFAKQY 1259
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1260 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR 1339
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1340 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGlqrRMQEEVARREEVAVEAQEQKRS-------------IQEEL 1406
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1407 QHLRQSSEA--------------EIQAKARQ-------VEAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1461
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpKYEPAFKYvfgdtlvVEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1462 LRARAEEAEAQkrQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeAEAAREKQRALQALEELRLQAEEAERRlRQAEA 1541
Cdd:TIGR02169 667 LFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKLK 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1542 ERARQVQVALETAQRSAEAElQSEHASFAEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaeRELERWQLK 1621
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENV-KSELKELEARIEELEEDLHKLEEALNDLEAR-------------------LSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1622 ANEalrLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIR 1701
Cdd:TIGR02169 797 QAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEE 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1702 LRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAEAGRFR 1781
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDE 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1782 ELAEEAARLRALAEEAKR-QRQLAEEDAVRQRA--EAERVLAEKLAAISEATRLKTEAEiALKEKEAENERLRRLAEDEA 1858
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKREVFMEA 1023
|
.
gi 1920237974 1859 F 1859
Cdd:TIGR02169 1024 F 1024
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1328-2199 |
5.88e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 89.26 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1328 MEEEERLAEQQRAEERERLAEVEaaLEKQRQLAEAHAQAKAQAEREAQGLqrRMQEEVARREEVAVEAQEQKRSIQEELQ 1407
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYL--LYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1408 HLRQSSEAEIQakarqvEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1485
Cdd:pfam02463 255 SSKQEIEKEEE------KLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1486 QVQDETQRKRQAEAELAL--RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEAE 1561
Cdd:pfam02463 329 ELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAakLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1562 LQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSL 1641
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1642 TQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEE 1718
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1719 ELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeagrfRELAEEAARLRALAEEAK 1798
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1799 RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1878
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1879 LAQLRKaseSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ 1958
Cdd:pfam02463 723 LADRVQ---EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1959 laaeeerrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2038
Cdd:pfam02463 800 ----------------EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2039 AFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAA 2118
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2119 AEKLRKEAEQEAARRAQAEQAALRQKQAadAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA 2198
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEE--LGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
.
gi 1920237974 2199 E 2199
Cdd:pfam02463 1022 F 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1299-1952 |
8.65e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.59 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1299 EYVDLRTR-----YSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAERE 1373
Cdd:TIGR02169 212 RYQALLKEkreyeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1374 AQGLQRRMQEEVARREEvAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAaersrlrIEEEIRVVRLQLEATERQRG 1453
Cdd:TIGR02169 289 QLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1454 GAEGELQALRARAEEAEAQKR--------------QAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAL 1519
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAetrdelkdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1520 QA-LEELRLQAEEAERRLRQAEAER--ARQVQVALETAQRSAEAELQS--EHASFAEKTAQLERTLKEEHVAVVQLREEa 1594
Cdd:TIGR02169 440 EEeKEDKALEIKKQEWKLEQLAADLskYEQELYDLKEEYDRVEKELSKlqRELAEAEAQARASEERVRGGRAVEEVLKA- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1595 trraqQQAEAERARAEAERELERWQLKANEALRLRLQA-----EEVAQQK---------------SLTQAEAEKQKEEAE 1654
Cdd:TIGR02169 519 -----SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1655 REARRRGKA---------EEQAVR---QRELAEQELEKQRQL--------------------------AEGTAQQRLAAE 1696
Cdd:TIGR02169 594 SEDGVIGFAvdlvefdpkYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1697 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQR 1772
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1773 LEAEAgrfrELAEEAARLRALaEEAKRQRQLAEED--------AVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKE 1844
Cdd:TIGR02169 754 ENVKS----ELKELEARIEEL-EEDLHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1845 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG 1924
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
730 740
....*....|....*....|....*...
gi 1920237974 1925 KAELELELGRIRGTAEDTLRSKEQAEQE 1952
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
159-258 |
1.21e-16 |
|
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: 78.36 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237974 239 ED-VDVPQPDEKSIITYVSSL 258
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1108-2034 |
4.92e-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: 86.18 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1108 ELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerlqqrhgerdveverwrervtlllerwqavlaqtdvRQRELE 1187
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------------------------------------------ELKLKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1188 QLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL-EDIERHGEKVEECQRFAKQYINAIKDY 1266
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1267 ELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRtryselstltsqyIRFISETLRRMEEEERLAEQQRAEERERL 1346
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE-------------KKKAEKELKKEKEEIEELEKELKELEIKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1347 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaeiQAKARQVEA 1426
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ------LEDLLKEEK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1427 AERSRLRIEEEIRVVRLQLEATERQrggaegelqaLRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1506
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEK----------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1507 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ-LERTLKEEHV 1585
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQkLVRALTELPL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1586 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGK--A 1663
Cdd:pfam02463 576 GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVslE 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1664 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK 1743
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1744 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKL 1823
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1824 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDT-LR 1902
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSK 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1903 QRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAArQRQLAAEEERRRREAEERVQKSLAAEE 1982
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-EADEKEKEENNKEEEEERNKRLLLAKE 970
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1983 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAE 2034
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1414-2340 |
4.96e-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: 85.89 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1414 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA-----QKRQAQEEAERLRRQVQ 1488
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1489 DETQRKRQAEAELALRVQAEAEAAR------EKQRALQALEELRLQAEEAE-----RRLRQAEAERARQVQVALETaqrs 1557
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSIAEKERELEDAEER---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1558 aEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQaeaeraraeaerelerwqlkanEALRLRLQAEEVAQ 1637
Cdd:TIGR02169 324 -LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------EDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1638 QKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1716
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1717 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFRELAEeaarlral 1793
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVAQLGS-------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1794 aeeAKRQRQLAEEDAVRQRAEAERVLAEKLAAiseatrlktEAEIALKEKEAENER---LRRLAEDEAFQRRLLEEQAAQ 1870
Cdd:TIGR02169 533 ---VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRDERRDLSILSEDGVIG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1871 HKADIEARLAQLRKASESELeRQKGLVEDTLRQRRQVEE-EILALKGS-FEKAAA--GKAElelelgRIRGTAEDTLRSK 1946
Cdd:TIGR02169 601 FAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKyRMVTLEGElFEKSGAmtGGSR------APRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1947 EQAEQEAARqrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ-----ESARQLQ 2021
Cdd:TIGR02169 674 AELQRLRER-------------------------LEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2022 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraAEEAEAARERAEREAAQSRRQVEEAERL 2101
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2102 KQSAEeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEE 2181
Cdd:TIGR02169 800 LSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2182 tdhqksiLDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRlLQEEAEKMKQVA 2261
Cdd:TIGR02169 866 -------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2262 EEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2340
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1126-2036 |
8.57e-16 |
|
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: 85.23 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1126 QQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1195
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1196 YRESADPLGAWLRDAKQR-QEQIQAVP--LANSQAVREQLRQEKALLE-DIERHGEKVEECQRFAKQYINAIKDYELQLV 1271
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKmQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1272 TYKAQLEPVASPAKK-PKVQSGSESIIQEyVDLRTRYSElstltsqyirfisETLRRMEEEERLAEQQRAEERERLAEVE 1350
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1351 AalekqrQLAEAHAQAkAQAEREAQGLQRRMQEEVARREevavEAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERS 1430
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKN----NALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1431 RLRIEEEIRVVRLQLEATErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeA 1509
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1510 EAAREKQRALQALEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQ 1589
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1590 LREEATRRAQQQAEAERARAEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVR 1669
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---------------EDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1670 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK------ 1743
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1744 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1802
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1803 LAEEDAVRQRAEAERVLAEKLAA---ISEATRLKTEAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADI 1875
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1876 EARlaqlrkaSESELERQKGLVedtlRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAAR 1955
Cdd:pfam01576 734 QAR-------DEQGEEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1956 QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAE 2034
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQD 882
|
..
gi 1920237974 2035 EK 2036
Cdd:pfam01576 883 EK 884
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
163-260 |
1.01e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 76.07 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 163 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 241
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237974 242 DVPQPDEKSIITYVSSLYD 260
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1341-1903 |
1.07e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.97 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1341 EERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRqsseaeIQAK 1420
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDARE------QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1421 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-AQKRQAQEEAERLRRQvQDETQRKRQAEA 1499
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERE-LEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1500 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS-EH------ASFAEK 1572
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlERrksnipARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1573 TAQLERTLKEEHVAV------VQLREEAtrraqqqaeaeraraeaerelERWQLKANEAL---RLRL--------QAEEV 1635
Cdd:COG4913 446 RDALAEALGLDEAELpfvgelIEVRPEE---------------------ERWRGAIERVLggfALTLlvppehyaAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1636 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG--- 1709
Cdd:COG4913 505 VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1710 ------------------------EQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRST 1765
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1766 S-EKSKQRLEAEagrFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1844
Cdd:COG4913 665 SaEREIAELEAE---LERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1845 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRkaseSELERQKGLVEDTLRQ 1903
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALR----ARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
905-1593 |
1.16e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.72 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 905 EQRQALRSLELHYQA----FLRDSQDAGgfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQE----ESRCQRCISELKDI 976
Cdd:TIGR02168 217 ELKAELRELELALLVlrleELREELEEL---QEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 977 RLQLEACETRTVH---RLRlPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELEL 1053
Cdd:TIGR02168 294 ANEISRLEQQKQIlreRLA-NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1054 TLGKL-EQVRSLSAIYLEKLKTISLvIRSTQEaeeVLRAHEEQLKEAQAVPATlpelEATKAALKKLRAQAEAQQPVFDA 1132
Cdd:TIGR02168 373 RLEELeEQLETLRSKVAQLELQIAS-LNNEIE---RLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1133 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTLL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRD 1209
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1210 AKQR---------------QEQIQAVPLANSQAVR---EQLRQEK----ALLEDIERHGEKVEECQRFAKQYINAIKDYE 1267
Cdd:TIGR02168 525 LSELisvdegyeaaieaalGGRLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1268 LQLVTYKAQLEPVASP---------------AKKPKVQSGSESIIQEYVDLRTRYS--------ELSTL-TSQYIRFISE 1323
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1324 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1403
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1404 EELQHLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1483
Cdd:TIGR02168 765 ELEERLEEAEEEL--------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1484 RRQVQDETQRKRQAEAELAlrvqaeaeaarekqRALQALEELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEAELQ 1563
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIE--------------SLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELS 900
|
730 740 750
....*....|....*....|....*....|..
gi 1920237974 1564 SEHASFAEKTAQLERTLKE--EHVAVVQLREE 1593
Cdd:TIGR02168 901 EELRELESKRSELRRELEElrEKLAQLELRLE 932
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1298-1954 |
2.21e-15 |
|
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: 84.12 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1298 QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE-EERLAE--QQRAEERERLAEVEAALEKQRQLAEAhAQAKAQAEREA 1374
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQEErQETSAElnQLLRTLDDQWKEKRDELNGELSAADA-AVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1375 QGLQRRMQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAeIQAKARQVEAA-ERSRLRIEEEIRVV--------RLQL 1445
Cdd:pfam12128 327 LEDQHGAFLDA--DIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKyNRRRSKIKEQNNRDiagikdklAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1446 EATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEA-----EAAREKQ--- 1516
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENfderiERAREEQeaa 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1517 -----RALQALEELRLQAEEAERRLRQAEAeRARQVQVALETAQR-------------SAEAELQSEHASFAEKTAQLER 1578
Cdd:pfam12128 484 naeveRLQSELRQARKRRDQASEALRQASR-RLEERQSALDELELqlfpqagtllhflRKEAPDWEQSIGKVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1579 TLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkaneALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREAR 1658
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNLY---------------------------GVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1659 RRGKAEEQAvRQRELAEQELEKQrQLAEGTAQQRLA-AEQELIRLraeTEQGEQQRQLLEEELARLQREaaaATQKRREL 1737
Cdd:pfam12128 616 AREKQAAAE-EQLVQANGELEKA-SREETFARTALKnARLDLRRL---FDEKQSEKDKKNKALAERKDS---ANERLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1738 EAELAKVraEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQraeaer 1817
Cdd:pfam12128 688 EAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD------ 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1818 vLAEKlaAISEATRLKTEAEIalKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKG-L 1896
Cdd:pfam12128 760 -LASL--GVDPDVIAKLKREI--RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI-SELQQQLArL 833
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1897 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTlrSKEQAEQEAA 1954
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA--NSEQAQGSIG 889
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2789-2827 |
2.50e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.36 E-value: 2.50e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 2789 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 2827
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
41-140 |
3.06e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.49 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 41 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 115
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1920237974 116 KLVNIRNDDIADGNPKLTLGLIWTI 140
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4026-4064 |
5.61e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 5.61e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 4026 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 4064
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3448-3486 |
5.66e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 5.66e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3448 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRVL 3486
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1732-2599 |
7.49e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1732 QKRRELEAELAKVrAEMEvllASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdavRQ 1811
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFD---RKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1812 RAEAERVLAEKLAAisEATRLKTEAEIAlkEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASESELE 1891
Cdd:TIGR02169 222 EYEGYELLKEKEAL--ERQKEAIERQLA--SLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1892 RQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDtlrSKEQAEQEAARQRQLAAEEERRRREAE 1971
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1972 ERVQKSLAAEEEAARQR---KAALEEVERLKAKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHA 2039
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRdelKDYREKLEKLKREINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2040 FAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAA 2119
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELY----------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2120 EKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTAlrlqleetdhQKSIldEELQRLKA- 2198
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA----------KEAI--ELLKRRKAg 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2199 EVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENR-----------ALVLRDKDSAQRLLQ---------EEAEKMK 2258
Cdd:TIGR02169 574 RATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLMGkyrmvtlegELFEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2259 QVA----EEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2325
Cdd:TIGR02169 654 AMTggsrAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2326 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARaeEDARRFRKQAEDIGERLYRTE 2405
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2406 LATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsfLSEKDS 2485
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2486 LLQRERC-IEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG---------VRRQQE 2555
Cdd:TIGR02169 886 DLKKERDeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaeLQRVEE 965
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1920237974 2556 ELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEEI 2599
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRldeLKEKRAKLEEERKAILERIEEY 1012
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
161-272 |
8.75e-15 |
|
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: 73.49 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 161 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1920237974 241 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 272
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1577 |
1.11e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 847 QEAQEAIARLEAQHQALVALWHQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQD 926
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 927 AggfgpEDRLQA-EREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQ 1005
Cdd:TIGR02168 370 L-----ESRLEElEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1006 RITEQQKAQAEVDGLGKGVARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLS---AIYLEKLKTISLVIRS 1081
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvKALLKNQSGLSGILGV 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1082 TQEAEEVlrahEEQLKeaQAVPATLPE---------LEATKAALKKLrAQAEAQQPVFDALrDELRGAQEVGERLQQRHG 1152
Cdd:TIGR02168 525 LSELISV----DEGYE--AAIEAALGGrlqavvvenLNAAKKAIAFL-KQNELGRVTFLPL-DSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1153 ERDV-----EVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYR------ESADPLGAWLRDAKQRqeqiQAVP 1221
Cdd:TIGR02168 597 IEGFlgvakDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgDLVRPGGVITGGSAKT----NSSI 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1222 LANSQAVREqLRQEKALLEDIERHGEKveecqrfakqyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYV 1301
Cdd:TIGR02168 673 LERRREIEE-LEEKIEELEEKIAELEK-------------ALAELRKELEELEEELE---------QLRKELEELSRQIS 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1302 DLRTRYSELST---LTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ 1378
Cdd:TIGR02168 730 ALRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1379 ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQR 1452
Cdd:TIGR02168 810 aelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1453 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-LRVQAEAEAAREKQRALQALEELRLQAEE 1531
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237974 1532 AERRLRQAEAERARQVQVALEtaqrsAEAELQSEHASFAEKTAQLE 1577
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLA-----AIEEYEELKERYDFLTAQKE 1010
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1228-1892 |
1.14e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.50 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1228 VREQLRQEKALLEDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQ---LEPVaspakkpkvqsgsESIIQEYVDLR 1304
Cdd:COG4913 213 VREYMLEEPDTFEAADA-----------LVEHFDDLERAHEALEDAREQielLEPI-------------RELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1305 TRYSELSTLTSQY-IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEREAQGLQR 1379
Cdd:COG4913 269 ERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1380 RMQEEVARREEVAVEAQEQKRSI--------------QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1445
Cdd:COG4913 349 RLERELEERERRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1446 EATERQRGGAEGELQALRARAEEAeaqkrqAQEEAERLR-----RQVQDETQRKRQAeAELALRVQA-----EAEAAREK 1515
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA------LGLDEAELPfvgelIEVRPEEERWRGA-IERVLGGFAltllvPPEHYAAA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1516 QRALQALE-ELRLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEAELQSehaSFAEKTAQLERTLKEEHVAV- 1587
Cdd:COG4913 502 LRWVNRLHlRGRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELGR---RFDYVCVDSPEELRRHPRAIt 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1588 --VQLREEATrraqqqaeaERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAE 1664
Cdd:COG4913 579 raGQVKGNGT---------RHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL----------EAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQREAAAATQKRRELEAEL 1741
Cdd:COG4913 640 LDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEI 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1742 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1821
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1822 -KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELER 1892
Cdd:COG4913 796 fNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1083-1583 |
1.17e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1083 QEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfDALRDELRGAQEVGERLQQRHGERDVEVERWR 1162
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1163 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ---AVPLANSQAVREQLRQEKALL 1239
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1240 EDIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1319
Cdd:PRK02224 387 EELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT------ 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1320 fISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAK--AQAEREAQG 1376
Cdd:PRK02224 435 -LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEdlVEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1377 LQRR---MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvRLQLEATERQRG 1453
Cdd:PRK02224 514 LEERredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1454 GAEGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDETQRKRQAEAELAlrvQAEAEAARE-KQRALQALeelrlq 1528
Cdd:PRK02224 592 ERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL------ 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 1529 aEEAERRLRQAEAERARqVQVALETAQRSAE--AELQSEHASFAEKTAQLErTLKEE 1583
Cdd:PRK02224 663 -EQVEEKLDELREERDD-LQAEIGAVENELEelEELRERREALENRVEALE-ALYDE 716
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
38-143 |
1.26e-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: 72.70 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 107
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237974 108 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 143
Cdd:cd21219 72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1323-1814 |
1.67e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.58 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA--QAKAQAEREAQGLQRRMQEEVARREEVAvEAQEQKR 1400
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR-ELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1401 SIQEELQHLRQSSEaeiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1480
Cdd:COG4717 167 ELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1481 ER--LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSA 1558
Cdd:COG4717 237 EAaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1559 EAElqsehasfaektaQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAqq 1638
Cdd:COG4717 317 EEE-------------ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1639 ksltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEE 1718
Cdd:COG4717 382 -----------------------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1719 ELARLQREAAAATQKRRELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAK 1798
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
490
....*....|....*....
gi 1920237974 1799 RQRQLAEED---AVRQRAE 1814
Cdd:COG4717 504 EAREEYREErlpPVLERAS 522
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1043-1796 |
1.78e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.78 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1043 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLkeaqavPATLPELEATKAALKKLRAQ 1122
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCM------PDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1123 AEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEverwrervtllLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdp 1202
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLAAHIK-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1203 lgAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAS 1282
Cdd:TIGR00618 301 --AVTQIEQQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1283 PAKKPKVQSGSESIIQEyvDLRTRYSELSTLTSQYIRFISETLRRMEEEERL--AEQQRAEERERLAEVEAALEKQRQ-- 1358
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQce 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1359 -LAEAHAQAKAQAERE-------AQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA--EIQAKARQVEAAE 1428
Cdd:TIGR00618 455 kLEKIHLQESAQSLKEreqqlqtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1429 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE 1508
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1509 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVV 1588
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1589 QLREEATRRAQQQAEAERARAEAERELERWQLkANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREArrrgkaEEQAV 1668
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE------AHFNN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1669 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKRRELEAELAK 1743
Cdd:TIGR00618 767 NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 1744 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1796
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
161-260 |
1.95e-14 |
|
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: 72.31 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 161 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1920237974 241 VDV--PQPDEKSIITYVSSLYD 260
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
44-144 |
3.09e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.56 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 44 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 115
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1920237974 116 KLVNIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
933-1472 |
3.48e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 933 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRITEQQK 1012
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1013 AQAEVDGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1092
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1093 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERw 1172
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1173 qavlaqtdvRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIERHGEKVEEC 1252
Cdd:COG1196 486 ---------LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1253 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEE 1331
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1332 ERLAEQQRAEERERLAEVEAALEKQRqLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQ 1411
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1412 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1472
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1317-2036 |
3.70e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.01 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1317 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQ 1396
Cdd:TIGR00618 140 YKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1397 EQKRSIQEELQHLR--QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL---RARAEEAEA 1471
Cdd:TIGR00618 219 ERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1472 QKRQAQEEAERLRRQVQ-DETQRKRQAEAELALRVQAEAEAAREKQRALQAL--EELRLQAEEAERRLRQAEAERARQVQ 1548
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1549 VALETAQRSAEAELQSEHASFAEKTaqlertlkeehvavvQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL 1628
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELD---------------ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1629 RLQAEEVAQQKSLTQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQ 1708
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSL--------KEREQQLQTKEQIHLQETRKKAVVL----ARLLELQEEPCPLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1709 GEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLAS----KARAEEESRSTSEKSKQR---------LEA 1775
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDnrskedipnLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1776 EAGRFRELAEEAARLR-ALAEEAKRQ-RQLAEEDAVRQRAEAERVLAEKLAaiSEATRLKTEAEIALKEKEAENERLRRL 1853
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEdMLACEQHALlRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1854 AEDEAFQRRLLEEQAAQHKADieaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1933
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKE---QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1934 RIRGTAEDTLRSKEQAEQEAARQrqlaaeeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2013
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEE----------VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
730 740
....*....|....*....|....
gi 1920237974 2014 QE-SARQLQLAQEAAQKRLQAEEK 2036
Cdd:TIGR00618 817 DIlNLQCETLVQEEEQFLSRLEEK 840
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1135-1914 |
4.63e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 79.73 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1135 DELRGAQEVGERLQQRHGERDvEVERWRERVTLLLERwqaVLAQTDVRQRELEQLGRqlryYREsadplgawLRDAKQRQ 1214
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDE---KRQQLERLRREREKAER----YQA--------LLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1215 EQiqAVPLANSQAVREQLRQEKALLEDIERHGEKVEEcqrfakqyinAIKDYELQLVTYKAQLEPVASPAKKpkvqSGSE 1294
Cdd:TIGR02169 224 EG--YELLKEKEALERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1295 SIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA 1374
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1375 QGLQRRMQEEVARREEVAVEAQEQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGG 1454
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1455 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEEL---RLQA-- 1529
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVlkaSIQGvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1530 ----------EEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFA-----EKTAQLERTLKEEHVA-------- 1586
Cdd:TIGR02169 525 gtvaqlgsvgERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplNKMRDERRDLSILSEDgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1587 --------------------VVQLREEATRRAQQQAEAERA--------------RAEAERELERWQLKAnEALRLRLQA 1632
Cdd:TIGR02169 605 lvefdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPA-ELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1633 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAV---RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1709
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1710 EQQRQLLEEELARLQreAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAAR 1789
Cdd:TIGR02169 764 EARIEELEEDLHKLE--EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1790 LRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA 1869
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1870 QHKADIEA---RLAQLRKASESELERQKGL--VEDTLRQRRQVEEEILAL 1914
Cdd:TIGR02169 921 ELKAKLEAleeELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
159-256 |
5.10e-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: 70.87 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 234
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1920237974 235 LLDPEDVDVPQPDEKSIITYVS 256
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
161-264 |
5.18e-14 |
|
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: 71.23 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 161 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1920237974 241 VDV--PQPDEKSIITYVSSLYDAMPR 264
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
164-259 |
6.05e-14 |
|
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: 70.85 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 164 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 242
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1920237974 243 VPQPDEKSIITYVSSLY 259
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1310-2221 |
7.76e-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: 78.68 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1310 LSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAQGLQRRMQEEV 1385
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1386 ARREEvaveAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1465
Cdd:pfam01576 257 AQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1466 AE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaeaEAAREKQRALQALEELRlQAEEAERRLRQAEAERA 1544
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1545 RQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1624
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1625 ALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1704
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1705 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK-------VRAEMEVLLAS-------------------KARA 1758
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1759 EEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---ISEATRLKT 1834
Cdd:pfam01576 612 EEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVgknVHELERSKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1835 EAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADIEARlaqlrkaSESELERQKGLVedtlRQRRQVEEE 1910
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDLQAR-------DEQGEEKRRQLV----KQVRELEAE 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1911 ILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1990
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1991 ALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSVLERLRSEAE 2068
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2069 AARR---AAEEAEAARERAEREAAQSRRQVEEAeRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2145
Cdd:pfam01576 918 QVEQlttELAAERSTSQKSESARQQLERQNKEL-KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2146 AADAE---------MEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2216
Cdd:pfam01576 997 VRRTEkklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVST 1076
|
....*
gi 1920237974 2217 LRVQM 2221
Cdd:pfam01576 1077 LKSKL 1081
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3707-3745 |
1.15e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.74 E-value: 1.15e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3707 LLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPELHDRL 3745
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1059-1562 |
1.17e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1059 EQVRSLSAI--YLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPatlpELEATKAALKKLRAQAEAQQPVFDALRDE 1136
Cdd:COG4913 249 EQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEA----ELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1137 LRGAQEV-----GERLQQRhgERDVE-VERWRERVTLLLERWQAVLAQTDVR---------------QRELEQLGRQLRY 1195
Cdd:COG4913 325 LDELEAQirgngGDRLEQL--EREIErLERELEERERRRARLEALLAALGLPlpasaeefaalraeaAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1196 YRESADPLGAWLRDAKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IE 1243
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1244 R--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQS------GSESIIQEYVD--LRTRY 1307
Cdd:COG4913 482 RvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSlagkldFKPHPFRAWLEaeLGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1308 S--------ELST----LTSQYIRFISETLRRMEEEERL---------AEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1366
Cdd:COG4913 560 DyvcvdspeELRRhpraITRAGQVKGNGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1367 KAQAEREAQGLQRRmqEEVARREEVAVEAQEQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQLE 1446
Cdd:COG4913 640 LDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1447 ATERQRGGAEGELQALRARAEEAE------------------AQKRQAQEEAERLRRQVQDETQRKRQAEAEL------- 1501
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaaLGDAVERELRENLEERIDALRARLNRAEEELeramraf 796
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1502 -------ALRVQAEAEAAREKQRALQALEELRL---QAEEAERRLRQAEAERArQVQVALETAQRSAEAEL 1562
Cdd:COG4913 797 nrewpaeTADLDADLESLPEYLALLDRLEEDGLpeyEERFKELLNENSIEFVA-DLLSKLRRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1619-2479 |
1.91e-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: 77.42 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1619 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1694
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1695 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1772
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1773 LEAEAGRFRELAEEAARLRALAEEAKRQRQlaeedavrQRAEAERVLAEKLAAISEatrLKTEAEIALKEKEAENERLRR 1852
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSE--------ELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1853 LAED-EAFQRRLLEEQAAQhkADIEARLAQLRKaSESELERQKGLVEDTLRQRRQVEEeilalkgsfekaaagkaELELE 1931
Cdd:TIGR02169 460 LAADlSKYEQELYDLKEEY--DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEE-----------------VLKAS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1932 LGRIRGTAEDTLRSKEQ---AEQEAARQRqlaaeeerrrrEAEERVQKSLAAEE--EAARQRK---AALEEVERLKAKVE 2003
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERyatAIEVAAGNR-----------LNNVVVEDDAVAKEaiELLKRRKagrATFLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2004 EARRLRERAEQESARQLqlaQEAAQKRlqaeEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2083
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDL---VEFDPKY----EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2084 AEREAAQSRRQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2160
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2161 ALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQveEELFSLRVQMEELGKLKARIEAENRALvl 2240
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREI-- 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2241 rDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQK 2320
Cdd:TIGR02169 818 -EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKER 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2321 ELAQEQARRLQEDKEQMAQQlaqetqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfRKQAEDIGER 2400
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAE 959
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2401 LYRTELAtqekvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSF 2479
Cdd:TIGR02169 960 LQRVEEE-------IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENF 1031
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1050-1572 |
1.91e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1050 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEvLRAHEEQLKEAQAvpaTLPELEATKAALKKLRAQAEAQQpv 1129
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE-LARLEAELERLEA---RLDALREELDELEAQIRGNGGDR-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1130 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLRD 1209
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1210 AKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IER--HGEK----VEE 1251
Cdd:COG4913 417 LRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIERvlGGFAltllVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1252 cQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsiiqeyvdlrtrysELSTLTSQYIRFISETLRRM- 1328
Cdd:COG4913 496 -EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRf 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1329 -----EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAEREAQGLQRRMQEEVARREEVAvE 1394
Cdd:COG4913 560 dyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-A 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1395 AQEQKRSIQEELQHLRQSSEAEIQakarqVEAAERSRLRIEEEIRvvrlQLEAterqrggAEGELQALRARAEEAEAQKR 1474
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1475 QAQEEAERLRRQVQDETQRKRQAEAEL-ALRVQAEAEAAREKQRALQALEELRlqAEEAERRLRQAEAERARQVQVALET 1553
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRA 780
|
570
....*....|....*....
gi 1920237974 1554 AQRSAEAELQSEHASFAEK 1572
Cdd:COG4913 781 RLNRAEEELERAMRAFNRE 799
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1700-2513 |
2.76e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.93 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1700 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEAea 1777
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLMN-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1778 grfrelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAErvlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1857
Cdd:TIGR00618 172 ------LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1858 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEeilalkgsfeKAAAGKAELELELGRIRG 1937
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1938 TAEdtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2017
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2018 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2097
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2098 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2177
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2178 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLkarIEAENRAlvlrdKDSAQRLLQEEAEKm 2257
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEA-----EDMLACEQHALLRK- 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2258 KQVAEEAARLSVAAQEAARLRQLAEEDLAQqraLAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA--RRLQEDKE 2335
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSekEQLTYWKE 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2336 QMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEdigERLYRTELATQEKVMLV 2415
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK---ARTEAHFNNNEEVTAAL 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2416 QTLeTQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQ 2495
Cdd:TIGR00618 775 QTG-AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
810
....*....|....*...
gi 1920237974 2496 EKAKLEQlfQDEVAKAQA 2513
Cdd:TIGR00618 854 YEECSKQ--LAQLTQEQA 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2141-2600 |
3.43e-13 |
|
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: 76.63 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2220
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2221 MEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2300
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2301 QAVQEATRLKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2379
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2380 QARAEEDARRFRKQAEDIGERLYRTE-----------------------------LATQEKV------------------ 2412
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVdegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2413 MLVQTLETQRQ--QSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE-----------------------MQTVRQEQ 2467
Cdd:TIGR02168 550 VVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2468 LLQETQALQ------------------------QSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQ 2523
Cdd:TIGR02168 630 DLDNALELAkklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 2524 QMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2600
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1340-2446 |
4.04e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.53 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1340 AEERERLaeVEAALEKQRQLAEAHAQAKAQAEReaqglqrrmQEEVARREEvavEAQEQKRSIQEELQ----HLRQSSEA 1415
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAEQYR---------LVEMARELA---ELNEAESDLEQDYQaasdHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1416 EIQAKA--RQVEAAERSRLRIEEEIRVVRlqlEATERQrggaegelqalraraEEAEAQKRQAQEEAERLRRQVQDETQr 1493
Cdd:PRK04863 344 LRQQEKieRYQADLEELEERLEEQNEVVE---EADEQQ---------------EENEARAEAAEEEVDELKSQLADYQQ- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1494 krqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVALETAQRSAEAElqsEH 1566
Cdd:PRK04863 405 --------ALDVQQTR--AIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ---AA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1567 ASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALRlrlqaeevaqqksltqaea 1646
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVS-----RSEA-----------------------WD-VARELLR------------------- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1647 ekqkeeaerearrrgkaeeQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1726
Cdd:PRK04863 504 -------------------RLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1727 AAAAtqkRRELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1806
Cdd:PRK04863 563 LEAR---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1807 dAVRQRAEAERVLAEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAEDeaFQRRLLEEQ----AAQHKADIEARLAQ 1881
Cdd:PRK04863 632 -YMQQLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER--FGGVLLSEIyddvSLEDAPYFSALYGP 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1882 LRKASeseLERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG--KAElELELGRIRGTAEDTLR-SKEQAEQ---EAAR 1955
Cdd:PRK04863 709 ARHAI---VVPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSvfSVE-ELEKAVVVKIADRQWRySRFPEVPlfgRAAR 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1956 QRQLaaeeerrrreaeervqkslaaeEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLA---------QEA 2026
Cdd:PRK04863 785 EKRI----------------------EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeaelRQL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2027 AQKRLQAEEKahafavqqkeqelqqtlqqeqsvLERLRSeaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSae 2106
Cdd:PRK04863 843 NRRRVELERA-----------------------LADHES---------------------QEQQQRSQLEQAKEGLSA-- 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2107 eqaqaqaqaqaaaekLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRlqleeTDhqk 2186
Cdd:PRK04863 877 ---------------LNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ-----SD--- 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2187 silDEELQRLKAEVTEAARQRGQVEEELFSLrvqmEELGKLKARIEAENRALVLRDKDSAQRLLQ---EEAEKMKQVAEE 2263
Cdd:PRK04863 934 ---PEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRARE 1006
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2264 AARlsvaaQEAARLRQLAE--EDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAE-LLQQQKELAQEQARRLQEDKEQMAQ 2339
Cdd:PRK04863 1007 QLR-----QAQAQLAQYNQvlASLKSSYDAKRQMLQELKQELQDLGvPADSGAEeRARARRDELHARLSANRSRRNQLEK 1081
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2340 QLaqetqgfqkTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEkvmlvqtLE 2419
Cdd:PRK04863 1082 QL---------TFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLS-------AD 1145
|
1130 1140
....*....|....*....|....*..
gi 1920237974 2420 TQRQQSDRDAERLREAIAELEHEKDKL 2446
Cdd:PRK04863 1146 ELRSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1106-1565 |
5.96e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1106 LPELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTL--LLERWQAVLAQTDVRQ 1183
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1184 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQekaLLEDIERHGEKVEECQRFAKQYINAI 1263
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1264 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESII-------QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE--EE 1332
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1333 RLAEQQRAEERERL--AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKrsIQEELQHLR 1410
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1411 QSSEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1488
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1489 DETQRKRQAEAElalrvqaeaeaarekqralQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEAELQSE 1565
Cdd:COG4717 457 ELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYREERLPP 516
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
161-256 |
6.81e-13 |
|
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: 67.80 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 161 KEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 239
Cdd:cd21229 5 KKLMLAWLQAVLPEL---KITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1920237974 240 DVDVPQPDEKSIITYVS 256
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
62-141 |
7.78e-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: 67.62 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 62 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 133
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1920237974 134 LGLIWTII 141
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3041-3079 |
8.13e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.04 E-value: 8.13e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3041 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPELHEKL 3079
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
161-262 |
9.24e-13 |
|
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: 67.80 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 161 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1920237974 241 -VDVPQPDEKSIITYVSSLYDAM 262
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
159-259 |
1.19e-12 |
|
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: 67.41 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 238
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1920237974 239 ED-VDVPQPDEKSIITYVSSLY 259
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1309-1526 |
1.19e-12 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 73.75 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1309 ELSTLTSQYIR-----FISETLRRMEEEERLAEQQRAEeRERLAEVEAAlEKQRQLAEAHAQAKAQAER----EAQGLQR 1379
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREIETariaEAEAELA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1380 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLEATERQRGGAEGEL 1459
Cdd:COG2268 248 KKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKPAEAEKQA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 1460 QALRARAeEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR 1526
Cdd:COG2268 321 AEAEAEA-EAEAIRAKGLAEAEGKRALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2142-2673 |
1.28e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2142 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV-Q 2220
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2221 MEELGKLKA--RIEAENRALVLRDKDSAQRllQEEAEKMKQV--AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2296
Cdd:PTZ00121 1190 AEELRKAEDarKAEAARKAEEERKAEEARK--AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2297 KEKMQAVQEATrlKAEaELLQQQKELAQEQARRLQEDKEqmAQQLAQETQGFQKTLETERQRQlEMSAEAERLRLRVAEM 2376
Cdd:PTZ00121 1268 RQAAIKAEEAR--KAD-ELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAE-EAKKKADAAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2377 SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLEtQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlK 2456
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-K 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2457 SEEMQTvRQEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQ--DEVAKAQALREEQQRqqqqmqqekqqlAA 2534
Cdd:PTZ00121 1420 ADEAKK-KAEEKKKADEAKKKAEEAKKADEAKKK---AEEAKKAEEAKKkaEEAKKADEAKKKAEE------------AK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2535 SMEEARRRQHEAeegvRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR-SEEIAPSRA-AAARALPN 2612
Cdd:PTZ00121 1484 KADEAKKKAEEA----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkAEEKKKADElKKAEELKK 1559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 2613 GQDAADGPAAAAEPEHAFDGLRR-----KVPAQRLQEVGVL-------SAEELQQLAQGRTTVAELAQREDVR 2673
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLyeeekkmKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1084-1580 |
1.29e-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: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1084 EAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELrgAQEVGERLQQRHGERDVEVERWRE 1163
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1164 RVTLLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDI 1242
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1243 ERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFIS 1322
Cdd:COG4913 397 EEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAEREAQGLQRRM- 1381
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1382 ----------QEEVARREEVA-VEAQEQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKARQVEA 1426
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1427 AERSRLRIEEEIRVVRLQLEATERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDETQRK 1494
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1495 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEAELQSEHASFAEK 1572
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 1920237974 1573 TAQLERTL 1580
Cdd:COG4913 782 LNRAEEEL 789
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1326-1828 |
1.55e-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: 74.60 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1326 RRMEEEERLAEQQRAEERERLAE----VEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRS 1401
Cdd:COG3096 242 RMTLEAIRVTQSDRDLFKHLITEatnyVAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1402 iQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQE 1478
Cdd:COG3096 322 -ESDLEQDYQAASdhlNLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1479 EAERLRRQVQDETQrkrqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVAL 1551
Cdd:COG3096 390 EVDSLKSQLADYQQ---------ALDVQQTR--AIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1552 ETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALR---- 1627
Cdd:COG3096 459 ELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQA-----------------------WQ-TARELLRryrs 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1628 LRLQAEEVAQQKSltqaeaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETE 1707
Cdd:COG3096 507 QQALAQRLQQLRA------------------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1708 QGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEA 1777
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLERER 640
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1778 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1828
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEIYD 691
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
46-147 |
1.92e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 66.88 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 46 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1327-2451 |
1.98e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.06 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1327 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHAQAKAQAEREAqglqrrmqEEVARREEVAVEAQEQKRSI 1402
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNALQEQLQAET--------ELCAEAEEMRARLAARKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1403 QEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAER 1482
Cdd:pfam01576 74 EEILHEL----ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR-------QKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1483 LRRQVQDETQRKRQAE---AELALRVQAEAEAA------REKQRALQALEELRLQAEEAERRlrqaEAERARQVQVALET 1553
Cdd:pfam01576 143 LEDQNSKLSKERKLLEeriSEFTSNLAEEEEKAkslsklKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1554 AQRSAEAELQsehASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKANEALRLRLQaE 1633
Cdd:pfam01576 219 DLQEQIAELQ---AQIAELRAQLAKKEEELQAALARLEEETAQKNNALK----------------KIRELEAQISELQ-E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1634 EVAQQKSltqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGT-----AQQRLAA--EQELIRLR--- 1703
Cdd:pfam01576 279 DLESERA----------------------ARNKAEKQRRDLGEELEALKTELEDTldttaAQQELRSkrEQEVTELKkal 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1704 -AETEQGEQQRQ-----------LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQ 1771
Cdd:pfam01576 337 eEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK-RKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1772 RLEA---EAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERV---LAEKLAAISEATRLKTEAEIALKEKE 1844
Cdd:pfam01576 416 ELQArlsESERQRaELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqLQDTQELLQEETRQKLNLSTRLRQLE 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1845 AENERLRRLAEDEAFQRRLLEEQAAQHkadiEARLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKGSFEKAAAG 1924
Cdd:pfam01576 496 DERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1925 KAELELELGRIRGTAEDTLRSKEQaeqeaarQRQLAAEEERRRREAEErvqksLAAEEEAARQRKAALEEVERLKAKVEE 2004
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDH-------QRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKE 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2005 ARRLRERAEQESARQLQLAQEAAQKRLQAEekahafavqqkeqelqqtlqqeqsvLERLRSEAEAARRAAEEAEAARERA 2084
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRAL 690
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2085 EREAAQSRRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKQfaeQALRQ 2164
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQ 750
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2165 KAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKD 2244
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2245 SAQRLLQEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2324
Cdd:pfam01576 831 SEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2325 EQARRLQEDKEQMAQQLAQETQGFQKtLETERQrqlEMSAEAERLRLRVAEMSRAQ---------------ARAEEDARR 2389
Cdd:pfam01576 910 DRLRKSTLQVEQLTTELAAERSTSQK-SESARQ---QLERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLEEQLEQ 985
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2390 FRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQ 2451
Cdd:pfam01576 986 ESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1457-2035 |
2.43e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1457 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELALRVQAEAEAAREKQRALQALEELRLQAEEA--ER 1534
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1535 RLRQAEAERARQVQVALETA---QRSAEAELQSEHASFAEKTAQLERTLKEehvavvqLREEATRRAQQQAEAERARAEA 1611
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1612 ERELERWQlKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELA---EQELEKQRQLAEGT 1688
Cdd:PRK02224 313 EARREELE-DRDEELRDRLEECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1689 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR---AEMEVLLA------------ 1753
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1754 --SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAVRQRAEAERVLAEKLAAISEA 1829
Cdd:PRK02224 463 gsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1830 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE---------ARLAQLRKASESELERQKGLVE-- 1898
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAEln 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1899 ----DTLRQRRqveEEILALKGSFEKAAAGKAELELElgrirgTAEDTLRSKEQAEQEAARQRqlaaeeerrrreaeERV 1974
Cdd:PRK02224 623 derrERLAEKR---ERKRELEAEFDEARIEEAREDKE------RAEEYLEQVEEKLDELREER--------------DDL 679
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1975 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2035
Cdd:PRK02224 680 QAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3783-3821 |
3.13e-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: 3.13e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3783 LLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDTHDQL 3821
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3372-3410 |
4.81e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.81e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3372 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3410
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4295-4333 |
4.95e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.95e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 4295 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4333
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
161-260 |
5.94e-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: 65.05 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 161 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 236
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1920237974 237 DPEDVdVPQPDEKSIITYVSSLYD 260
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1662-1883 |
7.08e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.56 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1741
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1742 AKVRAE----------------MEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1804
Cdd:COG4942 100 EAQKEElaellralyrlgrqppLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1805 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeafqrRLLEEQAAQHKADIEARLAQLR 1883
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------RLEAEAAAAAERTPAAGFAALK 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2159-2483 |
7.75e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 72.08 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2159 EQALRQKAQVEQELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSL--RVQMEELGKLK-------A 2229
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2230 RIEAENRALVLRDKDSAQRLLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2309
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2310 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARR 2389
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2390 fRKQAEDIGERLYRTELATQEKVM--------LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2461
Cdd:pfam17380 486 -RKRAEEQRRKILEKELEERKQAMieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
330 340
....*....|....*....|..
gi 1920237974 2462 TVRQEQLLQETQALQQSFLSEK 2483
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEK 586
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1860-2600 |
8.54e-12 |
|
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: 72.31 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1860 QRRLLEEQAA---QHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1936
Cdd:pfam02463 153 ERRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1937 GTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQES 2016
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2017 ARQLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRR 2093
Cdd:pfam02463 313 EEKLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2094 QVEEAErlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELT 2173
Cdd:pfam02463 393 KEEELE--LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2174 ALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE 2253
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2254 AEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqralaekmlkekmqavqeaTRLKAEAELLQQQKELAQEQARRLQED 2333
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARK------------------------LRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2334 KEQMAQQLAQETQGFQKTLETERQRQLEMSaeaERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVM 2413
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2414 LVQTLETQRQQSdrdaERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCI 2493
Cdd:pfam02463 684 KAESELAKEEIL----RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2494 EQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGvrrQQEELQRLAQQQQQQEKLLAE 2573
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELE 836
|
730 740
....*....|....*....|....*..
gi 1920237974 2574 ENQRLRERLQHLEEERRAALARSEEIA 2600
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEI 863
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1001-1586 |
8.76e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.29 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1001 RECAQRITEQQKAQAEVDGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEqvrslsaiylEKLKTISLVIR 1080
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELE----------AQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1081 STQEAEEVLRAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpvFDALRDELRGAQEVGERLQQRHGERDvEVE 1159
Cdd:COG3096 575 EAVEQRSELRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA---LADSQEVTAAMQQLLEREREATVERD-ELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1160 RWRERVTLLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLGAWLRDAKQrqeqiqAVPLANSQAVREQL 1232
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPARH------AIVVPDLSAVKEQL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1233 RQEKALLED---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKVQSGSESIIQEYVDL 1303
Cdd:COG3096 725 AGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEELRAERDELAEQYAKA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1304 RTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQE 1383
Cdd:COG3096 805 SFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLKEQLQLLNKLLP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1384 EV---------ARREEVAVE---AQEQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE 1449
Cdd:COG3096 882 QAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1450 --RQR------GGAEGEL-------QALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE 1514
Cdd:COG3096 962 evVQRrphfsyEDAVGLLgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE 1041
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1515 -KQRALQALEELRLQAEEaERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF--AEKTAQLERTLKEEHVA 1586
Cdd:COG3096 1042 lEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrkAERDYKQEREQVVQAKA 1115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3950-3988 |
1.14e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.14e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3950 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3988
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3117-3155 |
1.26e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.26e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3117 LLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKETSAAL 3155
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1358-1728 |
1.36e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 71.31 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1358 QLAEAHAQAKAQAEREAQGLQRRMQEEVARREevaveaqeqKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1430
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---------KEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1431 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQ-AEA 1509
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1510 EAAREKQRALQALEELRLQAEEA-ERRLRQAEAERARQVQ-VALETAQRSAEAE-LQSEHASFAEKTAQLERTLKEEHVA 1586
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMErVRLEEQERQQQVErLRQQEEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1587 VVQLREeatrraqqqaeaeraraeaereLERWQLKANEalrlRLQAEEVAQQKSLTQAEAEKQKEEAEREARRrgKAEEQ 1666
Cdd:pfam17380 490 EEQRRK----------------------ILEKELEERK----QAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1667 AVRQrelaeQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1728
Cdd:pfam17380 542 RRKQ-----QEMEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
159-259 |
1.63e-11 |
|
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: 63.90 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 238
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1920237974 239 ED-VDVPQPDEKSIITYVSSLY 259
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2185-2592 |
1.66e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2185 QKSILDEELQRLKAEVTEAARQRG---QVEEELFSLRVQMEELGKLKARIEAENRAL--------VLRDKDSAQRLLQEE 2253
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLekllqllpLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2254 AEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2333
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2334 KEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEED---------------ARRFRKQAEDIG 2398
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2399 ERLYRTELATQEkvmlvQTLETQRQQSDRDAERLREAI--AELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL- 2475
Cdd:COG4717 302 KEAEELQALPAL-----EELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALl 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2476 QQSFLSEKDSLLQRERCIEQEKAKLEQLfqdEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2555
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237974 2556 ELQRLAQQQQQQEK-----LLAEENQRLRERLQHLEEERRAA 2592
Cdd:COG4717 454 ELAELEAELEQLEEdgelaELLQELEELKAELRELAEEWAAL 495
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1297-1795 |
1.85e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.14 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1297 IQEYVDLRTRYSELSTLTSQYirFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqg 1376
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARES-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1377 lqrrmqeevarreevAVEAQEQKRSiqeelQHLrqsseAEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAE 1456
Cdd:COG3096 324 ---------------DLEQDYQAAS-----DHL-----NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1457 GELqalraraEEAEAQKRQAQEEAERLRRQVQDETQrkrqaeaelALRVQaeAEAAREKQRALQALEELR-------LQA 1529
Cdd:COG3096 375 EQL-------AEAEARLEAAEEEVDSLKSQLADYQQ---------ALDVQ--QTRAIQYQQAVQALEKARalcglpdLTP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1530 EEAERRLRQAEAERARQVQVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEATRRAQQQAEAERARA 1609
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQAWQTARELLRRYRSQQ 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1610 EAERELERWQLKANEA-LRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGT 1688
Cdd:COG3096 509 ALAQRLQQLRAQLAELeQRLRQQQNAERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEEL 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1689 AQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRRELEAE----LAKVRAEMEVLLaSKARAEEESRS 1764
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKEL-AARAPAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERD 647
|
490 500 510
....*....|....*....|....*....|....*
gi 1920237974 1765 TSEKSKQRLEAEAgrfRELA----EEAARLRALAE 1795
Cdd:COG3096 648 ELAARKQALESQI---ERLSqpggAEDPRLLALAE 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1391-1594 |
1.92e-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: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1391 VAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1470
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1471 AQKRQAQEEAERLRRQVQDET----QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEA 1541
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 1542 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1594
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
602-780 |
2.04e-11 |
|
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: 66.70 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 602 LHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQ 681
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 682 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTATRLEDLLQDAQDEKEQLSEY 761
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 1920237974 762 RGHLSGLAKRAKAIVQLKP 780
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1070-1955 |
2.12e-11 |
|
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: 70.77 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1070 EKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfdalrdelrgaqevgerlqq 1149
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----------------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1150 rhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplgawlrDAKQRQEQIQAVPLANSQAVR 1229
Cdd:pfam02463 231 ---YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE--------KEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1230 EQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsesiIQEYVDLRTRYSE 1309
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-----EKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1310 LSTLTSQYIRFISETLRRMEEEERLA-----EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEE 1384
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKseeekEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1385 VARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR-IEEEIRVVRLQLEATERQRGGAEGELQALR 1463
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1464 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ-AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1542
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVrALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1543 RARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERELERWQLKA 1622
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE----GLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1623 NEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1702
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1703 RAETEQGEQQRQLLEEELARLQREAAAATQKrrELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1782
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEE--ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1783 LAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 1862
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1863 LLEEQAAQHKADIEARLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDT 1942
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEE---RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 1920237974 1943 LRSKEQAEQEAAR 1955
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1499-2035 |
2.28e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 70.66 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1499 AELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEAELQSEHAS--------F 1569
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppaS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1570 AEKTAQLERTLKEEHVAVVQLREEATRRAQQ--QAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQkslTQAEAE 1647
Cdd:COG3899 792 ARAYANLGLLLLGDYEEAYEFGELALALAERlgDRRLEARALFNLGFILHWLGPLREALELLREALEAGLE---TGDAAL 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1648 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA 1727
Cdd:COG3899 869 ALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1728 AAATQKRRELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1807
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1808 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1887
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1888 SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRR 1967
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1968 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2035
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1672-2592 |
2.39e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.59 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1672 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeME 1749
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1750 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDavrqraeaervLAEKLAAISEA 1829
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1830 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRrlleEQAAQHKADIEARLAQLRKASESELERQKGLVEdtLRQRRqvEE 1909
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKTELEDTLDTTAAQQE--LRSKR--EQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1910 EILALKGSFEKAAAGKAELELELGRIRGTAEDTLrsKEQAEQeAARQRQLAAEEERRRREAEERVQKSL----AAEEEAA 1985
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEEL--TEQLEQ-AKRNKANLEKAKQALESENAELQAELrtlqQAKQDSE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1986 RQRKAALEEVERLKAKVEEARRLRERAEQESARqLQLAQEAAQKRLQAEEKahafavqqKEQELQQTLQQEQSVLERLRS 2065
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSSLLNEAEG--------KNIKLSKDVSSLESQLQDTQE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2066 EAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2145
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2146 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLeetDHQKSILDEELQRLKAEVTEAArqrgqvEEELFSLRVQMEelg 2225
Cdd:pfam01576 556 ALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVSNLEKKQKKFDQMLA------EEKAISARYAEE--- 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2226 klKARIEAENRalvlrDKDSAQRLLQEEAEKMKQVAEEAARlsvaaqeAARLRQLAEEDLAQQRALAEKMLKE----KMQ 2301
Cdd:pfam01576 624 --RDRAEAEAR-----EKETRALSLARALEEALEAKEELER-------TNKQLRAEMEDLVSSKDDVGKNVHElersKRA 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2302 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLEtERQRQL-----EMSAEAERLRLRVAEM 2376
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvkqvrELEAELEDERKQRAQA 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2377 SRAQARAEEDARRFRKQAEDIGERlyRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLK 2456
Cdd:pfam01576 769 VAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQ 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2457 SEEMQTVRQE-QLLQETQALQQ---SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQL 2532
Cdd:pfam01576 847 EDLAASERARrQAQQERDELADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2533 AAS---------------------------MEEARRRQHEA-----EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRE 2580
Cdd:pfam01576 927 AAErstsqksesarqqlerqnkelkaklqeMEGTVKSKFKSsiaalEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
970
....*....|..
gi 1920237974 2581 RLQHLEEERRAA 2592
Cdd:pfam01576 1007 VLLQVEDERRHA 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1703-2019 |
2.44e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.15 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1703 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElAKVRAEMEVLLASKARAEEESRSTSEKSkqrlEAEAGRFRE 1782
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKR----ELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1783 LAEEAARLRALaEEAKRQRQLAEEdAVRQRAEAERV--LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA-- 1858
Cdd:pfam17380 370 IAMEISRMREL-ERLQMERQQKNE-RVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAre 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1859 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKglvedtlRQRRQVEEEilaLKGSFEKAAAGKAELELELGRIRGT 1938
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQ---RRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1939 AEDTLRSKEQAEQEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2018
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE---------AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 1920237974 2019 Q 2019
Cdd:pfam17380 589 A 589
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1410-2035 |
3.08e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.25 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1410 RQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1483
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1484 RRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAeLQ 1563
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1564 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAerelerwqlkANEALRLRLQAEEVAQQKSLTQ 1643
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED----------DLQALESELREQLEAGKLEFNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1644 AEAEKQKEEAEREARRRG-KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1722
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQaTATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1723 LQREAAAATQ----KRRELEAELAKVRAEMEVLLASKARAEEESRS------TSEKSKQRLEAEAGRFRELAEEAARLRA 1792
Cdd:pfam12128 518 RQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTdldpevWDGSVGGELNLYGVKLDLKRIDVPEWAA 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1793 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1872
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1873 A-------DIEARLAQLRKASESELERQKG---------------LVEDTLRQRRQVEEEILALKGSFE----------- 1919
Cdd:pfam12128 678 DsanerlnSLEAQLKQLDKKHQAWLEEQKEqkreartekqaywqvVEGALDAQLALLKAAIAARRSGAKaelkaletwyk 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1920 --------------KAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 1985
Cdd:pfam12128 758 rdlaslgvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADT 837
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1986 RQRKAALEevERLKAKVEEARRLRE-----RAEQESARQLQLAQEAAQKRLQAEE 2035
Cdd:pfam12128 838 KLRRAKLE--MERKASEKQQVRLSEnlrglRCEMSKLATLKEDANSEQAQGSIGE 890
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2713-2751 |
3.36e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.42 E-value: 3.36e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 2713 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPELHHKL 2751
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1380-2478 |
3.58e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.20 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1380 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEA--AERSRLRIEEEIRvVRLQLEATErqrggAEG 1457
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqAETELCAEAEEMR-ARLAARKQE-----LEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1458 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDetqrkrqAEAELalrvqAEAEAAREKqralqaleeLRLQAEEAERRLR 1537
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQD-------LEEQL-----DEEEAARQK---------LQLEKVTTEAKIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1538 QAEAErarqvqVALETAQRSaeaELQSEHASFAEKTAQLERTLKEEHVAVVQL-----REEATRRAQQQAEAERARAEAE 1612
Cdd:pfam01576 135 KLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAKSLsklknKHEAMISDLEERLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1613 RELERWQLKAnEALRLRlqaEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1692
Cdd:pfam01576 206 LEKAKRKLEG-ESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE--LQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1693 LAAEqelirlRAETEQGEQQRQLLEEELARLQRE---AAAATQKRRELEAelakvRAEMEVLLASKArAEEESRSTSEKS 1769
Cdd:pfam01576 280 LESE------RAARNKAEKQRRDLGEELEALKTEledTLDTTAAQQELRS-----KREQEVTELKKA-LEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1770 KQRLEAEAGRFRELAEE---AARLRALAEEAK--------------RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1832
Cdd:pfam01576 348 QEMRQKHTQALEELTEQleqAKRNKANLEKAKqalesenaelqaelRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1833 KTEAEIALKEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASE--SELERQKGLVEDTLrqrRQVEEE 1910
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNE-------AEGKNIKLSKDVSSLESQLQDTQEllQEETRQKLNLSTRL---RQLEDE 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1911 ILALKGSFEKAAAGKAELELELGRIRGTAEDTlrsKEQAEQEAARQRQLaaeeerrrreaeERVQKSLAAEEEAARQRka 1990
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM---KKKLEEDAGTLEAL------------EEGKKRLQRELEALTQQ-- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1991 aLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKA-HAFAVQQKEQELQQTLQQEQSVL 2060
Cdd:pfam01576 561 -LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKAiSARYAEERDRAEAEAREKETRAL 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2061 ERLRSeaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAA 2140
Cdd:pfam01576 640 SLARA----------------------LEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQaadaEMEKHKQFAEQA-LR-------QKAQVEQELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQvee 2212
Cdd:pfam01576 698 KTQLE----ELEDELQATEDAkLRlevnmqaLKAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERKQRAQ--- 767
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2213 eLFSLRVQME-ELGKLKARIEAENRAlvlrdKDSAQRLLQEEAEKMKQVAeeaarlsvaaqeaarlRQLAEEDLAQQRAL 2291
Cdd:pfam01576 768 -AVAAKKKLElDLKELEAQIDAANKG-----REEAVKQLKKLQAQMKDLQ----------------RELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2292 AEKMLKEKmqavqeatRLKA-EAELLQQQKELA-QEQARR-LQEDKEQMAQQLAQETQGfqKTLETERQRQLEmsaeaER 2368
Cdd:pfam01576 826 AQSKESEK--------KLKNlEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE-----AR 890
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2369 LRLRVAEMSRAQARAEEDARRFRKQAEDIgERLyRTELATQEKvmLVQTLETQRQQSDRDAERLREAIAELEHE-KDKLK 2447
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQV-EQL-TTELAAERS--TSQKSESARQQLERQNKELKAKLQEMEGTvKSKFK 966
|
1130 1140 1150
....*....|....*....|....*....|.
gi 1920237974 2448 QEAQLLQLKSEEMqtvrQEQLLQETQALQQS 2478
Cdd:pfam01576 967 SSIAALEAKIAQL----EEQLEQESRERQAA 993
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2147-2503 |
3.74e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2147 ADAEMEKHKQFAEQA--LRQKA-QVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE 2223
Cdd:PRK02224 344 AESLREDADDLEERAeeLREEAaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2224 LGKLKARIEAENRALVLRDKDsAQRLLQE-EAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKM 2300
Cdd:PRK02224 424 LREREAELEATLRTARERVEE-AEALLEAgKCPECGQPVEGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERAE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2301 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSraQ 2380
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN--S 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2381 ARAEEDARrfRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERL---REAIAELEHEKDklkqEAQLLQLKS 2457
Cdd:PRK02224 580 KLAELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekRERKRELEAEFD----EARIEEARE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1920237974 2458 EEMQTVR-QEQLLQETQALQQsflsEKDSLLQRERCIEQEKAKLEQL 2503
Cdd:PRK02224 654 DKERAEEyLEQVEEKLDELRE----ERDDLQAEIGAVENELEELEEL 696
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1343-1868 |
4.94e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.50 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1343 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1422
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1423 QVEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1499
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1500 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1579
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1580 LKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARR 1659
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1660 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA 1739
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1740 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1819
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920237974 1820 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQA 1868
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2142-2344 |
6.16e-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: 67.87 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2142 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2221
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2222 EELGK---LKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2298
Cdd:COG4942 114 YRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237974 2299 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2344
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
39-138 |
8.08e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 62.06 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 110
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1920237974 111 RHRQVKLVNIRNDDIADGNPKLTLGLIW 138
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
981-1536 |
9.15e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 981 EACETRTVHRLRLPLDKEPARECAQRITEQQKAqaevDGLGKGV--ARLSAEAEKVLAlPEPSPAAPTLRSELELTLGKL 1058
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAeeAKKKADAAKKKA-EEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1059 EQVRSLS-AIYLEKLKTISLVIRSTQEAEEVLRAhEEQLKEAQAVPATLPELEATKAALKK---LRAQAEAQQPVfdalr 1134
Cdd:PTZ00121 1360 EAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKA----- 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1135 DELRGAQEvgERLQQRHGERDVEVERWRERVTLLLERwqavlaqtdvrQRELEQLGRQLRYYREsADPLGAWLRDAKQRQ 1214
Cdd:PTZ00121 1434 DEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEE-----------AKKADEAKKKAEEAKK-ADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1215 EQIQAVPLANSQAVREQLRQEKALLEDIERHGE--KVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1292
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1293 SESIIQEYVDLR----TRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERlaeveaalEKQRQLAEAHAQAKA 1368
Cdd:PTZ00121 1576 KNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--------KKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1369 QAEReaqgLQRRMQEEVARREEVAVEAQEQKRSIQEelqhLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEAT 1448
Cdd:PTZ00121 1648 KAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDE--------KKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1449 ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElalrvQAEAEAAREKQRALQALEELRLQ 1528
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-----KEEEKKAEEIRKEKEAVIEEELD 1786
|
....*...
gi 1920237974 1529 AEEAERRL 1536
Cdd:PTZ00121 1787 EEDEKRRM 1794
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
161-261 |
1.08e-10 |
|
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: 61.60 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 161 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1920237974 241 VdVPQPDEKSIITYVSSLYDA 261
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1329-1829 |
1.15e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.35 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1329 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-----EAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1403
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRhgnppASARAYANLGLLLLGDYEEAYEFGELALALA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1404 EELQHLRQSSEAEIqAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1483
Cdd:COG3899 821 ERLGDRRLEARALF-NLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1484 RRQVQDETQRKRQAEAELALRVQAEAEAAREkqRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1563
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAA--LALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1564 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQ 1643
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1644 AEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1723
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1724 QREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1803
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*.
gi 1920237974 1804 AEEDAVRQRAEAERVLAEKLAAISEA 1829
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRLL 1243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1316-2033 |
1.48e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.22 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1316 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1395
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1465
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1466 --AEEAEAQKRQAQEEAERLRRQVQDET-QRKRQAEAELAlRVQAEAEAAREKQRALQAleelrlQAEEAERRLRQAEAE 1542
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRIeQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1543 RARQVQvALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAeaerelerwQLKA 1622
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ---------KLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1623 NEALRLRLQAEEVAQQKSLtqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1693
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1694 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRRELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1769
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1770 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAV----RQ----------------------RAEAERVLAEK 1822
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQqienmtqlvgqhgrtagamqveKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1823 LAAISEATRLKTEAEIALKEKEAE---------------NERLRRLAEDEAFQRRLLEEQAAQHK------ADIEARLAQ 1881
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARvsdlelekvklvnagSERLRAVKDIKQERDQLLNEVKTSRNelnslsEDYEVLKRN 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1882 LRKASE------SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG-KAELELELGRIrgtaeDTLRSK----EQAE 1950
Cdd:pfam15921 683 FRNKSEemetttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGmQKQITAKRGQI-----DALQSKiqflEEAM 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1951 QEAARQRQLAAEEERRRREAEERV---QKSLAAEEEAARQRKAALEE--------VERLKAKVEEARRLRERAEQESARq 2019
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEkvanmevaLDKASLQFAECQDIIQRQEQESVR- 836
|
810
....*....|....
gi 1920237974 2020 LQLAQEAAQKRLQA 2033
Cdd:pfam15921 837 LKLQHTLDVKELQG 850
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2239-2595 |
1.58e-10 |
|
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: 67.77 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2239 VLRDKDSAQRLLQEEA---EKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL---AEKMlkEKMQAVQEATRlKA 2311
Cdd:TIGR02168 149 IIEAKPEERRAIFEEAagiSKYKERRKETERKLERTRENlDRLEDILNELERQLKSLerqAEKA--ERYKELKAELR-EL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2312 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQET---QGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2388
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2389 RFRKQAEDIGERLYRtelatqekvmlvqtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL 2468
Cdd:TIGR02168 306 ILRERLANLERQLEE--------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2469 LQEtQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfqdeVAKAQALreeqQRQQQQMQQEKQQLAASMEEARRRQHEAE- 2547
Cdd:TIGR02168 372 SRL-EELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERL----EDRRERLQQEIEELLKKLEEAELKELQAEl 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237974 2548 EGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2595
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1665-2039 |
1.86e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1742
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1743 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV------------- 1809
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1810 --RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1887
Cdd:COG4717 265 ggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1888 SELERQKGLVE-DTLRQRRQVEEEILALKGSFEKAAAGKAElelelgRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERR 1966
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1967 RREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2039
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1396-1585 |
2.18e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL--EATERQRGGAEGELQALRARAEEAEAQK 1473
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQkkQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1474 RQAQEEAERLRRQV-QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1552
Cdd:PRK09510 147 AKAEAEAKRAAAAAkKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|...
gi 1920237974 1553 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHV 1585
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2239-2594 |
2.73e-10 |
|
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: 67.00 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2239 VLRDKDSAQRLLQEEAEKMKQ-----VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQAVQEA-TRLK 2310
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERykelkAELRELELALLVLRLEELREELEELQEELKEAEEELeeLTAELQELEEKlEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2311 AEAELLQQQKELAQE---QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2387
Cdd:TIGR02168 274 LEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2388 RRFRKQAEdigerlyrtelatqEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKSE-EMQTVRQE 2466
Cdd:TIGR02168 354 ESLEAELE--------------ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARlERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2467 QLLQETQALQQSFLSEKDSLLQRErcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHeA 2546
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-S 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237974 2547 EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLqHLEEERRAALA 2594
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVDEGYEAAIE 540
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1665-2411 |
3.30e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1744
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1745 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1824
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1825 AISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRlleeqaaqhKADIEARLAQLRKAseseLERQKGLVEDTLR-- 1902
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELE--AEIASLERR---------KSNIPARLLALRDA----LAEALGLDEAELPfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1903 -QRRQVEEEILALKGSFEKAaagkaelelelgrIRGTAEDTLRSKEQAEQ--EAARQRQLAAEeerrrreaeerVQKSLA 1979
Cdd:COG4913 464 gELIEVRPEEERWRGAIERV-------------LGGFALTLLVPPEHYAAalRWVNRLHLRGR-----------LVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1980 AEEEAARQRKAALEE--VERLKAKVEEARrlrERAEQESARQLQLAQEAAQKRLQAEEKA--------HAFAVQQKEQEL 2049
Cdd:COG4913 520 RTGLPDPERPRLDPDslAGKLDFKPHPFR---AWLEAELGRRFDYVCVDSPEELRRHPRAitragqvkGNGTRHEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2050 QQTLQqeqSVLerlrseaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEaeqe 2129
Cdd:COG4913 597 RIRSR---YVL---------------------------GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA---- 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2130 aarraqaeqaaLRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQ 2209
Cdd:COG4913 643 -----------LQERREALQRLAEY-SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2210 VEEELFSLRvqmEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2289
Cdd:COG4913 711 LKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2290 ALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLeterqrQLEMSAEAER 2368
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVADL------LSKLRRAIRE 861
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2369 LRLRVAEMSRA----------------QARAEEDARRFRKQAEDIGERLYRTELATQEK 2411
Cdd:COG4913 862 IKERIDPLNDSlkripfgpgrylrleaRPRPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
45-141 |
3.72e-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: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 45 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 110
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1920237974 111 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 141
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1001-1589 |
4.59e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1001 RECAQRITEQQKAQaevdglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELEltlgkleqvrslsaiylEKLKTISLVI 1079
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELE-----------------ARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1080 RSTQEAEEVLRAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpvfdalrDELRGAQEVGERLQQrHGERDVEV 1158
Cdd:PRK04863 575 SEARERRMALRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLEREREL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1159 ERWRERVTlllERWQAVLAQTD-VRQRELEQLGRQLRYyresADPLGAWL----------RDAKQRQ----EQIQAVPLA 1223
Cdd:PRK04863 644 TVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDAPYFSalygPARHAIVVP 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1224 NSQAVREQLRQEKALLEDI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQSG 1292
Cdd:PRK04863 717 DLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRAE 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1293 SESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1372
Cdd:PRK04863 795 REELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1373 EAQGLQR-----------RMQEEVARREEVAVEAQEQKRSIQ---------EELQHLRQSSEAEIQAKARQVEAAE---- 1428
Cdd:PRK04863 873 GLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQqhgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqr 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1429 --RSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELALR 1504
Cdd:PRK04863 953 daKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASLKSS 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1505 VQAEAEAAREKQRALQAL---------EELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQsehaSFAEKTAQ 1575
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDLgvpadsgaeERARARRDELHARLSANRSRRN-----QLEKQLTFCEAEMD----NLTKKLRK 1099
|
650
....*....|....
gi 1920237974 1576 LERTLKEEHVAVVQ 1589
Cdd:PRK04863 1100 LERDYHEMREQVVN 1113
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1754-2025 |
5.28e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 65.74 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1754 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAVrqrAEAERVLAEKLAAISEATRL 1832
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDAV---AAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1833 KTEAEIALKEKEAEnERLRRLAEDEAFQRRLLEEQAAQHKADIEARL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1910
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1911 ILALKGSFEKAAAGKAELELELgrirgTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1990
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQV-----AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237974 1991 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2025
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1519-2014 |
5.41e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1519 LQALEELRLQAEEAE---RRLRQAEAERARQVQVALE-TAQRSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEA 1594
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIER-YEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1595 TRRAQQQAEAERARAEAERELERWQLKANEALRLRLQ-AEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1673
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1674 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1753
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1754 SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE----------------DAVRQRAEAER 1817
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1818 VLAEKLAAIsEATRLKTEAEIALKEKEAENE-RLRRLAEdeafQRRLLEEQAAQHKADIEA---RLAQLRKAS---ESEL 1890
Cdd:PRK02224 479 ELEAELEDL-EEEVEEVEERLERAEDLVEAEdRIERLEE----RREDLEELIAERRETIEEkreRAEELRERAaelEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1891 ERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELElELGRIRgtaeDTLRSKEQAEQEAARQRQLAAEEERRRREA 1970
Cdd:PRK02224 554 EEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIR----TLLAAIADAEDEIERLREKREALAELNDER 625
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1920237974 1971 EERVQkslaaeeeAARQRKAALEEvERLKAKVEEARRLRERAEQ 2014
Cdd:PRK02224 626 RERLA--------EKRERKRELEA-EFDEARIEEAREDKERAEE 660
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1676-2037 |
6.79e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1676 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRRELEAELAKVRAEMEvlla 1753
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1754 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLK 1833
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1834 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVE 1898
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1899 DTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERrrreaeerVQKSL 1978
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1979 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQEAAQKRLQAEEKA 2037
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1083-1534 |
7.46e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1083 QEAEEVLRAHEEQLK--EAQAVPATLPELEATKAALKKLRAQAEAQQPVFDAlrDELRGAQEVGERLQQRHGErdvEVER 1160
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKAEEKKKAE---EAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1161 WRERVTLLLERWQavlaqtDVRQRELEQLGRQLRYYRESADPLGAWLRdaKQRQEQIQAvplansqavrEQLRQEKALLE 1240
Cdd:PTZ00121 1572 AEEDKNMALRKAE------EAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA----------EELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1241 DIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESIIQEYVDLRtRYSELSTLTSQYIRF 1320
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK-KAAEALKKEAEEAKK 1703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1321 ISETLRRMEEEERLAEQQRAEERERLAEVEaalekqrqlaeahaQAKAQAEREaqglqRRMQEEVARREEVAVEAQEQKR 1400
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAE--------------EAKKEAEED-----KKKAEEAKKDEEEKKKIAHLKK 1764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1401 SIQEELQHLRQSSEAEIQAKARqvEAAERSRLRIEEEIRVVRLQLEATerQRGGAEGELQALRARAEEAEAQKRQAqEEA 1480
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELD--EEDEKRRMEVDKKIKDIFDNFANI--IEGGKEGNLVINDSKEMEDSAIKEVA-DSK 1839
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1481 ERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRaLQALEELRLQAEEAER 1534
Cdd:PTZ00121 1840 NMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDL-KEDDEEEIEEADEIEK 1892
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1087-1906 |
7.80e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1087 EVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpvfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERvt 1166
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1167 llLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReQLRQEKALLE----DI 1242
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1243 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQY-- 1317
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLqq 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1318 IRFISETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1390
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1391 VAVEAQEQkRSIQEELQHLRQSSEAE----------IQAKARQVEAAERSRLRIEEEIRVVRLQLEATErQRGGAEGE-L 1459
Cdd:PRK04863 598 LAARAPAW-LAAQDALARLREQSGEEfedsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSEDPrL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1460 QALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QRKRQA-----EA 1499
Cdd:PRK04863 676 NALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDSFDDSvfsveEL 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1500 ELALRVQ-AEAE--------------AAREKQralqaLEELRLQAEEAERRLRQAEAERaRQVQVALETAQR-------- 1556
Cdd:PRK04863 756 EKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAFSRfigshlav 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1557 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVA 1636
Cdd:PRK04863 830 AFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1637 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--------------LAEGTAQQRLAAEQEL-IR 1701
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahFSYEDAAEMLAKNSDLnEK 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1702 LRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRRELEAELAK--VRAEMEVLLASKARAEE----- 1760
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAEERARARRDElharl 1069
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1761 ----ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAVRQRAEAERVLAEKLAAIS--EAT 1830
Cdd:PRK04863 1070 sanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHRRELAYLSadELR 1148
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1831 RLKTEAEIALKEKEAENERLR---RLAEDEAFQ----------RRLLEEQAAQhkaDIeARLAQLRKASEsELERQKGLV 1897
Cdd:PRK04863 1149 SMSDKALGALRLAVADNEHLRdvlRLSEDPKRPerkvqfyiavYQHLRERIRQ---DI-IRTDDPVEAIE-QMEIELSRL 1223
|
....*....
gi 1920237974 1898 EDTLRQRRQ 1906
Cdd:PRK04863 1224 TEELTSREQ 1232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2252-2673 |
9.04e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2252 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2328
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2329 RLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQ-ARAEEDARRF---RKQAEDIGERLYRT 2404
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdAKKAEAVKKAeeaKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2405 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQllqlKSEEMQTVrqEQLLQETQALQQSFLSEKD 2484
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKA--DEAKKKAEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2485 SLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME-----------EARRRQHEAE---EGV 2550
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakkkaEEKKKADEAKkkaEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2551 RRQQEELQRLAQQQQQQEKLL--AEENQRLRERLQHLEEERRAalarseEIAPSRAAAARALPNGQDAADGPAAAAEPEH 2628
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKA------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1920237974 2629 AFDGLRRKVPAQRLQEVGVLSAEELQQLAQGRTTVAELAQREDVR 2673
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1191-1861 |
1.15e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1191 RQLRYYRESADPLGAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDY---- 1266
Cdd:PRK03918 111 SSVREWVERLIPYHVFLNAIYIRQGEIDA--ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1267 ---ELQLVTYKAQLEPVASPAKK-----PKVQSGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQ 1338
Cdd:PRK03918 189 eniEELIKEKEKELEEVLREINEisselPELREELEKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEER 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1339 RAEERERLAEVE---AALEKQRQLAEAHAQAK-----------------AQAEREAQGLQRRMQEEVARREEVAvEAQEQ 1398
Cdd:PRK03918 268 IEELKKEIEELEekvKELKELKEKAEEYIKLSefyeeyldelreiekrlSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1399 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1478
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1479 EAERLRRQVQDETQRKRQAEAELALRVQAEAEAarEKQRALQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQ- 1555
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEq 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1556 -RSAEAELQSEHASFAEKTAQLERTLKEEhvaVVQLREEATRRAQqqaeaeraraeaerelerwQLKANEALRLRLQAEE 1634
Cdd:PRK03918 505 lKELEEKLKKYNLEELEKKAEEYEKLKEK---LIKLKGEIKSLKK-------------------ELEKLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1635 VAQQKsltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRaeteQGEQQRQ 1714
Cdd:PRK03918 563 KKLDE----------------------LEEELAELLKELEELGFESVEEL-EERLKELEPFYNEYLELK----DAEKELE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1715 LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALA 1794
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAEL 682
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1795 EEAKRQRQLAEEDAvrqraeaeRVLAEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 1861
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1496-1863 |
1.38e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.76 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1496 QAEAELALRVQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQvqvaletaqrsaeAELQSEHASFAEktaq 1575
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEK---AREVERRRKLEEAEKARQ-------------AEMDRQAAIYAE---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1576 lertlkEEHVAVVQLREeatrraqqqaeaeraraeaereLERWQLKANEALRLRLQAEEVAQQksLTQAEAEKQKEEAER 1655
Cdd:pfam17380 339 ------QERMAMERERE----------------------LERIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1656 EARRRGKAEEQAVRQRELAEQE-----LEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQReaaaa 1730
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEErqrkiQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ----- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1731 TQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAvR 1810
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-R 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1811 QRAEAER---VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRL 1863
Cdd:pfam17380 536 REAEEERrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
934-1583 |
1.44e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 934 DRLQAEREYgscSRHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRITEQQKA 1013
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1014 QAEVDGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKL--------KTISLVIRS 1081
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELedaeerlaKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1082 TQEAEEVLRAHEEQLKEAQAVPAtlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGE-------- 1153
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkreldrl 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1154 ------RDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ--------- 1218
Cdd:TIGR02169 412 qeelqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEkelsklqre 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1219 -----AVPLANSQAVREQLRQEKALLEDI--------------ERHGEKVE-------------------ECQRFAKQY- 1259
Cdd:TIGR02169 492 laeaeAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgERYATAIEvaagnrlnnvvveddavakEAIELLKRRk 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1260 --------INAIK---------------DYELQLVTYKAQLEPVASPAKKPKV-----QSGSESIIQ-----------EY 1300
Cdd:TIGR02169 572 agratflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLvvediEAARRLMGKyrmvtlegelfEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1301 VDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRR 1380
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1381 MQEEVARREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAAERSRLRIE-----EEIRVVRLQLEATERQRGGA 1455
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1456 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELALRVQAEAEAAREKQRALQALEE----LRLQ 1528
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLESrlgdLKKE 890
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1529 AEEAERRLRQAEaERARQVQVALETAqRSAEAELQSEHASFAEKTAQLERTLKEE 1583
Cdd:TIGR02169 891 RDELEAQLRELE-RKIEELEAQIEKK-RKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
38-144 |
1.50e-09 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 58.75 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYLR 111
Cdd:cd21222 9 EAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELME 88
|
90 100 110
....*....|....*....|....*....|...
gi 1920237974 112 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21222 89 DAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1681-1887 |
2.32e-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: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1681 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEE 1760
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1761 ESRSTSEKSKQRLEA--------------EAGRFRELAEEAARLRALAEEAKRQ-----RQLAEEDAVRQRAEAERvlAE 1821
Cdd:COG4942 98 ELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQaeelrADLAELAALRAELEAER--AE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1822 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1887
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1335-1533 |
2.37e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.90 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1335 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARReevavEAQEQKrsiQEELQHLRQSS 1413
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ-----AALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1414 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1493
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237974 1494 KRQAEAELAL-RVQAEAEAAREKQRALQALEELRLQAEEAE 1533
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1228-1818 |
2.50e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1228 VREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDlrtRY 1307
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE---EY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1308 SELSTLTSQYIrfisETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLaeahaqakaqaeREAQGLQRRMQEEVAR 1387
Cdd:PRK03918 296 IKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELE---EKEERL------------EELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1388 REEvAVEAQEQKRSIQEELQHLRQS-SEAEIQAKARQVEAAERSRLRIEEEIRVV---RLQLEATERQRGGAEGELQALR 1463
Cdd:PRK03918 357 LEE-RHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1464 ARA---------EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaEAEAAREKQRALQALEELRLQAEEAER 1534
Cdd:PRK03918 436 GKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1535 RLRQAEAERarqvqvaLETAQRSAEaELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERE 1614
Cdd:PRK03918 511 KLKKYNLEE-------LEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1615 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLA 1694
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1695 AEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlaSKARAEEESrstSEKSKQRLE 1774
Cdd:PRK03918 657 SEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--EKAKKELEK---LEKALERVE 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1775 AEAGRFRELAEEAARlRALAEEAKRQRQLAEE------DAVRQRAEAERV 1818
Cdd:PRK03918 725 ELREKVKKYKALLKE-RALSKVGEIASEIFEEltegkySGVRVKAEENKV 773
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1080-1276 |
2.67e-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: 60.54 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1080 RSTQEAEEVLRAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVe 1159
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1160 rwRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLRDAKQRQEQIQavPLANSQAVREQLRQEKALL 1239
Cdd:cd00176 78 --QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELE 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237974 1240 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1276
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
159-261 |
2.79e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.77 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 159 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1920237974 238 PEDVDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2238-2589 |
3.06e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.60 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2238 LVLRDKDSAQRLLQEEAEKM-----KQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaE 2312
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqerlRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------Q 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2313 AELLQQQKELAQEQARRL----QEDKEQMAQQLAQETQGFQKTLETERQR-QLEMSAEAERLRLRVAEMSRAQARAEEDA 2387
Cdd:pfam17380 333 AAIYAEQERMAMERERELerirQEERKRELERIRQEEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2388 RRFRKQAEDIGERLYRTELATQEKVmlvQTLETQRQqsdRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQ 2467
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREV---RRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2468 LLQETQalqqsflsekdsllqRERCIEQEKAKLEQLFQDEVAKAQALREEqqrqqqqmqqekqqlaasMEEarRRQHEAE 2547
Cdd:pfam17380 487 KRAEEQ---------------RRKILEKELEERKQAMIEEERKRKLLEKE------------------MEE--RQKAIYE 531
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237974 2548 EGVRRQQEELQRlaqqqqqqEKLLAEENQRLRERLQHLEEER 2589
Cdd:pfam17380 532 EERRREAEEERR--------KQQEMEERRRIQEQMRKATEER 565
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2141-2599 |
3.17e-09 |
|
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: 63.45 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILdeelqRLKAEVTEAARQRGQVEEELFSLRVQ 2220
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2221 MEELGKLKARIEA--ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALA 2292
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2293 EKMLKEKMQAVQEATRLKAEAELLQQ------QKELAQEQARRLQEDKEQMAQQLAQETQGFQK-------------TLE 2353
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqqlqTKE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2354 TERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLR 2433
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2434 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQRERCIE---------QEKAKLEQLF 2504
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLrklqpeqdlQDVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2505 QDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEAR---------------------------------RRQHEAEEGVR 2551
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmqsekeqltywkemlaqcqtllRELETHIEEYD 717
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1920237974 2552 RQQEELQRLAQQQQQQeklLAEENQRLRERLQHLEEERRAALARSEEI 2599
Cdd:TIGR00618 718 REFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKARTEA 762
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1183-1561 |
3.55e-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: 63.43 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1183 QRELEQLGRQLRYYRESADplgawlrDAKQRQEQIQA-VPLANSQAvREQLRQekaLLEDIERHGEKVEECQRFAKQYIN 1261
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKlLPQANLLA-DETLAD---RLEELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1262 AIkdyelqlvtykAQLEPVASPAKKPKVQSgsESIIQEYVDLRTRYSELStltsQYIRFISETLRRM------EEEERLA 1335
Cdd:COG3096 918 AL-----------AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRLK----QQIFALSEVVQRRphfsyeDAVGLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1336 EQQRAEE--RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEevarreevaveAQEQKRSIQEELQHLrqss 1413
Cdd:COG3096 981 ENSDLNEklRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL---- 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1414 eaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQ 1486
Cdd:COG3096 1046 --GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRL 1123
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1487 VQDETQRKRQAEAELalrvqaeaeaarekqrALQALEELRLQAEEAERRLRQAEAERArQVQVALETAQRSAEAE 1561
Cdd:COG3096 1124 ARDNDVERRLHRREL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPRRPE 1181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1704-2293 |
3.57e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1704 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAG--- 1778
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRele 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1779 --------RFRELAEEAARLRALAEEAKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKEAENERL 1850
Cdd:PRK03918 266 erieelkkEIEELEEKVKELKELKEKAEEYIKLSEF--YEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1851 RRLAEDEAFQRRLLEEQAAQHKA--DIEARLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILAL---KGSFEKA 1921
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKItarIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1922 AAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEEVERLKAK 2001
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT---------AELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2002 VEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAeeaeaa 2080
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE------ 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2081 reraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2160
Cdd:PRK03918 563 ------------KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2161 ALRQKAQVEQELTALRLQLEETdhQKSILDEELQRLKAEVTEaarqrgqVEEELFSLRVQMEELGKLKARIEAEnralvL 2240
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKT-----L 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 2241 RDkdsaqrlLQEEAEKMKQVAEEAARLSVAAQEAARLRQ--LAEEDLAQQRALAE 2293
Cdd:PRK03918 697 EK-------LKEELEEREKAKKELEKLEKALERVEELREkvKKYKALLKERALSK 744
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1097-1518 |
4.05e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.22 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1097 KEAQAVPATLPELEA-----------------TKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERdVEVE 1159
Cdd:pfam17380 221 KEVQGMPHTLAPYEKmerrkesfnlaedvttmTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1160 RWR---ERVTLLLERWQAVLAQTDVRQRELEqlgRQLRYYRESAdplgawlRDAKQRQEQIQAVPLANSQAVREQLRQEK 1236
Cdd:pfam17380 300 RLRqekEEKAREVERRRKLEEAEKARQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEERKRELERIRQEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1237 ALLEDierhgEKVEECQRFakqyinaikdyelqlvtykaQLEPvaspakkpkvQSGSESIIQEYVDLRtrysELSTLTSQ 1316
Cdd:pfam17380 370 IAMEI-----SRMRELERL--------------------QMER----------QQKNERVRQELEAAR----KVKILEEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1317 YIRFISETLRRMEEEERLAEQQRAEERERLAEveaalEKQRQLAEAHAQakaQAEREAQGLQRRMQEEVARREEVAVEAQ 1396
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEE-----ERAREMERVRLE---EQERQQQVERLRQQEEERKRKKLELEKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1397 EQKRSIQEELQhlRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleatERQRGGAEGElqalRARAEEAEAQKRQA 1476
Cdd:pfam17380 483 KRDRKRAEEQR--RKILEKELEERKQAMIEEERKRKLLEKEME---------ERQKAIYEEE----RRREAEEERRKQQE 547
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237974 1477 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRA 1518
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
154-256 |
4.35e-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: 57.10 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 154 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 232
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1920237974 233 TRLLDPEDVDVPQPDEKSIITYVS 256
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1477-1958 |
4.53e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1477 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1556
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1557 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREeatrraqqqaeaeraraeaerelerwqlKANEALRLRLQAEEVA 1636
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEE----------------------------LEAELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1637 QQKSLTQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1716
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1717 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1796
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1797 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKAD 1874
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1875 IEARLAQLRKASESELERQKGLVEDTLRQR-RQVEEEILALKGSFEKAAAGKAELELELGRIRGtaEDTLRSKEQAEQEA 1953
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEEL 481
|
....*
gi 1920237974 1954 ARQRQ 1958
Cdd:COG4717 482 KAELR 486
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4371-4409 |
4.59e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 4.59e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 4371 FLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTAQKL 4409
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1360-1583 |
4.70e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1360 AEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEE 1436
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1437 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1516
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1517 RALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQSEHASFAEKTAQLERTLKEE 1583
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1673-1904 |
4.75e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.40 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1673 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAelakvraemevll 1752
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1753 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAVRQRAEAervlAEKLAaisEATRL 1832
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1833 KTEAEiALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE----ARLAQLRKASESELERQKGLVEDTLRQR 1904
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
44-143 |
5.41e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 56.74 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 44 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILH 143
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4293-4330 |
6.78e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 6.78e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1920237974 4293 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4330
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1351-1575 |
7.91e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1351 AALEKQRQLAEAHAQAKAQAEREAQGLQRrmQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAK---ARQVEAA 1427
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKqaaLKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1428 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELALRVQ 1506
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1507 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1575
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1325-1545 |
8.70e-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: 60.93 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1325 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1404
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1405 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1481
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1482 RLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1545
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2148-2598 |
8.72e-09 |
|
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: 62.29 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2148 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKaevtEAARQRGQVEEELFSLRVQMEELGKL 2227
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2228 KARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLA------EEDLAQQRALAEKMLKEKM 2300
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2301 QAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLaqetQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQ 2380
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2381 ARAEEDARRFRKQAEDIGER----------LYRTELATQEKVMLVQTLETQRQQSDR-----DAERLREAIAELEHEKDK 2445
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTaqceklekihLQESAQSLKEREQQLQTKEQIHLQETRkkavvLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2446 LKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQM 2525
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2526 QQEKQQLAASMEEARRR------QHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2598
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEdmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1804-2337 |
9.05e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1804 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1883
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1884 KASESELERQKGLVEDT--LRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAA 1961
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1962 EEERrrreaeerVQKSLAAEEEAArqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfA 2041
Cdd:PRK03918 346 KLKE--------LEKRLEELEERH-------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-K 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2042 VQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEReaaqsRRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2121
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2122 LRKEAEQEAARraqaeqaaLRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA--- 2198
Cdd:PRK03918 485 LEKVLKKESEL--------IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkk 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2199 EVTEAARQRGQVEEELFSLRVQMEELG---------KLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLS 2268
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGfesveeleeRLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfEELA 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2269 VAAQEAARLR-QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2337
Cdd:PRK03918 637 ETEKRLEELRkELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1362-1821 |
1.08e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.96 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1362 AHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1441
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLA---LAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1442 RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQA 1521
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1522 LEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1601
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1602 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1681
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1682 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1761
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1762 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1821
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1079-2016 |
1.13e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1079 IRSTQEAEEVLRAHEEQLKEAQAvpatlpeleatkaALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQ--RHGERdv 1156
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQY-------------RLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1157 eVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReqlrqek 1236
Cdd:COG3096 349 -IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1237 ALledierhgEKVEECQRFAKQYINAIKDYelqLVTYKAQLEpvaspakkpkvqsgseSIIQEYVDLRTRYSELSTLTSQ 1316
Cdd:COG3096 421 AL--------EKARALCGLPDLTPENAEDY---LAAFRAKEQ----------------QATEEVLELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1317 YIRFIsETLRRMEEE-ERLAEQQRAEERER-------LAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARR 1388
Cdd:COG3096 474 FEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1389 EEVAVEAQEQKRSIQEELQHLRQSSEAEIQakarqveaaersrlrieeeirvvrlqleaTERQRGGAEGELQALRARAEE 1468
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSE-----------------------------LRQQLEQLRARIKELAARAPA 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1469 AeaqkRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAeeaeRRLRQAE-AERARQV 1547
Cdd:COG3096 604 W----LAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQI----ERLSQPGgAEDPRLL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1548 Q----------------VALETAQR-------SAEAELQSEHASFAEKTAQLERTLkeEHVAVVQLREEATRRAQQQAEA 1604
Cdd:COG3096 676 AlaerlggvllseiyddVTLEDAPYfsalygpARHAIVVPDLSAVKEQLAGLEDCP--EDLYLIEGDPDSFDDSVFDAEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1605 ERARAEAERELERWQL-------------KANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQR 1671
Cdd:COG3096 754 LEDAVVVKLSDRQWRYsrfpevplfgraaREKRLEELRAERDELAEQYA------------------------KASFDVQ 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1672 ELaeQELEKQ-RQLAEGTAQQRLAAEQElirlrAETEQGEQQRQLLEEELARL----QREAAAATQKRRELEAeLAKVRA 1746
Cdd:COG3096 810 KL--QRLHQAfSQFVGGHLAVAFAPDPE-----AELAALRQRRSELERELAQHraqeQQLRQQLDQLKEQLQL-LNKLLP 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1747 EMEVL----LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAKRQRQL---AEEDAVRQRAEAER 1817
Cdd:COG3096 882 QANLLadetLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpEQFEQLQADYLqakEQQRRLKQQIFALS 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1818 VLAEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1894
Cdd:COG3096 962 EVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1895 GLvedtlrQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG--TAEDTLRSKEQAEQEAARQRqlaaeeerrrreaEE 1972
Cdd:COG3096 1037 EL------EQELEELGVQADAEAEERARIRRDELHEELSQNRSrrSQLEKQLTRCEAEMDSLQKR-------------LR 1097
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1920237974 1973 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL--RERAEQES 2016
Cdd:COG3096 1098 KAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSA 1143
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1331-1545 |
1.13e-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: 60.24 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1331 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiQEELQHLR 1410
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK-QAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1411 QSSEAEIQAKA-RQVEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE----AERLRR 1485
Cdd:TIGR02794 128 QAAEAKAKAEAeAERKAKEEAAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKA 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1486 QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1545
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
154-261 |
1.31e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 154 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 232
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1920237974 233 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2141-2597 |
1.39e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2215
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2216 SLRVQMEELG-----KLKARIEAENRALVLRDKDSAQrlLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2289
Cdd:COG4913 327 ELEAQIRGNGgdrleQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2290 ALAEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM------------------------ 2337
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2338 ---AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyRTELATQEKVML 2414
Cdd:COG4913 485 ggfALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWL-EAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2415 VQTLE-------------------TQRQQSDRDAERL--------REAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQ-- 2465
Cdd:COG4913 564 VDSPEelrrhpraitragqvkgngTRHEKDDRRRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDal 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2466 EQLLQETQALQQSFLSEKDsLLQRERCIEQEKAKLEQL--FQDEVAKAQALREEqqrqqqqmqqekqqLAASMEEARRRQ 2543
Cdd:COG4913 644 QERREALQRLAEYSWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEE--------------LEAELEELEEEL 708
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 2544 HEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSE 2597
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1474-1994 |
1.69e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1474 RQAQEEAERLRRQVQD----ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARqvqv 1549
Cdd:COG4913 238 ERAHEALEDAREQIELlepiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1550 aLETAQRSAEAELQSEHASFAEKTAQLERTLKEEhvavvqlreeatrraqqqaeaeraraeaereLERWQLKANEALRLR 1629
Cdd:COG4913 314 -LEARLDALREELDELEAQIRGNGGDRLEQLERE-------------------------------IERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1630 LQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1709
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1710 EQQRQLLEEELARLQREAAAATQ-KRRELE--AELAKVRAE-------MEVLLASKAR---------------------- 1757
Cdd:COG4913 432 ERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrlhlr 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1758 ------------AEEESRSTSEKS-KQRLEAEAGRFR-----ELAEEAARLRALAEEA-----------------KRQRQ 1802
Cdd:COG4913 512 grlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgnGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1803 LAEEDAVRQR----AEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEE-----QAAQHKA 1873
Cdd:COG4913 592 KDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvaSAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1874 DIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRirgtAEDTLRSKEQAEQEA 1953
Cdd:COG4913 672 ELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE----LQDRLEAAEDLARLE 746
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1920237974 1954 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1994
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1346-1758 |
1.83e-08 |
|
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: 61.03 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1346 LAEVEAALEKQRQLAEAHAQAkaqaeREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE----------- 1414
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1415 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1486
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1487 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1566
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1567 ASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEA 1646
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1647 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1726
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 1920237974 1727 AAAATQKRRELEAELAKVRAEMEVLLASKARA 1758
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
46-140 |
2.80e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 54.65 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 46 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 117
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1920237974 118 VNIRNDDIADGNPKLTLGLIWTI 140
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
506-695 |
3.69e-08 |
|
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: 57.07 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 506 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQLSPATRGAY---RDCLGRLD 582
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 583 LQYAKLLSSSKARLRSLE---SLHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEI 659
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237974 660 QSTGDRLLREDHP-ARPTAESFQAALQTQWSWMLQLC 695
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1084-1439 |
4.62e-08 |
|
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: 59.69 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1084 EAEEVLRAHEEQLKEAQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWR 1162
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1163 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLrDAKQRQEQIQAVPLANSQAVREQLRQEKALLED- 1241
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERr 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1242 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELstltsqyirfi 1321
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL----------- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1322 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ------------------LAEAHAQAKAQAEREAQGLQRRMQE 1383
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltleEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1384 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAErsrlRIEEEIR 1439
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE----EIDREAR 1031
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1674-1861 |
4.90e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1674 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRRELEAELAKVRAEMEVL 1751
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1752 LASKARAEEESrstseksKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAVRQRAEAERVlAEKLAAISEATR 1831
Cdd:PRK09510 157 AAAAKKAAAEA-------KKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAE 222
|
170 180 190
....*....|....*....|....*....|
gi 1920237974 1832 LKTEAEIALKEKEAENERLRRLAEDEAFQR 1861
Cdd:PRK09510 223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1480-1939 |
5.28e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 59.65 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1480 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAleelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1559
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1560 AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQK 1639
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1640 SLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1719
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1720 LARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1799
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1800 QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARL 1879
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1880 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTA 1939
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2159-2599 |
5.44e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.47 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2159 EQALRQKAQVEQELTALRLQL-EETDHQKSILDEELQRLKAEVTEAARQRGQV---EEELFSLRVQMEELGKLKARIEAE 2234
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2235 NRAlvlrdkdsaQRLLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE 2314
Cdd:pfam12128 484 NAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2315 LLQQQ--KELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA-------QARAEE 2385
Cdd:pfam12128 546 DWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsarekQAAAEE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2386 DARRFRKQAE--DIGERLYRTELaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTV 2463
Cdd:pfam12128 626 QLVQANGELEkaSREETFARTAL-KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2464 RQEQLLQETQALQQSFL---SEKDSLLQR-----ERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAAS 2535
Cdd:pfam12128 705 QKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREIRTLERK 783
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 2536 MEEARRRQHEAEEGVRRQQE----ELQRLAQQQQQQEKLLAEENQRL-------RERLQHLEEERRAALARSEEI 2599
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRL 858
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1396-1936 |
5.65e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 58.89 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1473
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1474 RQAQEEAERLRRQVQDETQRKRQAEAELALrVQAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEAERAr 1545
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1546 QVQVALETAQRS-AEAELQSEHASFA--EKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKA 1622
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1623 NEALRLRLQAEEVAQQKSltqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1699
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1700 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1779
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1780 frelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1857
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1858 AFQR----------------RLLEEQAaqhKADIEARLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKGSFEKA 1921
Cdd:pfam05701 466 DSPRgvtlsleeyyelskraHEAEELA---NKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKA 541
|
570
....*....|....*
gi 1920237974 1922 AAGKAELELELGRIR 1936
Cdd:pfam05701 542 KEGKLAAEQELRKWR 556
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2150-2598 |
6.65e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2150 EMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEE------ELFSLRVQMEE 2223
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklseFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2224 LGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2301
Cdd:PRK03918 312 IEKRLSRLEEEINGIeeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2302 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQ-----RQLEMSAEAERLRLRVAEM 2376
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2377 SRAQ---ARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKL-KQEAQL 2452
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2453 LQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRER-----CIEQEKAKLEQL--FQDEVAKAQALREEQQRQQQQM 2525
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELepFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 2526 QQEKQQLAASMEEARRRQHEAEEgVRRQQEELQRlaqqqqqqeKLLAEENQRLRERLQHLEEERRAALARSEE 2598
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEE-LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
163-258 |
7.03e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 54.23 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 163 KLLL-WSQrMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNL-----------------------EN 218
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 219 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 258
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2191-2459 |
7.52e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2191 EELQRLKAEVTEAARQRGQVE------EELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkQVAEEA 2264
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2265 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2344
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2345 TQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedigerlyrtelatqekvmlVQTLETQRQQ 2424
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE---------------------IASLERRKSN 437
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237974 2425 SDRDAERLREAIAE-LEHEKDKLKQEAQLLQLKSEE 2459
Cdd:COG4913 438 IPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1637-1832 |
7.58e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1637 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1716
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1717 EEELARLQREAAAATQKRRELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1796
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237974 1797 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1832
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
32-152 |
7.95e-08 |
|
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: 54.68 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 32 ASEGKKDERDRVQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFH 98
Cdd:cd21325 13 SSEGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFI 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 99 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 152
Cdd:cd21325 93 IQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1415-1567 |
9.37e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.96 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1415 AEIQAKARQVEA-AERsrlriEEEIRVVRLQLEATERQrggAEGELQALRARAEEAEAQKRQAQEEAERlrrqvqdETQR 1493
Cdd:COG2268 195 AEIIRDARIAEAeAER-----ETEIAIAQANREAEEAE---LEQEREIETARIAEAEAELAKKKAEERR-------EAET 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 1494 KRqAEAELALRVQaEAEAAREKQRALQALE---ELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHA 1567
Cdd:COG2268 260 AR-AEAEAAYEIA-EANAEREVQRQLEIAErerEIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRA 334
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1464-1915 |
9.95e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1464 ARAEEAEAQKRQAQEEAERLRRQVQD-ETQRKRQAEAELAL----RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1538
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1539 AEAERARQVQV-----ALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEaer 1613
Cdd:COG4717 151 LEERLEELRELeeeleELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1614 elerwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAvrqrELAEQELEKQRQLAEGTAQQRL 1693
Cdd:COG4717 228 -----ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA----GVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1694 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRL 1773
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1774 EAEAGrfrelAEEAARLRALAEEAKRQRQLAEEdavrqRAEAERVLAEKLAAISEATRLKTEAEiaLKEKEAENERLRRL 1853
Cdd:COG4717 376 LAEAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1854 AEDEafqrrllEEQAAQHKADIEARLAQLrkASESELERQKGLVEDTLRQRRQVEEEILALK 1915
Cdd:COG4717 444 LEEE-------LEELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1384-1549 |
1.01e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 58.61 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1384 EVARR----EEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegel 1459
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1460 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelalrvQAEAEAAREKQRALQALEElRLQAEEAERRLRQ 1538
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 1920237974 1539 AEAERARQVQV 1549
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4024-4060 |
1.13e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 1.13e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 4024 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 4060
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1050-1498 |
1.40e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1050 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKA-------ALKKLRAQ 1122
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelaelpeRLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1123 AEAQQPVFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1202
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1203 LGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVeecqrfakQYINAIKDYELQLVTYKAQLEPVAS 1282
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV--------LFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1283 PAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRfiseTLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA 1362
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1363 HAQAKAQAEREAQGLQRRmQEEVARREEVAVEAQEQKRSIQEELQHLRQSS-EAEIQAKARQVEAAERSRLRIEEEIRVV 1441
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 1442 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDETQRKRQAE 1498
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1323-1583 |
1.49e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 56.85 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSI 1402
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1403 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1482
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1483 LR-RQVQDETQRK-RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1560
Cdd:pfam13868 206 LRaKLYQEEQERKeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR 285
|
250 260
....*....|....*....|...
gi 1920237974 1561 ELQSEHASFAEKTAQLERTLKEE 1583
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAA 308
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
32-151 |
1.53e-07 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 53.51 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 32 ASEGKKDERDRVQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFH 98
Cdd:cd21323 13 SSEGTQHSYSEEEKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFT 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 99 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 151
Cdd:cd21323 93 ISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1031-1593 |
1.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1031 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEaqaVPATLPELE 1110
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1111 ATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLqqrhgerdvevERWRERvtllLERWQAVLAQTDVRQRELEQLG 1190
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-----------SRLEEE----INGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1191 RQLRYYRESADPLGAWLR---DAKQRQEQIqavplansqavrEQLRQEKALL--EDIERHGEKVEECQRFAKQYINAIKD 1265
Cdd:PRK03918 345 KKLKELEKRLEELEERHElyeEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1266 YELQLVTYKAQLEPVASPAKKPKVQS---GSESIIQEYVDLRTRYSElstltsqYIRFISETLRRMEEEERlaeqqraEE 1342
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1343 RERLAEVEAALEKQRQLAEAHAQAKaqaereaqglQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1422
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAE----------QLKELEE--KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1423 QVEAAERsrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1502
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1503 lRVQAEAEAAREK-QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERtLK 1581
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LK 700
|
570
....*....|..
gi 1920237974 1582 EEHVAVVQLREE 1593
Cdd:PRK03918 701 EELEEREKAKKE 712
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1331-1958 |
2.13e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.50 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1331 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAQGLQRRMQEEVARREEV 1391
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1392 AVEAQEQKRSIQEELQHLRQ-SSEAEIQAKARQVEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1466
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1467 EEAEAQKRQAQEEAER-----LRRQVQDETQRKRQAEAelalrvqAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1541
Cdd:PRK10246 410 EVAAALAQHAEQRPLRqrlvaLHGQIVPQQKRLAQLQV-------AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1542 ERARQVQVALETAQRsaeAELQS----------EHASFAEKTAqLERTlkeehvaVVQLREEATRRAQQQAeaeraraea 1611
Cdd:PRK10246 483 ICEQEARIKDLEAQR---AQLQAgqpcplcgstSHPAVEAYQA-LEPG-------VNQSRLDALEKEVKKL--------- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1612 erelerwqlkANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQ 1691
Cdd:PRK10246 543 ----------GEEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1692 RLAAEQELIRLRAETEQGEQQRQLLEEELArLQREAAAATQKRRELEAELAKVRAEMEVLLASKA------RAEEESRST 1765
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLAT 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1766 SEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAVrqRAEAERVLAEKLAAISEATrLKTEAEIALKEKEA 1845
Cdd:PRK10246 670 RQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQD 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1846 ENERLR---------------RLAEDEAFQRRLLEEQAAQhkadieaRLAQLRKASESELERQKGLVEdtlrQRRQVEEE 1910
Cdd:PRK10246 741 VLEAQRlqkaqaqfdtalqasVFDDQQAFLAALLDEETLT-------QLEQLKQNLENQRQQAQTLVT----QTAQALAQ 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 1911 ILALKGSFEKAAAGKAELELELGRIRGT-AEDTLRSKE---QAEQEA-ARQRQ 1958
Cdd:PRK10246 810 HQQHRPDGLDLTVTVEQIQQELAQLAQQlRENTTRQGEirqQLKQDAdNRQQQ 862
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
39-146 |
2.33e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 52.70 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 111
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237974 112 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1695-1895 |
2.43e-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: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1695 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1774
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1775 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEA 1836
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1837 EIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKG 1895
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1316-1577 |
2.67e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.88 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1316 QYIRFISETLRRMEEEERLAEQ--QRAEER-ERLAEVEAA-LEKQRQLAEAHAQAKAQA---------EREAQGLQRRMQ 1382
Cdd:PRK05035 429 QYYRQAKAEIRAIEQEKKKAEEakARFEARqARLEREKAArEARHKKAAEARAAKDKDAvaaalarvkAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1383 EEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEeirvvrlQLEATERQRGGAEGELQA 1461
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAA-------QQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1462 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAelalrvqaeAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1541
Cdd:PRK05035 582 VAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAA---------AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237974 1542 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLE 1577
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1674-1926 |
2.74e-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: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1674 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1753
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1754 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEK 1822
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1823 LAAISEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLR 1902
Cdd:COG3883 174 EAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|....
gi 1920237974 1903 QRRQVEEEILALKGSFEKAAAGKA 1926
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1427-1547 |
2.75e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.82 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1427 AERSRLRIEEEIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------RQVQDETQRKR-Q 1496
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQQELDEARAALdA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1497 AEAELAlRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1547
Cdd:COG1566 160 AQAQLE-AAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1681-1881 |
3.14e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.42 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1681 QRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRqllEEELARLQREAAAATQKRRELEAELAKVraemevllaskaraEE 1760
Cdd:COG2268 191 RRKIAEIIRDARIAEAE--AERETEIAIAQANR---EAEEAELEQEREIETARIAEAEAELAKK--------------KA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1761 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA-----ERVLAEKLAAISEAtrlKTE 1835
Cdd:COG2268 252 EERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadvrKPAEAEKQAAEAEA---EAE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237974 1836 AEIALKEKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1881
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2259-2712 |
4.39e-07 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 56.52 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2259 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMA 2338
Cdd:COG4995 9 LLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2339 QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2418
Cdd:COG4995 89 LLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2419 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2498
Cdd:COG4995 169 ALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2499 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRL 2578
Cdd:COG4995 249 ALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2579 RERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLRRKVPAQRLQEVGVLSAEELQQLAQ 2658
Cdd:COG4995 329 ALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQL 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 2659 GRTTVAELAQREDVRHYLQGRSSIAGLL-LKPADEKLTIYAALRRQLLSPGTALI 2712
Cdd:COG4995 409 LRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1710-1894 |
4.70e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1710 EQQRQLLEEELAR-LQREAAAATQKRRELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1788
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1789 RLRALAEeakrqrQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRrllEEQA 1868
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK--AEAEAKKK---AAAE 214
|
170 180
....*....|....*....|....*.
gi 1920237974 1869 AQHKADIEARLAQLRKASESELERQK 1894
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1734-2440 |
4.72e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1734 RRELEAELAKVRAEMEVLLASKARAEEESRStsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRA 1813
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQ--IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1814 EAERvlaeklaaiSEATRLKTEAEIALKEKEAENERLRRLaedeafqrrllEEQAAQHKADIEARLAQLRKASESELERQ 1893
Cdd:COG4913 298 EELR---------AELARLEAELERLEARLDALREELDEL-----------EAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1894 KGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerrrreaeer 1973
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR--------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1974 vqkSLAAEEEAARQRKAAL-EEVERLKAKVEEARRLRE------------RAEQES-------------------ARQLQ 2021
Cdd:COG4913 423 ---ELEAEIASLERRKSNIpARLLALRDALAEALGLDEaelpfvgelievRPEEERwrgaiervlggfaltllvpPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2022 LAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAAREraereaaqSRRQVEEAERL 2101
Cdd:COG4913 500 AALRWVN-RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRF--------DYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2102 KQSAEEQAQAQaqaqaaaekLRKeaeqeaarraqaEQAALRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEE 2181
Cdd:COG4913 571 RRHPRAITRAG---------QVK------------GNGTRHEKDDRRRIRSRY-VLGFDNRAKLAALEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2182 TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQmEELGKLKARIEAenralvLRDKDSAQRLLQEEAEKMKQVA 2261
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELER------LDASSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2262 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQ 2340
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlGDAVERELRENLEERIDALRAR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2341 LAQETQGFQKTleterqrqleMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERL------YRTELATQEKVML 2414
Cdd:COG4913 782 LNRAEEELERA----------MRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeerfkeLLNENSIEFVADL 851
|
730 740
....*....|....*....|....*.
gi 1920237974 2415 VQTLETQRQQSDRDAERLREAIAELE 2440
Cdd:COG4913 852 LSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1662-1879 |
4.96e-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: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRreleAEL 1741
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA----KEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1742 AKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDA---VRQRAEAERV 1818
Cdd:TIGR02794 148 AAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEA-----KAKAEAEAKAKAEEAKAKAEAAKAKAaaeAAAKAEAEAA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1819 LAEKLAAISEATRLKTEAEIAL-KEKEAENERLRRLAEDEAFQRRLleeqAAQHKADIEARL 1879
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGSEVDKY----AAIIQQAIQQNL 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2147-2347 |
5.37e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2147 ADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE--- 2223
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2224 --------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2295
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2296 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQG 2347
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2154-2457 |
5.58e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2154 HKQFAEQALRQKAQVEQ---ELTALRLQLEEtdhQKSILDEelqrLKAEVTEAARQRGQVEEELFSLRVQME-------- 2222
Cdd:PRK04863 336 HLNLVQTALRQQEKIERyqaDLEELEERLEE---QNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLAdyqqaldv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2223 ---------------------------ELGKLKARIEAenraLVLRDKDSAQRLLQEE-----AEKMKQVAEEAARL--- 2267
Cdd:PRK04863 409 qqtraiqyqqavqalerakqlcglpdlTADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrk 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2268 ---SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2335
Cdd:PRK04863 485 iagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2336 QMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAE-MSRAQA--RAEEDARRFRKQAEDigerlyrtELATQEKV 2412
Cdd:PRK04863 565 ARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARAPAwlAAQDALARLREQSGE--------EFEDSQDV 629
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2413 M--LVQTLETQRQQSdRDAERLREAIAELEHEKDKLKQ-----EAQLLQLKS 2457
Cdd:PRK04863 630 TeyMQQLLERERELT-VERDELAARKQALDEEIERLSQpggseDPRLNALAE 680
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1461-1859 |
6.13e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1461 ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAeaelalrvqaeAEAAREKQRALQAL---------EELRLQAEE 1531
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ-----------LDQLKEQLQLLNKLlpqanlladETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1532 AERRLRQAEAERA--RQVQVALETAQRSAEAeLQSEHASFAEktaqlertLKEEHVAVVQLREEATRRAQQQAEAERARA 1609
Cdd:COG3096 898 LREELDAAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQ--------LQADYLQAKEQQRRLKQQIFALSEVVQRRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1610 EAERELERWQLKANEALRLRLQAeevaqqksltqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTA 1689
Cdd:COG3096 969 HFSYEDAVGLLGENSDLNEKLRA-------------------------------------RLEQAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1690 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA-----AAATQKRRELEAELAKVRAEmevllaskaraeeesRS 1764
Cdd:COG3096 1012 AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSR---------------RS 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1765 TSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAK----RQRQLAEEDAVRQRAEAERVL---AEKLAAISEatrlk 1833
Cdd:COG3096 1077 QLEKQLTRCEAEmdslQKRLRKAERDYKQEREQVVQAKagwcAVLRLARDNDVERRLHRRELAylsADELRSMSD----- 1151
|
410 420
....*....|....*....|....*....
gi 1920237974 1834 tEAEIALKEKEAENERLR---RLAEDEAF 1859
Cdd:COG3096 1152 -KALGALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1466-1583 |
6.61e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1466 AEEAEAQKRQAQEEAErLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAlQALEELRLQAEEAERRLRQA--EAER 1543
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARA-EAEAAYEIAEANAEREVQRQleIAER 288
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1920237974 1544 ARQVQVALETAQRsAEAELQSEHASFAEktAQLERTLKEE 1583
Cdd:COG2268 289 EREIELQEKEAER-EEAELEADVRKPAE--AEKQAAEAEA 325
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1086-1748 |
7.47e-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: 55.95 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1086 EEVLRAHEEQLKE-----AQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1160
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1161 WRERVT-------LLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAK-QRQEQIQAvPLANSQAVReQL 1232
Cdd:pfam01576 417 LQARLSeserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQeLLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1233 RQEKALLEdiERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESIIQEYVDLRTRY 1307
Cdd:pfam01576 495 EDERNSLQ--EQLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLEEKAAAY 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1308 SELS-------------TLTSQYIRFISETLRR-------MEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAHA--- 1364
Cdd:pfam01576 569 DKLEktknrlqqelddlLVDLDHQRQLVSNLEKkqkkfdqMLAEEKAISARYAEERDR-AEAEAREKETRALSLARAlee 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1365 --QAKAQAEREAQGLQRRMQEEVARREEV------------AVEAQEQKRSIQEE-------------------LQHLRQ 1411
Cdd:pfam01576 648 alEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskrALEQQVEEMKTQLEeledelqatedaklrlevnMQALKA 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1412 SSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAERLR 1484
Cdd:pfam01576 728 QFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1485 RQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERAR-QVQVALETAQRSA 1558
Cdd:pfam01576 805 AQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGKSA 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1559 eaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAE-----AERARAEAERELERWQL-KANEALRLRLQA 1632
Cdd:pfam01576 880 ---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelAAERSTSQKSESARQQLeRQNKELKAKLQE 956
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1633 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIRLR 1703
Cdd:pfam01576 957 MEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQLK 1036
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1920237974 1704 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEM 1748
Cdd:pfam01576 1037 RQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2142-2583 |
7.47e-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: 55.95 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2142 RQKQAADAEMEKHKQFAEQALRqkaqvEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV 2219
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLD-----EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2220 QMEE-------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMK----------QVAEEAARLS-VAAQEAARLRQLA 2281
Cdd:pfam01576 167 NLAEeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAeLRAQLAKKEEELQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2282 E-----EDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL--AQETQGFQKTLET 2354
Cdd:pfam01576 247 AalarlEEETAQKNNALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKTELedTLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2355 ERQRQLEMSAEAERLRLRVAEMSRAQARaeedaRRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLRE 2434
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMR-----QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2435 AIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL-------------------------------------LQETQALQQ 2477
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAeklsklqselesvssllneaegkniklskdvsslesqLQDTQELLQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2478 SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQekqqLAASMEEARRRQHEAEEGVRRQQEEL 2557
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQREL 554
|
490 500 510
....*....|....*....|....*....|
gi 1920237974 2558 ----QRLAQQQQQQEKLlaeenQRLRERLQ 2583
Cdd:pfam01576 555 ealtQQLEEKAAAYDKL-----EKTKNRLQ 579
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2787-2823 |
8.47e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 8.47e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 2787 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 2823
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2240-2677 |
9.71e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2240 LRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2319
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2320 KELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRqLEMSAEAERLRLRVAEMSRAQARAEEdarrFRKQAEDI 2397
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQ----IEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2398 GERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS---EEMQTVRQEQLLQETQA 2474
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCqqhTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2475 LQQSFLSEKDSLLQRErciEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ 2554
Cdd:TIGR00618 393 QKLQSLCKELDILQRE---QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2555 EELQRLAQQQQQQEKlLAEENQRLRERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLR 2634
Cdd:TIGR00618 470 EREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 2635 RKVPA-----QRLQEVGVLSAEELQQLAQGRTTVAELAQR-----EDVRHYLQ 2677
Cdd:TIGR00618 549 HQLTSerkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitVRLQDLTE 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2245-2461 |
9.81e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2245 SAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrqlAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQ 2324
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2325 EQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2404
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 2405 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2461
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1858-2347 |
1.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1858 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRg 1937
Cdd:COG4717 41 AFIRAMLLERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1938 tAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2017
Cdd:COG4717 116 -EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2018 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVL-ERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVE 2096
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2097 EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQA------LRQKAQVEQ 2170
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldrIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2171 ELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL-GKLKARIEAENRALVLRDKDSAQRL 2249
Cdd:COG4717 355 EAEELEEELQLEELEQEI-AALLAEAGVEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2250 LQEEAEKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQ-AVQEATRLKAEAELLQQQKELAQEqa 2327
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELeAELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALELLEEAREEYRE-- 511
|
490 500
....*....|....*....|
gi 1920237974 2328 RRLQEDKEQMAQQLAQETQG 2347
Cdd:COG4717 512 ERLPPVLERASEYFSRLTDG 531
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4127-4155 |
1.12e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.12e-06
10 20
....*....|....*....|....*....
gi 1920237974 4127 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4155
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1463-1593 |
1.14e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.96 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1463 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAER-- 1534
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1535 -RLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ----LERTLKEEHVAVVQLREE 1593
Cdd:pfam15709 411 rLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkeLEMQLAEEQKRLMEMAEE 474
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1326-1594 |
1.29e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1326 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVeaQEQKRSIQEE 1405
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM--DEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1406 LQHLRQSSEAEIQAKARQVEAAERSRLRI---------EEEIRVVRLQLEATERQRggAEGELQALRARAEEAEAQKRQA 1476
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1477 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1556
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270
....*....|....*....|....*....|....*...
gi 1920237974 1557 SAEAELQSEhasfAEKTAQLERTLKEEHVAVVQLREEA 1594
Cdd:pfam13868 272 EDEEIEQEE----AEKRRMKRLEHRRELEKQIEEREEQ 305
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1662-2035 |
1.61e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.10 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1741
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1742 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAVRQRAEAERVL 1819
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1820 AEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRLLEEQAAQhkadiearlaqlrkASESELERQKGLVED 1899
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKSQ--------------NGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1900 TLRQRRQVEEEilalkgsfEKAAAGKAELELELGRIRGTAEDtlrsKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 1979
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRRRRQE----KESEEFEKLRQKQQEAELELEELKKKREERRKLL 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1980 AEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2035
Cdd:pfam02029 294 EEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2312-2598 |
1.77e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2312 EAELLQQQKELAQEQA----RRLQEDKEQMAQQ-LAQETQgfQKTLETERQRQLEMS-----AEAERLRLRVAEMSRAQA 2381
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQErLRQEKE--EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2382 RAEEDARRFRKQAEDI-GERLYRTELATQ-EKVMLVQTLETQRQQSDrdaERLREAIAELEHEKDKLKQEAQLLQLKSEE 2459
Cdd:pfam17380 345 ERERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2460 MQTVRQEQLLQETQALQQsflsekdslLQRERCIEQEKAKLEQLfqdevakaqalreeqqRqqqqMQQEKQQLAASMEEA 2539
Cdd:pfam17380 422 MEQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2540 RRRQHEAEEGVRRQQ--EELQRLAQQQQQQEKLLAE-ENQRLRERLQHLEEERRAALARSEE 2598
Cdd:pfam17380 473 KRKKLELEKEKRDRKraEEQRRKILEKELEERKQAMiEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1330-1514 |
1.88e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.66 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1330 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveaqEQKRSIQEELQhl 1409
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA------EAKKKAEAEAA-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1410 rQSSEAEIQAKARQVEAAersrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1489
Cdd:PRK09510 177 -KKAAAEAKKKAEAEAAA----------------KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 1920237974 1490 ETQRKRQAEAELALRVQAEAEAARE 1514
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1384-2011 |
2.02e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1384 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ----------LEATERQRG 1453
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleelkeeIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1454 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEaEAAREKQRALQALEELRLQAEEAE 1533
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1534 RRLRQAEAERARQVQValetaqRSAEAELQSEHASFaEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaer 1613
Cdd:PRK03918 328 ERIKELEEKEERLEEL------KKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKR-------------------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1614 elerwqLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREarrrgkaeEQAVRQRELAEQELEKqrqlAEGTAQ--Q 1691
Cdd:PRK03918 381 ------LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL--------KKEIKELKKAIEELKK----AKGKCPvcG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1692 RLAAEQELIRLRAEteqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVraEMEVLLASKARAE----EESRSTSE 1767
Cdd:PRK03918 443 RELTEEHRKELLEE----------YTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLkelaEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1768 KSK----QRLEAEAGRFRELAEEAARLRalaeeaKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 1843
Cdd:PRK03918 511 KLKkynlEELEKKAEEYEKLKEKLIKLK------GEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1844 --EAENERLRRLAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSF--- 1918
Cdd:PRK03918 583 gfESVEELEERLKELEPFYNEYLELKDAEK--ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYsee 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1919 --EKAAAGKAELELELGRIRGTAEDTLRSKEQAEqeaarqrqlaaeeerrrreaeervqKSLAAEEEAARQRKAALEEVE 1996
Cdd:PRK03918 660 eyEELREEYLELSRELAGLRAELEELEKRREEIK-------------------------KTLEKLKEELEEREKAKKELE 714
|
650
....*....|....*
gi 1920237974 1997 RLKAKVEEARRLRER 2011
Cdd:PRK03918 715 KLEKALERVEELREK 729
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3446-3482 |
2.03e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.03e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 3446 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 3482
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2239-2592 |
2.03e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2239 VLRDKDSAQRLLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2312
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2313 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAQETQGFQKTLETER-------QRQLEMSAEAERLRLRVAEMSRAQAR 2382
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2383 AEEDARRFRKQAEDIGERlyrtelaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQT 2462
Cdd:PRK02224 340 HNEEAESLREDADDLEER-------AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2463 VRQEqllqetqalqqsFLSEKDSLLQRERCIEqekAKLEQLfQDEVAKAQALREE--------------QQRQQQQMQQE 2528
Cdd:PRK02224 413 FLEE------------LREERDELREREAELE---ATLRTA-RERVEEAEALLEAgkcpecgqpvegspHVETIEEDRER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2529 KQQLAASMEEARRRQHEAEEGVRRQQE------ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2592
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2151-2375 |
2.12e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2151 MEKHKQFAEQALR----QKAQVEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2224
Cdd:COG3206 166 LELRREEARKALEfleeQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2225 GKLKARIEAENRALVlrDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQ 2304
Cdd:COG3206 246 RAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 2305 EATRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLET--ERQRQLEMSAEAERLRLRVAE 2375
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESllQRLEEARLAEALTVGNVRVID 392
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1326-1587 |
2.49e-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: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1326 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR--REEVAVEAQEQKRSIQ 1403
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1404 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleaterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1483
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1484 RRQVQDETQRKRQAEAELALRVQAEAEAAREK----QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1559
Cdd:pfam15558 168 KVQENNLSELLNHQARKVLVDCQAKAEELLRRlsleQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 1920237974 1560 AELQSEHASFAEKTAQLERTLKEEHVAV 1587
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1661-1881 |
2.51e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.80 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1661 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRREL 1737
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1738 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1817
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1818 VLAEKLAAISEATRLKTEAEIALkeKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1881
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLM--EMAEEERLEYQRQkQEAEEKARLEAEERRQKEEEAARLAL 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1459-1733 |
2.70e-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: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1459 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQA--------LEELRLQAE 1530
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQelaaleaeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1531 EAERRLRQAEAERARQVQVALETAQRSAEAELQSehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaeaerarae 1610
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRA----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1611 aerelerwQLKANEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaq 1690
Cdd:COG4942 158 --------DLAELAALRAELEAERAELEALL----------------------AELEEERAALEALKAERQKLLAR---- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237974 1691 qrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQK 1733
Cdd:COG4942 204 ----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2246-2573 |
2.96e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2246 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2325
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2326 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERlrlRVAEMSRAQARAEEDARRFRKQAEDIGERLYrte 2405
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREI--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2406 latqeKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqllqlksEEMQTVRQEQLLQETQALQQSFLSEKDS 2485
Cdd:pfam13868 187 -----ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE--------EAEKKARQRQELQQAREEQIELKERRLA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2486 LLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQ 2565
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
....*...
gi 1920237974 2566 QQEKLLAE 2573
Cdd:pfam13868 334 ERQKKLKE 341
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1356-1484 |
3.08e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 52.74 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1356 QRQLAEAHAQ-AKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1434
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1435 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1484
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2190-2395 |
3.24e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2190 DEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSV 2269
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2270 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2341
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 2342 AQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2395
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2248-2496 |
3.28e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.90 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2248 RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2323
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2324 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAE-AERLRLRVAEMSRAQARA----EEDARRFRKQAEDIG 2398
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2399 ERLYRTELATQEKVMLVQTLETQRQQ------SDRDAERLREAIAELEhEKDKLKQ----EAQLL--QLKSEEMQTvRQE 2466
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldteMAQLRvqRLRYEDLLN-KQP 360
|
250 260 270
....*....|....*....|....*....|
gi 1920237974 2467 QLLQETQALQQSFLSEKDSLLQRERCIEQE 2496
Cdd:PRK10929 361 QLRQIRQADGQPLTAEQNRILDAQLRTQRE 390
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2163-2594 |
3.39e-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: 53.60 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2163 RQKAQVEQELTALRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALV 2239
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2240 LRDKDSAQRLLQEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2318
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2319 QKELAQEQA--RRLQEDKEQMAQQLAQETQGFQKTL----ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRK 2392
Cdd:pfam07111 347 VTSQSQEQAilQRALQDKAAEVEVERMSAKGLQMELsraqEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2393 QAEDIGERLYRTELATQE----------KVMLVQTLETQRQQSDRDAERLREAIAELEH---EKDKLKQEAQL-LQLKSE 2458
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKvhtikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQlreERNRLDAELQLsAHLIQQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2459 EMQTVRQE-------------QLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQ-LFQDEVAKAQALREEQQRQ 2521
Cdd:pfam07111 507 EVGRAREQgeaerqqlsevaqQLEQELQRAQESLASvgqQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEKVAEV 586
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 2522 QQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2594
Cdd:pfam07111 587 ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLA 663
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1872-2590 |
3.43e-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: 53.69 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1872 KADIEARLAQlRKASESELERQKGLVEDTLRQRrQVEEEILALKGSFEKAAAG-----KAELELELGRIRGTAEDTLRSK 1946
Cdd:pfam12128 199 KSMIVAILED-DGVVPPKSRLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEfntleSAELRLSHLHFGYKSDETLIAS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1947 EQAEQEA--ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2024
Cdd:pfam12128 277 RQEERQEtsAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2025 EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQS 2104
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2105 AEEQAQaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDh 2184
Cdd:pfam12128 437 EEEYRL----------KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2185 qksildEELQRLKAEVTEAARQRGQVEEELFS--------LRVQM----EELGKLKARieaenrALVLR-------DKDS 2245
Cdd:pfam12128 506 ------EALRQASRRLEERQSALDELELQLFPqagtllhfLRKEApdweQSIGKVISP------ELLHRtdldpevWDGS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2246 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2325
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2326 QARRLQEDKEQMAQQLAQETQGFQKTLETERQrqlEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQA--EDIGERLYR 2403
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLN---SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqVVEGALDAQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2404 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqLLQETQALQQSFLSEK 2483
Cdd:pfam12128 731 LALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQETWLQRR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2484 DSLLQRERCIEQEKAKLEQlfqdevakaqalreEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQ 2563
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ--------------QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
730 740
....*....|....*....|....*..
gi 1920237974 2564 QQQQEKllAEENQRLRERLQHLEEERR 2590
Cdd:pfam12128 876 KEDANS--EQAQGSIGERLAQLEDLKL 900
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1393-2228 |
3.52e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1393 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAersrLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1472
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKA----CEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1473 KRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKqraLQALEELR-LQAEEAERRLRQAEAERARQVQVAL 1551
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSRKKQMEKD-NSELELKMEKVFQGTDEQ---LNDLYHNHqRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1552 ETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL--R 1629
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLcaD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1630 LQAEEVAQQKSLTQAEAEKQKEEAEREArrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1709
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIEL----KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1710 EQQR--QLLEEELARLQREAAAATQKRRELEAELAKV------RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFR 1781
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1782 ELAEEAARLRALAEEAKRQRQ-LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEI----ALKEKEAENERLRRLAED 1856
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1857 EAFQRRLLEEQAAQHKADIEAR---------LAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKaaagkaE 1927
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK------R 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1928 LELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRR--EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2005
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2006 RRLRERAEQESaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERA 2084
Cdd:TIGR00606 805 ERKIAQQAAKL-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2085 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKL----------RKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2154
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDqqekeelissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 2155 KQfaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVtEAARQRGQVEEELFSLRVQMEELGKLK 2228
Cdd:TIGR00606 964 IQ--DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1227-1959 |
3.59e-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: 53.57 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1227 AVREQLRQEKALLEDierhGEKVEECQRFAKQyinaikdyELQLVTYKAQLepvaspakkpKVQSGsesiIQEYVDLRTR 1306
Cdd:pfam05483 96 SIEAELKQKENKLQE----NRKIIEAQRKAIQ--------ELQFENEKVSL----------KLEEE----IQENKDLIKE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1307 yselSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAQGLQRRMQEEva 1386
Cdd:pfam05483 150 ----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK---MILAFEELRVQAENARLEMHFKLKED-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1387 rreevaveaqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1466
Cdd:pfam05483 221 ----------------HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1467 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR----LQAEEAERRLRQAEaE 1542
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsFVVTEFEATTCSLE-E 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1543 RARQVQVALEtaqrSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaeaerarAEAERELERWQLKA 1622
Cdd:pfam05483 364 LLRTEQQRLE----KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK-------------ILAEDEKLLDEKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1623 NEALRLRLQAEEvaQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR-QLAEGTAQ--------QRL 1693
Cdd:pfam05483 427 FEKIAEELKGKE--QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHcdklllenKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1694 AAEQE--LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLL---ASKARAEEESRST 1765
Cdd:pfam05483 505 TQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreEFIQKGDEVKCKLdksEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1766 SEKSKQRLEAEAGRFRELAEEAAR-LRALAEEAKRQRQlaEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1844
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKnIEELHQENKALKK--KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1845 AENERL--RRLAEdEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRrqvEEEILALKGSFEKAA 1922
Cdd:pfam05483 663 IEDKKIseEKLLE-EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQS 738
|
730 740 750
....*....|....*....|....*....|....*..
gi 1920237974 1923 AGKAELELELGRIRGtaeDTLRSKEQAEQEAARQRQL 1959
Cdd:pfam05483 739 SAKAALEIELSNIKA---ELLSLKKQLEIEKEEKEKL 772
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1329-1494 |
3.66e-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: 52.54 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1329 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQH 1408
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1409 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1477
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 1920237974 1478 EEAERLRRQVQDETQRK 1494
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2151-2454 |
3.91e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2151 MEKHKQFAEQALRQKAQVEQELTAlrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKAR 2230
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2231 IEAENRALvlrdKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAarlRQLAEE--DLAQQRALaekmLKEKMQavqeatr 2308
Cdd:TIGR04523 466 LETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEK---KELEEKvkDLTKKISS----LKEKIE------- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2309 lKAEAELLQQQKELAQeqarrLQEDKEQMAQQLAQETqgfqktLETERQRQLEmsaEAERLRLRVAEMSRAQARAEEDAR 2388
Cdd:TIGR04523 528 -KLESEKKEKESKISD-----LEDELNKDDFELKKEN------LEKEIDEKNK---EIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 2389 RFRKQAEDIGERLyrtelatQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQ 2454
Cdd:TIGR04523 593 QKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1310-1565 |
4.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1310 LSTLTSQYIRFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAEREAQGLQRRMQEEVAR 1387
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1388 ReevaVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAE 1467
Cdd:COG3206 228 L----AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR--AQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1468 EAEAQKRQaqeEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAeaeRARQV 1547
Cdd:COG3206 302 ALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL---LQRLE 375
|
250
....*....|....*...
gi 1920237974 1548 QVALETAQRSAEAELQSE 1565
Cdd:COG3206 376 EARLAEALTVGNVRVIDP 393
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1761-2560 |
4.09e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1761 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIAL 1840
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1841 KEKEAENERlrrlAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKASESELERQKGLVEDTLRQR--------RQVEEEIL 1912
Cdd:pfam15921 161 KEDMLEDSN----TQIEQLRKMMLSHEGVLQ--EIRSILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1913 ALKGSF----EKAAAGKAELELELGRIRGTAEDTLrskEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 1988
Cdd:pfam15921 235 YLKGRIfpveDQLEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1989 KAA----LEEVE----RLKAKVEEARRLRERAEQESARQLQLAQ----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2056
Cdd:pfam15921 312 NSMymrqLSDLEstvsQLRSELREAKRMYEDKIEELEKQLVLANseltEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2057 QSVLERlrseaeaarraaeeaeaareraereaAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2136
Cdd:pfam15921 392 ELSLEK--------------------------EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2137 EQAALRQKQAADAEMEKHKQFAEQALRQKA---QVEQELTALRLQLEETDHQKSILDEELQR----LKAEVTEAARQRGQ 2209
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2210 VE---EELFSLRVQMEELGKLKAriEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ-EAArlrQLAEEDL 2285
Cdd:pfam15921 526 VDlklQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKA---QLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2286 AQQRALAE-KMLKEKMQAvqEATRLKAEAELLQQQK-ELAQEQARRLQEDKEqmaqqLAQETQGFQKTLETERQRQLEMS 2363
Cdd:pfam15921 601 DRRLELQEfKILKDKKDA--KIRELEARVSDLELEKvKLVNAGSERLRAVKD-----IKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2364 AEAERLRlrvaemsraqaraeedaRRFRKQAEDIGERLYRTELATQE-KVMLVQTLETQRQQSDRDAERLREA------I 2436
Cdd:pfam15921 674 EDYEVLK-----------------RNFRNKSEEMETTTNKLKMQLKSaQSELEQTRNTLKSMEGSDGHAMKVAmgmqkqI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2437 AELEHEKDKLKQEAQLLQlksEEMQTVRQEQ-LLQEtqalqqsflsEKDSLLQRERCIEQEKAKLEQlfQDEVAKAQALR 2515
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLE---EAMTNANKEKhFLKE----------EKNKLSQELSTVATEKNKMAG--ELEVLRSQERR 801
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1920237974 2516 eeqqrqqqqMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRL 2560
Cdd:pfam15921 802 ---------LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRL 837
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1346-1440 |
4.19e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.42 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1346 LAEVEAALEKQRQLAEAHAQAKAQAEREAqglqRRMQEEVARREEVAVEAQEQKRSIQEELQHLR-QSSEAEIQAKARQV 1424
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1920237974 1425 EAAERSRLRI---EEEIRV 1440
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1667-2409 |
4.24e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1667 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQrEAAAATQKrrelea 1739
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEK------ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1740 eLAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAVRQRAEAERvl 1819
Cdd:COG3096 349 -IERYQEDLEEL---TERLEEQEEVVEEAAEQLAEAEA-RLEAAEEEVDSLKS--QLADYQQAL---DVQQTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1820 aEKLAAISEATRLKTEAEIALKEKEAENERLRRlAEDEAFQRRLleeQAAQHKADIEARLAQLRKAseseLERQKGLVED 1899
Cdd:COG3096 417 -QAVQALEKARALCGLPDLTPENAEDYLAAFRA-KEQQATEEVL---ELEQKLSVADAARRQFEKA----YELVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1900 TLRQRR-QVEEEILALKGSFEKAAAGKAELELELGrirgtaedtlrskeQAEQEAARQRQLAAEEERRRREAEERVQKSL 1978
Cdd:COG3096 488 VERSQAwQTARELLRRYRSQQALAQRLQQLRAQLA--------------ELEQRLRQQQNAERLLEEFCQRIGQQLDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1979 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEA-----AQKRLQ--AEEKAHAFAVQQkeqelqQ 2051
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaAQDALErlREQSGEALADSQ------E 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2052 TLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklrkeaeqeaa 2131
Cdd:COG3096 628 VTAAMQQLLERER----------------------EATVERDELAARKQ------------------------------- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2132 rraQAEQAALRQKQAADAEMEKHKQFAEQ----------------------AL--------------------------- 2162
Cdd:COG3096 655 ---ALESQIERLSQPGGAEDPRLLALAERlggvllseiyddvtledapyfsALygparhaivvpdlsavkeqlagledcp 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2163 ---------------------------------RQ-------------KAQVEQELTALRLQLEETD---HQKSILDEEL 2193
Cdd:COG3096 732 edlyliegdpdsfddsvfdaeeledavvvklsdRQwrysrfpevplfgRAAREKRLEELRAERDELAeqyAKASFDVQKL 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2194 QRL--------------------KAEVTEAARQRGQVEEELFSLRVQM----EELGKLKARIEAENRAL----VLRDKDS 2245
Cdd:COG3096 812 QRLhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2246 AQRL--LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlKEKMQAVQEATRLKAEA---------- 2313
Cdd:COG3096 892 ADRLeeLREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQ----ADYLQAKEQQRRLKQQIfalsevvqrr 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2314 -------------------ELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQkTLETERQRQLEMSAEAERlrlRVA 2374
Cdd:COG3096 968 phfsyedavgllgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELE 1043
|
890 900 910
....*....|....*....|....*....|....*...
gi 1920237974 2375 EMS-RAQARAEEDA--RRFRKQAEDIGERLYRTELATQ 2409
Cdd:COG3096 1044 ELGvQADAEAEERAriRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2143-2328 |
4.38e-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: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2143 QKQAADAEMEKHKQFAEQALRQKAQvEQELTALRLQLEETDHQKSILDEELQRLKAEVTeaarqrgQVEEELFSLRVQME 2222
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSIK-------QVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2223 ELGK---LKARI-----EAENRALVLrdkdsaQRLLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALA 2292
Cdd:pfam05667 381 ELEKqykVKKKTldllpDAEENIAKL------QALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLE 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 1920237974 2293 E-KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2328
Cdd:pfam05667 455 EiKELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3705-3740 |
4.48e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 4.48e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1920237974 3705 RQLLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPE 3740
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1415-1594 |
4.55e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.16 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1415 AEIQAKARQVEAAERSRLRIEEEirvvrlQLEATERQRGGAEGELQALRARAEEAEAqKRQAQEEAERLRRQVQDETQRK 1494
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQ------QAEEAEKQRAAEQARQKELEQRAAAEKA-AKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1495 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1574
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180
....*....|....*....|
gi 1920237974 1575 QLERTLKEEHVAVVQLREEA 1594
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEA 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2191-2599 |
4.70e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2191 EELQRLKAEVteAARQRGQVEEELFSLRVQMEELGKLKARIEaENRALVLRDKDSAQRLLQEEAEKMKQ---VAEEAARL 2267
Cdd:PRK02224 187 GSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYE-EQREQARETRDEADEVLEEHEERREEletLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2268 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaqetQG 2347
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA----QA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2348 FQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2427
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI--------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2428 DAERLREAIAELEHEKDKLKQEAQLLQ--LKSEEMQTVRQEQLLQE------TQALQQSflSEKDSLLQRERCIEQEKAK 2499
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEatLRTARERVEEAEALLEAgkcpecGQPVEGS--PHVETIEEDRERVEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2500 LEQL------FQDEVAKAQALREEQQR--QQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLL 2571
Cdd:PRK02224 484 LEDLeeeveeVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430
....*....|....*....|....*....|....
gi 1920237974 2572 AEENQRLRERLQHLEE------ERRAALARSEEI 2599
Cdd:PRK02224 564 EEEAEEAREEVAELNSklaelkERIESLERIRTL 597
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2143-2327 |
4.98e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2143 QKQAADAEMEKHKQFAEQA--LRQKAQVEQEltalRLQLEETDHQKSildeelQRLKAEVTEAARQRGQVEEELFSLRVQ 2220
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLEKERLAA------QEQKKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2221 MEELGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEK-----MKQVAEEAARLSVAAQEAARLRQLAEE---DLAQQRAL 2291
Cdd:PRK09510 141 AAAAAKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAKkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKkaaAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237974 2292 AEKmlKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2327
Cdd:PRK09510 221 AEA--KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1323-1556 |
5.31e-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: 52.35 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQRAEERERLA--EVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvavEAQEQKR 1400
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGreERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQ---RKQCQEQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1401 SIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA------EAQKR 1474
Cdd:pfam15558 128 RLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1475 QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ----RALQALEELRL-QAEEAERRLRQAEAERARQVQV 1549
Cdd:pfam15558 208 RSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNL 287
|
....*..
gi 1920237974 1550 ALETAQR 1556
Cdd:pfam15558 288 EREKNHH 294
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3910-3947 |
5.62e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 5.62e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1920237974 3910 QRFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 3947
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
154-261 |
5.79e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 154 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 232
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1920237974 233 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1364-1586 |
6.19e-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: 51.77 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1364 AQAKAQAEREAQGLQ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRV 1440
Cdd:TIGR02794 46 GAVAQQANRIQQQKKpaaKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1441 vrlQLEATERQRggaegelqALRARAEEAEAqKRQAQEEAerlRRQVQDETQRKRQAEAelalrvQAEAEAAREKQRAL- 1519
Cdd:TIGR02794 121 ---AEEAKAKQA--------AEAKAKAEAEA-ERKAKEEA---AKQAEEEAKAKAAAEA------KKKAEEAKKKAEAEa 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1520 --QALEELRLQAEEAERRLRQAE----------AERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA 1586
Cdd:TIGR02794 180 kaKAEAEAKAKAEEAKAKAEAAKakaaaeaaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2141-2587 |
7.82e-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: 52.42 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQ-----KAQVEQELTA---LRLQLEETDHQKSI-LDEELQRLKAEVTEAARQRGQVE 2211
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQvymdlNNNIEKMILAfeeLRVQAENARLEMHFkLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2212 EELFSLRVQM-EELGKLKARI----EAENRALVLRDKDSAQ-RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2285
Cdd:pfam05483 240 KQVSLLLIQItEKENKMKDLTflleESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2286 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ--------KELAQEQARRLQEDKEQMaQQLAQETQgfQKTLETERQ 2357
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcslEELLRTEQQRLEKNEDQL-KIITMELQ--KKSSELEEM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2358 RQLEMSAEAERLRLRVAeMSRAQARAEEdarrfRKQAEDIGERLYRTElatQEKVMLVQTLETQRQQSDRDAERLREAIA 2437
Cdd:pfam05483 397 TKFKNNKEVELEELKKI-LAEDEKLLDE-----KKQFEKIAEELKGKE---QELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2438 ELEHEKDKLKQEAQLLQLKSEEMqTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQdevaKAQALREE 2517
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIEL-TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK----QIENLEEK 542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2518 QQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEE 2587
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1661-1943 |
8.21e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1661 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1740
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1741 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ----LAEEDAVRQRAEAE 1816
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1817 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL 1896
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1920237974 1897 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1943
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2169-2598 |
8.75e-06 |
|
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: 52.48 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2169 EQELTALRLQLEETDHQKSILDEElQRLKAEvtEAARQRGQVEeelfslRVQMEelGKLKariEAENRALVLRDKDSaqR 2248
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLE-EQLDEE--EAARQKLQLE------KVTTE--AKIK---KLEEDILLLEDQNS--K 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2249 LLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-KMQAVQEATRLKAEAELLQqqkelAQEQA 2327
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEeKGRQELEKAKRKLEGESTD-----LQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2328 RRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQA--RAEEDAR-RFRKQAEDIGERL--Y 2402
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEdlESERAARnKAEKQRRDLGEELeaL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2403 RTELA-TQEKVMLVQTLETQRQQsdrDAERLREAIaelehEKDKLKQEAQLLQLKSEEMQTVR--QEQLLQ--------- 2470
Cdd:pfam01576 305 KTELEdTLDTTAAQQELRSKREQ---EVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEelTEQLEQakrnkanle 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2471 -ETQALQQSFL---SEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQalreEQQRQQQQMQQEKQQLAASMEEARRRQHEA 2546
Cdd:pfam01576 377 kAKQALESENAelqAELRTLQQAKQDSEHKRKKLEGQLQELQARLS----ESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 2547 EEGVRRQQEELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEE 2598
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2300-2445 |
9.04e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 52.33 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2300 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLAQetQGFQKTLETERQRQLEMSAEAERLR 2370
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 2371 LRVAEMSRAQARAEEDARRFRKQAEdigerLYRTEL-ATQEKVMLVQTLETQRQQSDRDAERlREAIAELEHEKDK 2445
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1288-1502 |
9.05e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1288 KVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1362
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1363 --HAQAKAQAEREAQGLQRRMQeevARREEVaveaqEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrv 1440
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAP---ARREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1441 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1502
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1509-2040 |
9.23e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1509 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQS------EHASFAEKTAQLERTL 1580
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKlekevkELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1581 KEEHVAVVQLRE---EATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREA 1657
Cdd:PRK03918 248 ESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1658 RRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR--LQREA 1727
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1728 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQ-RQLAE 1805
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKElRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1806 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlRRLAEDEAFQRRLLEEqaAQHKADIEARLAQLRKA 1885
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK-EKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1886 SEsELERQKGLVEDTLRQR-----RQVEEEILALKGSFEK---AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQR 1957
Cdd:PRK03918 565 LD-ELEEELAELLKELEELgfesvEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1958 QLAAEEERRrreaeervqKSLAAEEEAARQRKAALE---EVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQ 2032
Cdd:PRK03918 644 ELRKELEEL---------EKKYSEEEYEELREEYLElsrELAGLRAELEELEKRREEIKKtlEKLKEELEEREKAKKELE 714
|
....*...
gi 1920237974 2033 AEEKAHAF 2040
Cdd:PRK03918 715 KLEKALER 722
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1211-1530 |
9.26e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1211 KQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ 1290
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1291 SGSESIIQEYVDLRTRYSELSTLTSQ---YIRFISETLRRMEeeerlaeQQRAEERERLAEVEAALEKQRQLAEAHAQAK 1367
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQeqdRAREISDSLSQLP-------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1368 AQAereaqglqrrMQEEVARReevaveaqeqkRSIQEELQhLRQSSEAEIQAKAR-QVEAAERSRLRIEEEIRVVRLQLE 1446
Cdd:PRK10929 175 LTA----------LQAESAAL-----------KALVDELE-LAQLSANNRQELARlRSELAKKRSQQLDAYLQALRNQLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1447 aTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ-------AEAEAAREKQRAL 1519
Cdd:PRK10929 233 -SQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQrmdliasQQRQAASQTLQVR 299
|
330
....*....|.
gi 1920237974 1520 QALEELRLQAE 1530
Cdd:PRK10929 300 QALNTLREQSQ 310
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
31-151 |
9.27e-06 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 48.47 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 31 RASEGKKDERDRVQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRF 97
Cdd:cd21324 12 QSSAGTQHSYSEEEKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPF 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 98 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 151
Cdd:cd21324 92 TIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3912-3950 |
9.84e-06 |
|
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: 9.84e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3912 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 3950
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1338-2042 |
1.08e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1338 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-EAQGlqrrmqeevarrEEVAVEAQEQKRSIQEELQHLRQsseae 1416
Cdd:PRK10246 168 ERAELLEELTGTEIYGQISAMVFEQHKSARTELEKlQAQA------------SGVALLTPEQVQSLTASLQVLTD----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1417 iqakarqveaaersrlriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvQDETQRKRQ 1496
Cdd:PRK10246 231 ------------------EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-------QPQLAALSL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1497 AEAELALRVQAEaeaarEKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQrsaeaELQSEHASFAEKTAql 1576
Cdd:PRK10246 286 AQPARQLRPHWE-----RIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLA-- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1577 ertlkeEHVAVVQLREE-----ATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLtqaeaekqke 1651
Cdd:PRK10246 354 ------EHDRFRQWNNElagwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQ---------- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1652 eaerearrrgKAEEQAVRQR--ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqREAAA 1729
Cdd:PRK10246 418 ----------HAEQRPLRQRlvALHGQIVPQQKRLAQ-LQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1730 ATQKRRELEAELAKVRAEMEVLL--ASKARAEEESRS-TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1806
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQAlEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1807 DAvRQRAEAERVLAEKLAAISEA--TRLKTEAEIA--LKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKADIEARLA 1880
Cdd:PRK10246 566 EA-QSLRQEEQALTQQWQAVCASlnITLQPQDDIQpwLDAQEEHERQLRLLSQRHELQGQIAAhnQQIIQYQQQIEQRQQ 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1881 QLR----------------------KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1938
Cdd:PRK10246 645 QLLtalagyaltlpqedeeaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1939 AEDTLRSK-----EQAEQEAARQRQLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEevERLKAKVEEARRLRER 2011
Cdd:PRK10246 725 QCLSLHSQlqtlqQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAAllDEETLTQLEQLK--QNLENQRQQAQTLVTQ 802
|
730 740 750
....*....|....*....|....*....|.
gi 1920237974 2012 AEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2042
Cdd:PRK10246 803 TAQALAQHQQHRPDGLDLTVTVEQIQQELAQ 833
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2258-2474 |
1.15e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2258 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2337
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2338 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKvmlvQT 2417
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 2418 LETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA 2474
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1724-2045 |
1.21e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1724 QREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAARLralaeEAKRQRQL 1803
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM-----AMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1804 AEEDAVRQRAEAERVLAEKLAAisEATRLKtEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1883
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1884 KASESELERQ-KGLVEDTLRQRRQVEEEilalkgsfekaaagKAELELELGRIRGTAEDTLRSKEQAEQEaaRQRQLAAE 1962
Cdd:pfam17380 427 AEQEEARQREvRRLEEERAREMERVRLE--------------EQERQQQVERLRQQEEERKRKKLELEKE--KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1963 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHA 2039
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRL 568
|
....*.
gi 1920237974 2040 FAVQQK 2045
Cdd:pfam17380 569 EAMERE 574
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2421-2610 |
1.42e-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: 50.92 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2421 QRQQSDRDAERLREAIAELEHEKDKLKQEAQLL--QLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2498
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALlkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2499 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME------EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2572
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237974 2573 EENQRLRERLQHLEEERRAALARSEEIAPSRAAAARAL 2610
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2309-2595 |
1.48e-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: 51.49 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2309 LKAEAELLQQQKELAQEQARRlqedkEQMAQQLAQETQGfQKTLETERQrqlemsAEAERLRLRVAEMsraqaRAEEDAR 2388
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRL-----VEMARELEELSAR-ESDLEQDYQ------AASDHLNLVQTAL-----RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2389 RFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEA----QLLQLKsEEMQTVR 2464
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQAL-EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2465 Q---------EQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQ------DEVAKAQA-------LREEQQRQQ 2522
Cdd:COG3096 430 GlpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiaGEVERSQAwqtarelLRRYRSQQA 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 2523 QQMQQEKqqLAASMEEARRRQHEAEEgVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2595
Cdd:COG3096 510 LAQRLQQ--LRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
41-140 |
1.48e-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: 47.27 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 41 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1920237974 117 LVNIRNDDIADGNPKLTLGLIWTI 140
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1803-2503 |
1.51e-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: 51.59 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1803 LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKAdiEARLAQL 1882
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLES--SREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1883 RKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaae 1962
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1963 eerrrrEAEERVQKSLAAEEEAAR---QRKAALE-EVERLKAKVE---EARRLRERAEQESARQLQLAQEAAQKRLQAEE 2035
Cdd:TIGR00606 319 ------RELVDCQRELEKLNKERRllnQEKTELLvEQGRLQLQADrhqEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2036 K-AHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQ 2114
Cdd:TIGR00606 393 KnFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2115 AQAAAEKLRKEAE---------------QEAARRAQAEQAALRQKQAADAEME----------------KHKQFAEQALR 2163
Cdd:TIGR00606 473 ILELDQELRKAERelskaeknsltetlkKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtttrtqmemltKDKMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2164 Q-KAQVEQELTAL------RLQLEETDHQKS----ILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGklkariE 2232
Cdd:TIGR00606 553 KiKSRHSDELTSLlgyfpnKKQLEDWLHSKSkeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE------D 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2233 AENRALVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQeaaRLRQLAEED-----LAQQRALAEKMLKEKMQAVQEA 2306
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQ---FITQLTDENqsccpVCQRVFQTEAELQEFISDLQSK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2307 TRLkAEAELLQQQKELAQEQARRlqEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSR--AQARAE 2384
Cdd:TIGR00606 704 LRL-APDKLKSTESELKKKEKRR--DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2385 EDARRFRKQAEDIGERLYRtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVR 2464
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQM-ELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
730 740 750
....*....|....*....|....*....|....*....
gi 1920237974 2465 QeQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2503
Cdd:TIGR00606 860 Q-HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2159-2598 |
1.52e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2159 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenral 2238
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2239 vLRDKDSAQRLLQEEAEKMKQVAEEaarlsvaaqeaaRLRQLAEedlaqQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2318
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE------------KIRELEE-----RIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2319 QKELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMsRAQARAEEDARRFRKQAED 2396
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2397 IGERLyrTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKS---------EEMQTVRQEQ 2467
Cdd:PRK03918 377 LKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--KAIEELKKakgkcpvcgRELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2468 LLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEvAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAE 2547
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 2548 EGVRRQQEELQRLAqQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2598
Cdd:PRK03918 532 EKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1304-1445 |
1.54e-05 |
|
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: 49.98 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1304 RTRYSELSTLTSQYIRFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaqakAQAEREAQglqR 1379
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKR----------YQDQLEAQ---R 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1380 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1445
Cdd:pfam12037 123 RRNEELLRKQEESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQ 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1460-1724 |
1.71e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1460 QALRARAEEAEAQKRQAQEEAERLRRQVqDETQRKRQA--EAELALRVQAEAEAAREKQRALQA-LEELRLQAEEAERRL 1536
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1537 RQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerele 1616
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI---------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1617 rwqlkanEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgKAEEQAVRQRelaEQELEKQRQLAEGTAQQRLAAE 1696
Cdd:COG3206 301 -------AALRAQLQQEAQRILASL--------------------EAELEALQAR---EASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*...
gi 1920237974 1697 QELIRLRAETeqgEQQRQLLEEELARLQ 1724
Cdd:COG3206 351 AELRRLEREV---EVARELYESLLQRLE 375
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1694-1789 |
1.77e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.49 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1694 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1773
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 1920237974 1774 EAEAGRFrELAEEAAR 1789
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1324-1540 |
1.81e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1324 TLRRMEEEERLAEQQRAEERERLAEVEAALEkqrqlaEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1403
Cdd:pfam02029 134 EIREKEYQENKWSTEVRQAEEEGEEEEDKSE------EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1404 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRV-VRLQLEATERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAE 1481
Cdd:pfam02029 208 KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLeAEQKLEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKRE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1482 RLRRQVQDETQRKRQAEAELALRVQaeaeaaREKQRALQALEelRLQAEEAERRLRQAE 1540
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREE------EEKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1374-2010 |
1.89e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1374 AQGLQR---RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATER 1450
Cdd:pfam05483 73 SEGLSRlysKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1451 QRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElaLRVQAEaeaarekqralQALEELRLQAE 1530
Cdd:pfam05483 153 TRHLCN-LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1531 EAERRLRQAEAERARQV-----QVALETAQrSAEAElqsehasfaEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAE 1605
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEIndkekQVSLLLIQ-ITEKE---------NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1606 RARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQla 1685
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR-- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1686 egTAQQRLaaeqelirlraetEQGEQQRQLLEEELARLQREAAAATQ----KRRELEaELAKVRAEMEVLLASKARAEEE 1761
Cdd:pfam05483 367 --TEQQRL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1762 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLkteaeialk 1841
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL--------- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1842 ekeaENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEI 1911
Cdd:pfam05483 500 ----ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1912 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKsLAAEEEAARQR--- 1988
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfee 654
|
650 660 670
....*....|....*....|....*....|....*...
gi 1920237974 1989 ----------------KAALEEVERLKAKVEEARRLRE 2010
Cdd:pfam05483 655 iidnyqkeiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1827-2580 |
1.91e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.37 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1827 SEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQ 1906
Cdd:NF041483 22 AEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1907 VEEEIlaLKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQ----------AEQEAARQRQLAAEEERRRREAEERVQK 1976
Cdd:NF041483 102 QTQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1977 SLAAEEEAARqrkAALEEVERLKAKVEEARRLRE----RAEQESARQLQLAQEAAQKRLQAEEKAHAF-------AVQQK 2045
Cdd:NF041483 180 LAAARAEAER---LAEEARQRLGSEAESARAEAEailrRARKDAERLLNAASTQAQEATDHAEQLRSStaaesdqARRQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2046 EQELQQTLQQEQSVLERLR-----SEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAE 2120
Cdd:NF041483 257 AELSRAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2121 KLRKEAEQEAARRAQAEQAALRQKQAAdAEMEKHKQFAEQALRQKAQVEQELTalRLQLEETDHQKSILDEELQRLKAEV 2200
Cdd:NF041483 337 ADARAEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLTKASEDAKATT--RAAAEEAERIRREAEAEADRLRGEA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2201 TEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAAR-----LSVAAQEA 2274
Cdd:NF041483 414 ADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADA 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2275 ARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLAQETQGFQKTLE 2353
Cdd:NF041483 494 DELRSTATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQ 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2354 TERQRQLE-MSAEAERlRLRVAEMSRAQARAEedARRFRKQAEDIGERLyRTELAtqekvmlvQTLETQRQQSDRDAERL 2432
Cdd:NF041483 571 AEAAEELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--------ERIRTLQAQAEQEAERL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2433 R-EAIAELEHEkdKLKQEAQLLQLKSEEMQtvRQEQLLQETQALQQSFLSEKDSLLQRercIEQEKAKleqlfqdevaka 2511
Cdd:NF041483 639 RtEAAADASAA--RAEGENVAVRLRSEAAA--EAERLKSEAQESADRVRAEAAAAAER---VGTEAAE------------ 699
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2512 qalreeqqrqqqqmqqekqQLAASMEEARRRQHEAEEGVRRQQEEL-QRLAQQQQQQEKLLAEENQRLRE 2580
Cdd:NF041483 700 -------------------ALAAAQEEAARRRREAEETLGSARAEAdQERERAREQSEELLASARKRVEE 750
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1521-1959 |
1.93e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 51.17 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1521 ALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQ---------LR 1591
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1592 EEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR 1671
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1672 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVL 1751
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1752 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATR 1831
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1832 LKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 1911
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1920237974 1912 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQL 1959
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1336-1490 |
1.96e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1336 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaqglQRRMQEEVARREEVAVEAQEQKRSIqeelqhlrqSSEA 1415
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNV---------RNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1416 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1490
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1335-1763 |
2.20e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1335 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1414
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1415 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1494
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1495 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1574
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1575 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1654
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1655 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1734
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 1920237974 1735 RELEAELAKVRAEMEVLLASKARAEEESR 1763
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2141-2346 |
2.29e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADA-----EMEKHKQFAEQALRQKaqveqeltalrlQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2206
Cdd:NF012221 1561 LADKERAEAdrqrlEQEKQQQLAAISGSQS------------QLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2207 RGQVEEElfslRVQMEELGKlKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQ--------VAEEAARLSVAAQEAAR 2276
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSEAGVAQGEQ 1703
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2277 LRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2346
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2141-2588 |
2.35e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.59 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTalrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVE-----EELF 2215
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2216 SLRVQMEELgklKARIEAENRALVLRDkDSAQRLL---QEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2292
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLemlQSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2293 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLAQETQgfqkTLETErqrqLEMSAEAERLRLR 2372
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQ----MLKTN----GLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2373 VAEMSRAQARaeedarrFRK-QAEDIGERLYRTE---LATQEKVmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQ 2448
Cdd:pfam10174 276 QMEVYKSHSK-------FMKnKIDQLKQELSKKEselLALQTKL---ETLTNQNSDCKQHIEVLKESLTAKEQRAAILQT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2449 EAQLLQLKSEEMQTV-----RQEQLLQETQALQQSFLSE-KDSLLQRERCIEQEKAKLEQL---FQDEVAKAQALREEQQ 2519
Cdd:pfam10174 346 EVDALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLqeqLRDKDKQLAGLKERVK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2520 RQQQQMQQEKQQLAaSMEEARRrqhEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2588
Cdd:pfam10174 426 SLQTDSSNTDTALT-TLEEALS---EKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPE 490
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1360-1575 |
2.45e-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: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1360 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1439
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1440 VVRLQLEATERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1499
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1500 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1575
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
39-147 |
2.46e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.52 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 109
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237974 110 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3781-3817 |
2.47e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.47e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 3781 LRLLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDT 3817
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1619-2037 |
2.59e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1619 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1698
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1699 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1778
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1779 RFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA 1858
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1859 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1938
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1939 AEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2018
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 1920237974 2019 QLQLAQEAAQKRLQAEEKA 2037
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1253-1584 |
2.96e-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: 50.40 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1253 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESIIQEYVDLRTRY-SELSTLTSQyirfiSETLRRMEEE 1331
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1332 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ----RRMQEEVArreEVAVEAQEQKRSIQEELQ 1407
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPtntyKTLELEIA---ESDVEVKKAELELVKEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1408 HLRQSSEAEIQAKAR-QVEAAERSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA--------- 1476
Cdd:NF033838 198 KEPRDEEKIKQAKAKvESKKAEATRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlgepa 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1477 -----QEEAERLRRQVQDET-------QRKRQAEAE-LALRVQAEAEAAREKQR---ALQALEELRLQAEEAERRLRQAE 1540
Cdd:NF033838 275 tpdkkENDAKSSDSSVGEETlpspslkPEKKVAEAEkKVEEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237974 1541 A----ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEH 1584
Cdd:NF033838 355 LelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2220-2600 |
3.00e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 50.38 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2220 QMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2299
Cdd:COG5281 1 AAALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2300 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2379
Cdd:COG5281 81 AAALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2380 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2459
Cdd:COG5281 161 AAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2460 MQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEA 2539
Cdd:COG5281 241 SAAAQALAALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2540 R-RRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2600
Cdd:COG5281 321 AqALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWA 382
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2141-2443 |
3.00e-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: 49.68 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHkqfAEQALRQKAQVEQELTALRLQLEETDHQksildeeLQRLKAEVTEAARQRGQVEEELFSLRVQ 2220
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2221 MEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2299
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2300 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLEterqrqlEMSAEAERLRLRVAEMSRA 2379
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRLA-------GLEADLERRTQQFQEMQRA 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 2380 QARAEEDARRFRKQAEDIGERLYRTE---LATQEKV-MLVQTLETQRQQSDRDAERLREaiaELEHEK 2443
Cdd:pfam19220 320 RAELEERAEMLTKALAAKDAALERAEeriASLSDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
934-1504 |
3.22e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 934 DRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRlpldkepaRECAQRITEQQK 1012
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR--------RELDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1013 AQAEVDGL-----GKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEE 1087
Cdd:pfam15921 431 LEALLKAMksecqGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1088 VlraheeqlkeaqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRER 1164
Cdd:pfam15921 511 A--------------------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1165 VTLLLE-------RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLR--DAKQRQEQIQAVPLANSQAvrEQLRQE 1235
Cdd:pfam15921 571 IENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGS--ERLRAV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1236 KALLEDIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesiiqeyvdLRTRYSELSTLTS 1315
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1316 qyirfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKAqaereaqglqrrMQEEVARREEVAVEA 1395
Cdd:pfam15921 714 --------TLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNA 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRSIQEELQHLRQsseaeiqakarqveaaersrlrieeeirvvRLQLEATERQRggAEGELQALRA---RAEEAEAQ 1472
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQ------------------------------ELSTVATEKNK--MAGELEVLRSqerRLKEKVAN 808
|
570 580 590
....*....|....*....|....*....|..
gi 1920237974 1473 KRQAQEEAERLRRQVQDETQRKRQAEAELALR 1504
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2157-2388 |
3.25e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.69 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2157 FAEQALRQKAQ---VEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQrgqveeelfsLRVQMEELGKLKARIEA 2233
Cdd:PRK11637 38 FSAHASDNRDQlksIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK----------LRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2234 ENRalvlrdkdSAQRLLQEEAEKMKqvaeeaarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA----VQEAtRL 2309
Cdd:PRK11637 108 LNA--------SIAKLEQQQAAQER---------LLAAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgyLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2310 KAEAELLQQQKELAQEqaRRLQEDKEQMAQQLAQETQGFQKTLETER-----------------QRQL-EMSAEAERLRL 2371
Cdd:PRK11637 170 ETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEQARnerkktltglesslqkdQQQLsELRANESRLRD 247
|
250
....*....|....*...
gi 1920237974 2372 RVAEMSR-AQARAEEDAR 2388
Cdd:PRK11637 248 SIARAEReAKARAEREAR 265
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1394-1531 |
3.30e-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: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1394 EAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQA 1461
Cdd:COG1579 21 RLEHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1462 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEE 1531
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1662-1884 |
3.58e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQRELAEQELEK-QRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRE-LEA 1739
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDmEEDLVE--------ARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1740 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1819
Cdd:COG1842 88 EALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1820 AEklaaiseatrlkteAEIALKEKEAENERLRRLAEDEAFQRRLLEeqaAQHKADIEARLAQLRK 1884
Cdd:COG1842 168 ER--------------MEEKIEEMEARAEAAAELAAGDSLDDELAE---LEADSEVEDELAALKA 215
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1083-1582 |
3.67e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1083 QEAEEVLRAHEEQlkeaQAVPATLPELEATKAALKK-LRAQAEAQQpvfdaLRDELRGAQEVG-------ERLQQRHGER 1154
Cdd:PRK04863 496 DVARELLRRLREQ----RHLAEQLQQLRMRLSELEQrLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1155 ----DVEVERWRERVTLLlerwQAVLAQTDVRQRELEQLGRQLRYYRESADPL----GAWLRDAKQRQEQIQ--AVPLAN 1224
Cdd:PRK04863 567 leslSESVSEARERRMAL----RQQLEQLQARIQRLAARAPAWLAAQDALARLreqsGEEFEDSQDVTEYMQqlLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1225 SQAVREQLRQEK-ALLEDIER----HGEKVEECQRFAKQ-------------------YINA-------------IKDYE 1267
Cdd:PRK04863 643 LTVERDELAARKqALDEEIERlsqpGGSEDPRLNALAERfggvllseiyddvsledapYFSAlygparhaivvpdLSDAA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1268 LQLVT--------YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSelstltsqyiRFISETL-RRMEEEERLAEQQ 1338
Cdd:PRK04863 723 EQLAGledcpedlYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYS----------RFPEVPLfGRAAREKRIEQLR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1339 RaeERERLAEveaalekqrqlaeahaqAKAQAEREAQGLQRRMQE---------EVARREEVAVEAQEQKRSIQEELQHL 1409
Cdd:PRK04863 793 A--EREELAE-----------------RYATLSFDVQKLQRLHQAfsrfigshlAVAFEADPEAELRQLNRRRVELERAL 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1410 RQSSEAEIQAKARQVEAAERSRL--------------RIEEEIRVVRLQLEATE------RQRGGA----EGELQALRAR 1465
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSAlnrllprlnlladeTLADRVEEIREQLDEAEeakrfvQQHGNAlaqlEPIVSVLQSD 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1466 AEEAEAQKR---QAQEEAERLRRQVQDET---QRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQA 1539
Cdd:PRK04863 934 PEQFEQLKQdyqQAQQTQRDAKQQAFALTevvQRRAHFSYEDAAEMLAKNSDLNEKLR--QRLEQAEQERTRAREQLRQA 1011
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1920237974 1540 EAERARQVQValetaqrsaEAELQSEHASFAEKTAQLERTLKE 1582
Cdd:PRK04863 1012 QAQLAQYNQV---------LASLKSSYDAKRQMLQELKQELQD 1045
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1371-1565 |
3.87e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.02 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1371 EREAQGLQRRMQEEVarreEVAVEAQEQKRSIQEELQhlrqsseaEIQAKARqveaAERSRL--RIE-EEIRVVRLQLEA 1447
Cdd:PTZ00491 643 ERTRDSLQKSVQLAI----EITTKSQEAAARHQAELL--------EQEARGR----LERQKMhdKAKaEEQRTKLLELQA 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1448 TerqrgGAEGELQAlRARAE-EAEAQKRQAQEEAErlrrqVQDETQRKRqaeaelALRVQAEAEAAREKQRALQALEELR 1526
Cdd:PTZ00491 707 E-----SAAVESSG-QSRAEaLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQ 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237974 1527 LQAE---EAERRLRQAEAERARQVQVAL--ETAQRSAEA--ELQSE 1565
Cdd:PTZ00491 770 AQNEleiAKAKELADIEATKFERIVEALgrETLIAIARAgpELQAK 815
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1387-1740 |
3.93e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1387 RREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1466
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1467 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1546
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1547 VQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1626
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1627 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1706
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 1920237974 1707 EQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1740
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
846-1496 |
3.96e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 846 NQEAQEAIARlEAQHQALVALWhQLHTEMKSLLAWQSLGRDMQlirsWSLATFRTLKPEE------------QRQALRsL 913
Cdd:TIGR00618 223 VLEKELKHLR-EALQQTQQSHA-YLTQKREAQEEQLKKQQLLK----QLRARIEELRAQEavleetqerinrARKAAP-L 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 914 ELHYQAFLRDSQDAGGFGPEDRLQaEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRL 993
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 994 PLDKEPARECAQRIT----EQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAptlRSELELTLGKLEQVRSLSAIYL 1069
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA---KKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1070 EKLKtisLVIRSTQEAEEVLRAHEEQLKEAQAVpaTLPELEATKAALKKLRAQAEAQQPVFDALR---------DELRGA 1140
Cdd:TIGR00618 452 QCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1141 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakqRQEQIQAV 1220
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1221 PLansqaVREQLRQEKALLEDIERHGEKVEECQRFAK--QYINAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESIIQ 1298
Cdd:TIGR00618 598 DL-----TEKLSEAEDMLACEQHALLRKLQPEQDLQDvrLHLQQCSQELALKLTALHALQ--LTLTQERVREHALSIRVL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1299 EYVDLRTRYSELSTLTSQY--IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQG 1376
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1377 LQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1456
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE 830
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1920237974 1457 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ 1496
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
937-1375 |
4.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 937 QAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRITE 1009
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1010 QQKAQAEVDGLGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVL 1089
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1090 R------AHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRE 1163
Cdd:COG4717 233 EneleaaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1164 RVTLLLERWQAVLAQTDVRQREleqlgrQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIE 1243
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE-AGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1244 RHGEKVEECQRFaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELstltSQYIRFISE 1323
Cdd:COG4717 386 ELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL----REELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1324 TLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQ 1375
Cdd:COG4717 461 ELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3334-3372 |
4.42e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.09 E-value: 4.42e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3334 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3372
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1321-1545 |
4.53e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1321 ISETLRRMEEEERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQglqRRMQEEVARREEVavEAQEQKR 1400
Cdd:pfam02029 100 VAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVRQAE---EEGEEEEDKSEEA--EEVPTEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1401 SIQEELQHLRQSSEAEIQAKARQVEaaERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEA 1480
Cdd:pfam02029 174 FAKEEVKDEKIKKEKKVKYESKVFL--DQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL-EAEQKL 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1481 ERLRRQVQD------ETQRKRQAEAELALrvqAEAEAAREKQRAL--------QALEELRLQAEEAERRLRQAEAERAR 1545
Cdd:pfam02029 251 EELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKREERRKLleeeeqrrKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3334-3369 |
4.68e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.68e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1920237974 3334 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3369
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1335-1732 |
4.99e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1335 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEElqhlrqsse 1414
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1415 aeiqaKARQVEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1494
Cdd:COG3064 75 -----AAKKLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1495 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1574
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1575 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1654
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1655 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1732
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLA 381
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1811-2201 |
4.99e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1811 QRAEAERVLAEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadIEARLAQLRKASESEL 1890
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAA-----IYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1891 ERQKglVEDTLRQRRQVEEEilalkgsfekaaagkaELELELGRIRGTaeDTLRSKEQAEQEAARQRqlaaeeerrrrea 1970
Cdd:pfam17380 351 ERIR--QEERKRELERIRQE----------------EIAMEISRMREL--ERLQMERQQKNERVRQE------------- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1971 EERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKeqel 2049
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK---- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2050 qqtlqqeqsvleRLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2129
Cdd:pfam17380 474 ------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2130 aarraqaeqaalRQKQaadAEMEKHKQFAEQALRqkaqVEQELTALRLQLEETDHQKSILDEELQRLKAEVT 2201
Cdd:pfam17380 542 ------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1069-1537 |
5.30e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.35 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1069 LEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpVFDALRDELRGAQEVGERLQ 1148
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1149 QRHGERDVEVERWRERVTLLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLRDAKQRQEQIqavpl 1222
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1223 ANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQ 1290
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlRSPE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1291 SGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL---------- 1359
Cdd:pfam05557 280 DLSRRIEQLQQREIVLKEENSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgy 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1360 ------------AEAHAQAKAQAEREAQGLQRRMQ---EEVARREEVAVEA----QEQKRSIQEELQHLRQ--------S 1412
Cdd:pfam05557 359 railesydkeltMSNYSPQLLERIEEAEDMTQKMQahnEEMEAQLSVAEEElggyKQQAQTLERELQALRQqesladpsY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1413 SEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DE 1490
Cdd:pfam05557 439 SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKR 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920237974 1491 TQRKRQAEAELALRVQAEAEAAREKQralqaLEELRLQAEEAERRLR 1537
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4120-4148 |
5.31e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.31e-05
10 20
....*....|....*....|....*....
gi 1920237974 4120 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4148
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1501-1770 |
5.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1501 LALRVQAEAEAAREKQRALQALEElRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTL 1580
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1581 KEEHVAVVQLREeatrraqqqaeaeRARAEAERELERWQLKANEALRLRLQAEEVAQqksltqaeaekqKEEAEREARRR 1660
Cdd:COG4942 90 KEIAELRAELEA-------------QKEELAELLRALYRLGRQPPLALLLSPEDFLD------------AVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1661 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1740
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260 270
....*....|....*....|....*....|
gi 1920237974 1741 LAKVRAEMEVLLASKARAEEESRSTSEKSK 1770
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
43-144 |
5.69e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.49 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 43 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1631-1807 |
5.80e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1631 QAEEVAQQKsltQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1706
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1707 EQGEQQRQLLEEELArlQREAAAATQKRRELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1781
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 1920237974 1782 ELAEEAARLRALAEEAKRQRQLAEED 1807
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1685-2181 |
5.83e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.47 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1685 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV----------RAEMEVLLAS 1754
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1755 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKT 1834
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1835 EAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 1914
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1915 KGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1994
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1995 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAA 2074
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2075 EEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2154
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 1920237974 2155 KQFAEQALRQKAQVEQELTALRLQLEE 2181
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2141-2591 |
5.94e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFA--EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSL 2217
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTklQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTlDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2218 R----VQMEELGKLKARIEA-ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---------RLRQLAEE 2283
Cdd:pfam12128 307 NgelsAADAAVAKDRSELEAlEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKhqdvtakynRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2284 DLA------QQRALAEKMLKEKMQAVQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLAQETQGfQKTLET 2354
Cdd:pfam12128 387 QNNrdiagiKDKLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2355 ERQRQLEMSAEAERLRLRVAEMSRAQaraeEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQ-RQQSDRDAERLR 2433
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQ----SELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2434 EAIAELEHEKDKLKQEAQL----LQLKSEEMQTVRQEQLLQETQALQQSflsEKDSLLQRERCIEQEKAKLEQLFQDEVA 2509
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLhrtdLDPEVWDGSVGGELNLYGVKLDLKRI---DVPEWAASEEELRERLDKAEEALQSARE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2510 KAQALreeqqrqqqqmQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLA----QQQQQQEKLLAEENQRLRERLQHL 2585
Cdd:pfam12128 619 KQAAA-----------EEQLVQANGELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKALAERKDSANERLNSL 687
|
....*.
gi 1920237974 2586 EEERRA 2591
Cdd:pfam12128 688 EAQLKQ 693
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1321-1526 |
6.00e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1321 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-REEVAVEAQEQK 1399
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1400 RSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1474
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1475 ------QAQEEAERLRRQVqDETQRKRQAEAELALR--VQAEAEAAREKQRALQALEELR 1526
Cdd:COG1842 156 sgidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
181-258 |
6.06e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.60 E-value: 6.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 181 DNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 258
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1671-2383 |
6.16e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1671 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQ-REAAAATQK-RRELEAELA--- 1742
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKiLRELDTEISylk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1743 ----KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1817
Cdd:pfam15921 238 grifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1818 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQL-----RKASESELER 1892
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEK 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1893 QK-----------GLVEDTLRQR---RQVEEEIL-ALKGSFEKAAAGkaELELELGRIRGtaedtlrSKEQAEQEAARQR 1957
Cdd:pfam15921 398 EQnkrlwdrdtgnSITIDHLRRElddRNMEVQRLeALLKAMKSECQG--QMERQMAAIQG-------KNESLEKVSSLTA 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1958 QLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEEVER-LKAKVEEARRLRERAEQesarQLQLAQEaaqkrLQAE 2034
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLEssERTVSDLTASLQEKERaIEATNAEITKLRSRVDL----KLQELQH-----LKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2035 EKaHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraereaaqsrRQVEEAERLkqsaeeqaqaqaq 2114
Cdd:pfam15921 540 GD-HLRNVQTECEALKLQMAEKDKVIEILR----------------------------QQIENMTQL------------- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2115 aqaaaeklrkeaeqeaarraqaeqaalrqkqaadaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQ 2194
Cdd:pfam15921 578 ------------------------------------VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2195 RLKAEVTEAARQRGQV----EEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEE-AARL 2267
Cdd:pfam15921 622 ELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKlKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2268 SVAAQEAARLR---QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAqe 2344
Cdd:pfam15921 702 KSAQSELEQTRntlKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS-- 779
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1920237974 2345 tqgfqkTLETERQR---QLE-MSAEAERLRLRVAEMSRAQARA 2383
Cdd:pfam15921 780 ------TVATEKNKmagELEvLRSQERRLKEKVANMEVALDKA 816
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1412-1625 |
6.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1412 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1489
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1490 -ETQRKRQAEAELAL------------RVQAEAEAAREKQRALQALEELRLQAEEAerrlrQAEAERARQVQVALETAQR 1556
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1557 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEA 1625
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1292-1594 |
6.71e-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: 48.91 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1292 GSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQ--------RQLAEAH 1363
Cdd:pfam19220 63 AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA-LERQlaaeteqnRALEEEN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1364 AQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRsiqeeLQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRL 1443
Cdd:pfam19220 142 KALREEAQAAEKALQRAEGELATARERLALLEQENRR-----LQALSEEQAAELAELTRRLAELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1444 QL--EATERQRGGAEGELQALRARAEEAEAQKRQaqeEAERLRRQVQDetqrkrQAEAELALRVQAEAEAAREKQRalqA 1521
Cdd:pfam19220 217 QLaaEQAERERAEAQLEEAVEAHRAERASLRMKL---EALTARAAATE------QLLAEARNQLRDRDEAIRAAER---R 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1522 LEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSE--HASFAEKTAQLERTlkEEHVAVVQLREEA 1594
Cdd:pfam19220 285 LKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEmlTKALAAKDAALERA--EERIASLSDRIAE 357
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3115-3151 |
6.92e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.92e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 3115 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKET 3151
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1808-2019 |
6.98e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1808 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIeARLAQLRKASE 1887
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-AELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1888 SELERQKGLVEDTL----RQRRQVEEEILALKGSFEKAAAGKA-------ELELELGRIRGTAEDTLRSKEQAEQEAARQ 1956
Cdd:COG4942 97 AELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 1957 RQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2019
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2253-2388 |
6.99e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2253 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2332
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 2333 DKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2388
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1388-1548 |
7.72e-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: 48.98 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1388 REEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1467
Cdd:pfam07111 490 RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELT 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1468 EAEAQKRQAQEEA-----ERLRRQVQDETQ-----RKRQAEAELALRvQAEAEAAREKQRAlqalEELRLQAEEAerrlR 1537
Cdd:pfam07111 570 QQQEIYGQALQEKvaeveTRLREQLSDTKRrlneaRREQAKAVVSLR-QIQHRATQEKERN----QELRRLQDEA----R 640
|
170
....*....|..
gi 1920237974 1538 QAEAER-ARQVQ 1548
Cdd:pfam07111 641 KEEGQRlARRVQ 652
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1983-2327 |
7.95e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1983 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2054
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2055 qeqsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArra 2134
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEA--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2135 qaeqaalRQKQAADAEMEKhkqfaeqalrqkaqvEQELTALRLQLEETDHQKSILDEElqrlkaevtEAARQRGQVEeel 2214
Cdd:pfam17380 433 -------RQREVRRLEEER---------------AREMERVRLEEQERQQQVERLRQQ---------EEERKRKKLE--- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2215 fslrvqMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK 2294
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
330 340 350
....*....|....*....|....*....|....*..
gi 1920237974 2295 MLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2327
Cdd:pfam17380 553 RIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1456-1590 |
8.13e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.22 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1456 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERR 1535
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1536 LRQAEAERARQ-VQVALETAQRSAEAELQSE-HA---SFAEKTAQLERTLKEEHVAVVQL 1590
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlHQlteTLIQKQTMLEALSTEKNSLVLQL 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2160-2387 |
8.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2160 QALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKL--KARIEAENRA 2237
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2238 LVLRDKDSAQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2315
Cdd:COG3883 93 RALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2316 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2387
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1806-2284 |
8.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1806 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLleEQAAQHKADIEARLAQLRKA 1885
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1886 seselerqkglvedtLRQRRQVEEEILALKgsfEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEER 1965
Cdd:COG4717 155 ---------------LEELRELEEELEELE---AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1966 RRREAEervqKSLAAEEEAARQRKAALEEVERLKakveearRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQK 2045
Cdd:COG4717 217 EAQEEL----EELEEELEQLENELEAAALEERLK-------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2046 EQELQQTLQQEQSVLERLRseaeaarraaeeaEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKE 2125
Cdd:COG4717 286 LALLFLLLAREKASLGKEA-------------EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2126 AEQEAARRAQAEQAALRQKQAADaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQ-KSILDEELQRLKAEVTEAA 2204
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2205 RQR-GQVEEELFSLRVQMEELGKLKARIEAENRAlvLRDKDSAQRLLQEEAE---KMKQVAEEAARLSVAAQEAARLRQL 2280
Cdd:COG4717 431 EEElEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1920237974 2281 AEED 2284
Cdd:COG4717 509 YREE 512
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1858-2383 |
9.80e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.10 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1858 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEkAAAGKAELELELGRIRG 1937
Cdd:COG3321 867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA-LLALVALAAAAAALLAL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1938 TAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2017
Cdd:COG3321 946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2018 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2097
Cdd:COG3321 1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2098 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2177
Cdd:COG3321 1106 LLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2178 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEElgklkARIEAENRALVLRDKDSAQRLLQEEAEKM 2257
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAA-----ALALLALAAAAAAVAALAAAAAALLAALA 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2258 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2337
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1920237974 2338 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARA 2383
Cdd:COG3321 1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1495-1779 |
1.08e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1495 RQAEAELALRVQAEAEAAREKQR--ALQAleelRLQAEEAER--RLRQAEAERARQVQVALETAQRSAEAELQSEHASFA 1570
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAReaRHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1571 EKTAQlertlKEEHVAVVQLREEATRRAQQQAEAERARAEAERelerwQLKANEALRLRLQAEEVAQQKSLTqaeAEKQK 1650
Cdd:PRK05035 508 IKAGA-----RPDNSAVIAAREARKAQARARQAEKQAAAAADP-----KKAAVAAAIARAKAKKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1651 EEAEREARRRGKAEEQAvrqRELAEQELEKQRQLAEGTAQQRLAAEQELIrLRAETEQGEQQRQLLEEElarlqreaaAA 1730
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAI-ARAKAKKAEQQANAEPEE---------PV 641
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1920237974 1731 TQKRRELEAELAKVRAEmevlLASKARAEEESRSTSEKSKQRLEAEAGR 1779
Cdd:PRK05035 642 DPRKAAVAAAIARAKAR----KAAQQQANAEPEEAEDPKKAAVAAAIAR 686
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1665-2375 |
1.10e-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: 48.56 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR-----LQREAAAATQKRRELEA 1739
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1740 ELAKVR---AEMEVLLASKARAEEESRSTSEKSkqRLEAEAgrfrELAEEAARLRALAEEAKRQRQlaeedavrqraEAE 1816
Cdd:pfam05483 177 EREETRqvyMDLNNNIEKMILAFEELRVQAENA--RLEMHF----KLKEDHEKIQHLEEEYKKEIN-----------DKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1817 RVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRLLEeQAAQHKADIEARLAQLRKASESELERQKGL 1896
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1897 VED---TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEerrrreaeer 1973
Cdd:pfam05483 316 EEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1974 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEK-AHAFAVQqkeqeLQ 2050
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ-----LT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2051 QTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqea 2130
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM----------------------------- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2131 arraqaeQAALRQKQAadaEMEKHKQFAEQALRQKAQVEQELTALRLQLE--------ETDHQKSILD---EELQRLKAE 2199
Cdd:pfam05483 512 -------TLELKKHQE---DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2200 VTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEeaarLSVAAQEAARLRQ 2279
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE----LASAKQKFEEIID 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2280 LAEEDLAQQRALAEKMLKEKMQA---VQEATRLKAEAELLQQQK--------ELAQEQARRLQEDKEQ---MAQQLAQET 2345
Cdd:pfam05483 658 NYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIDKRCQHKiaemvalmEKHKHQYDKIIEERDSelgLYKNKEQEQ 737
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1920237974 2346 QGFQKTLETER----------QRQLEMS-AEAERLRLRVAE 2375
Cdd:pfam05483 738 SSAKAALEIELsnikaellslKKQLEIEkEEKEKLKMEAKE 778
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1467-1546 |
1.20e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.41 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1467 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE------AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1539
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvaleglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 1920237974 1540 EAERARQ 1546
Cdd:PRK11448 218 RKEITDQ 224
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
44-141 |
1.20e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 44 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 110
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1920237974 111 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 141
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1982-2595 |
1.25e-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: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1982 EEAARQRKAALEEVERLKAKVEEARRlreraeqeSARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqSVLE 2061
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERYAAARERL--------------------AELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2062 RLRSEAEAARRAAEEAEAARERAEREAAQSRRQvEEAERLKQsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2141
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELRAELARLE-AELERLEA-----------------RLDALREELDELEAQIRGNGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2142 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETdhqKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2221
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2222 EELGKLKARIEAENRALVLRDKDSAQRLLQeeaekMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2296
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLA-----LRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2297 ------KEKMQAVQEAT-RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETE--RQRQLEMSAEAE 2367
Cdd:COG4913 489 ltllvpPEHYAAALRWVnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgRRFDYVCVDSPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2368 RLRLRVAEMSRA-QARAeeDARRFRKQAEDIGERLYRTELATQEKvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKL 2446
Cdd:COG4913 569 ELRRHPRAITRAgQVKG--NGTRHEKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2447 KQEAQLLQ-LKSEEMQTVRQEQLLQETQALQQsflsekdsllQRERcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQM 2525
Cdd:COG4913 644 QERREALQrLAEYSWDEIDVASAEREIAELEA----------ELER-LDASSDDLAAL-EEQLEELEAELEELEEELDEL 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 2526 QQEKQQLAASMEEARRRQHEAEEGVRRqQEELQRLAQQQQQQEKLLAEENQRLRERL-QHLEEERRAALAR 2595
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRAR 781
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1469-1594 |
1.33e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1469 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR----QAEAERA 1544
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAlkqkQAEEAAA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1545 RQVQVA----------LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1594
Cdd:PRK09510 140 KAAAAAkakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1141-1546 |
1.34e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1141 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAV 1220
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1221 planSQAVREQLRQEKALLED---IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE--- 1294
Cdd:TIGR00606 774 ----LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIElnr 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1295 SIIQEYVD-LRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR---------AEERERLAEVEAALEKQRQLAEAHA 1364
Cdd:TIGR00606 850 KLIQDQQEqIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevqslireiKDAKEQDSPLETFLEKDQQEKEELI 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1365 QAKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1444
Cdd:TIGR00606 930 SSKETSNKKAQDKVNDIKEKV---KNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1445 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALrvqaeaeAAREKQRALQALEE 1524
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKRNHVLALGRQKG 1079
|
410 420
....*....|....*....|..
gi 1920237974 1525 LRLQAEEAERRLRQAEAERARQ 1546
Cdd:TIGR00606 1080 YEKEIKHFKKELREPQFRDAEE 1101
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2164-2407 |
1.36e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2164 QKAQVEQELTALRLQleetdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2243
Cdd:TIGR02794 44 DPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2244 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAELLQ 2317
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2318 QQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedI 2397
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA---I 272
|
250
....*....|
gi 1920237974 2398 GERLYRTELA 2407
Cdd:TIGR02794 273 QQNLYDDPSF 282
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1331-1560 |
1.40e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.67 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1331 EERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELqhlr 1410
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1411 qsSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1490
Cdd:PRK07735 86 --TEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1491 TQRKRQAEAELALrvqaeaEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1560
Cdd:PRK07735 164 KAKAKAAAAAKAK------AAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2157-2323 |
1.40e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.54 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2157 FAEQALrqkAQVEQELTALRLQLEETDHQKSILDEElqrlkAEVTEAARQRGQVEEELFSLRVQMEELgklkarieaenR 2236
Cdd:COG3524 181 FAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL-----------R 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2237 AlVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEAE 2314
Cdd:COG3524 242 S-YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEAA 317
|
....*....
gi 1920237974 2315 llQQQKELA 2323
Cdd:COG3524 318 --RQQRYLA 324
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2251-2349 |
1.46e-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: 47.19 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2251 QEEAEKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKMQavQEATRLKAEAELLQQQKElaQ 2324
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKME--EERENLLKEQERALESKL--K 266
|
90 100
....*....|....*....|....*
gi 1920237974 2325 EQARRLQEDKEQMAQQLAQETQGFQ 2349
Cdd:cd16269 267 EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2158-2547 |
1.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2158 AEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT--EAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2235
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2236 RALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKekmQAVQEATRLKAEAEL 2315
Cdd:COG4717 156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2316 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLET----------------------ERQRQLEMSAEAERLRLRV 2373
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgllallfllLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2374 AEMSRAQARAEEDARRFRKQAEDIGER---LYRTELATQEKVMLVQTLETQRQQSDRDAER---LREAIAELEHEKDKLK 2447
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEElleLLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2448 QEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQ 2527
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|
gi 1920237974 2528 EKQQLAASMEEARRRQHEAE 2547
Cdd:COG4717 472 AELLQELEELKAELRELAEE 491
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3078-3114 |
1.46e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.46e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 3078 KLLSAEKAVTGYKDPYSGQSVSLFQALKKGLIPREQG 3114
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1665-1860 |
1.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1741
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1742 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1806
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1807 DAVRQRAEAERVLAEKLAAIS-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1860
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1404-1778 |
1.51e-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: 47.97 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1404 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEAT----ERQRGGAEGELQALRARAEEAEAQKRQAQEE 1479
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1480 AERL---RRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAERRLRQAEAERaRQVQVALETAQ- 1555
Cdd:pfam07888 110 SEELseeKDALLAQRAAHEARIRELEEDIKTLTQRVLERE---TELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1556 --RSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLqaE 1633
Cdd:pfam07888 186 elRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV-EGLGEEL--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1634 EVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1713
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1714 QLLEEELArlqREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1778
Cdd:pfam07888 342 EKLEVELG---REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1294-1505 |
1.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1294 ESIIQEYVDLRTRYSelSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERL------AEVEAALEKQRQLAEAHAQAK 1367
Cdd:COG3206 155 NALAEAYLEQNLELR--REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlsEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1368 AQAeREAQGLQRRMQEEVARREEVAVEA-------------QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI 1434
Cdd:COG3206 233 AEL-AEAEARLAALRAQLGSGPDALPELlqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1435 EEEIRVVRLQLEATERQRGGAEGELQALRARAE---EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRV 1505
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2158-2592 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2158 AEQALRQKAQVEQELTALRLQL-------EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLK-A 2229
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApA 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2230 RIEAENRALVLRD------KDSA------QRLLQEE----------AEKMKQVAEEAARLSVAA-QEAARLRQLAE---- 2282
Cdd:COG3096 604 WLAAQDALERLREqsgealADSQevtaamQQLLEREreatverdelAARKQALESQIERLSQPGgAEDPRLLALAErlgg 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2283 -------EDLAQQRA-LAEKMLKEKMQA--VQEATRLKAEAE----------LLQQQKELAQEQARRLQEDKEQMAQQLA 2342
Cdd:COG3096 684 vllseiyDDVTLEDApYFSALYGPARHAivVPDLSAVKEQLAgledcpedlyLIEGDPDSFDDSVFDAEELEDAVVVKLS 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2343 QETQGFQKTLE------TERQRQLE-MSAEAERLRLRVAEMS---RAQARAEEDARRFrkqaedIGERLYRTELATQEKV 2412
Cdd:COG3096 764 DRQWRYSRFPEvplfgrAAREKRLEeLRAERDELAEQYAKASfdvQKLQRLHQAFSQF------VGGHLAVAFAPDPEAE 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2413 MlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQsflsEKDSLLQRERC 2492
Cdd:COG3096 838 L--AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELRE----ELDAAQEAQAF 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2493 IEQEKAKLEQLfqdeVAKAQALReeqqrqqqQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2572
Cdd:COG3096 912 IQQHGKALAQL----EPLVAVLQ--------SDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLL 979
|
490 500
....*....|....*....|....
gi 1920237974 2573 EENQ----RLRERLQHLEEERRAA 2592
Cdd:COG3096 980 GENSdlneKLRARLEQAEEARREA 1003
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3950-3984 |
1.64e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.64e-04
10 20 30
....*....|....*....|....*....|....*
gi 1920237974 3950 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3984
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1696-1846 |
1.72e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1696 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1774
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1775 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEdavrQRAEAERVLAEKLAAISEATRlKTEAEIALKEKEAE 1846
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEA----ELAELEAELEEKKAELDEELA-ELEAELEELEAERE 166
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1778-2024 |
1.90e-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: 47.58 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1778 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1857
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1858 AFQRRLLEEQAAQHKADIE------ARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELE 1931
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIReleediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1932 LGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2010
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 1920237974 2011 RAEQESAR-QLQLAQ 2024
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2162-2602 |
2.02e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2162 LRQKAQVEQ-ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIeaenralvl 2240
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2241 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2320
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2321 ELAQEQARRLQEDKEQMAQQLAQET--QGFQKTLETERQRQLEMSAEAERLRlrvAEMSRAQARAEEDARRFRKQAEDIG 2398
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2399 ERL--YRTELAT--QEKVMLVQTLETQRQQSD----------------------------RDAERLREAIAELEHEKDKL 2446
Cdd:PRK01156 416 VKLqdISSKVSSlnQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeksnhiinhynEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2447 KQEAQLLQ-----LKSEEM-QTVRQEQLLQETQALQQSFLSE----KDSLLQRERCIEQEKA-KLEQLFQDEVAKAQALR 2515
Cdd:PRK01156 496 DEKIVDLKkrkeyLESEEInKSINEYNKIESARADLEDIKIKinelKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2516 EEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG-----------VRRQQEELQRLaqqqqQQEKLLAEENQRLRERLQH 2584
Cdd:PRK01156 576 VISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddksyidksIREIENEANNL-----NNKYNEIQENKILIEKLRG 650
|
490
....*....|....*...
gi 1920237974 2585 LEEERRAALARSEEIAPS 2602
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPD 668
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4259-4292 |
2.21e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.21e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237974 4259 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4292
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2156-2602 |
2.30e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2156 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2235
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2236 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2315
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2316 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2395
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2396 DIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL 2475
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2476 QQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2555
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1920237974 2556 ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2602
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1294-1638 |
2.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1294 ESIIQEYVDLRTRYSELST---LTSQYIRFISETLRRMEEEERLAE-QQRAEE-RERLAEVEAALEKQRQLAEAHAQAKA 1368
Cdd:COG4717 98 EELEEELEELEAELEELREeleKLEKLLQLLPLYQELEALEAELAElPERLEElEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1369 QAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQ---- 1444
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAALEERLKEARllll 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1445 --------------LEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1506
Cdd:COG4717 254 iaaallallglggsLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1507 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV----------------------QVALETAQRSAEAELQS 1564
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaeeYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1565 -----EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLQAEEVAQQ 1638
Cdd:COG4717 414 llgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ-ELEELKAELRELAEE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2361-2595 |
2.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2361 EMSAEAERLRLRVAEMSRAQARAEeDARRFRKQAEDIgERLYRTELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAE 2438
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE-DAREQIELLEPI-RELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2439 LEHEKDKLKQEAQLLQLKSEEMQtvrqEQLLQETQALQQSFLSEKDSLlqrERCIEQEKAKLEQLFQdevaKAQALREEQ 2518
Cdd:COG4913 300 LRAELARLEAELERLEARLDALR----EELDELEAQIRGNGGDRLEQL---EREIERLERELEERER----RRARLEALL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 2519 QRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQqqqekllaeenQRLRERLQHLEEERRAALAR 2595
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-----------RDLRRELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2363-2611 |
2.74e-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: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2363 SAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHE 2442
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2443 KDKLKQEAQLLQLKSEEMQTVRQEQLLqetqaLQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2522
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2523 QqmqqEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2602
Cdd:COG4942 174 A----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*....
gi 1920237974 2603 RAAAARALP 2611
Cdd:COG4942 250 ALKGKLPWP 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1457-1679 |
2.75e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1457 GELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDETQRKRQAEAElalRVQAEAEAAREKQRALQALEELRlQAEEAERR 1535
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQrKKKEQQQAEELQQKQAAEQERLKQLEKE---RLAAQEQKKQAEEAAKQAALKQK-QAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1536 LRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerel 1615
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA--------------------- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1616 erwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1679
Cdd:PRK09510 200 ---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1356-1535 |
2.97e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1356 QRQLAEAHAQAK---AQAEREAQglqrrmqeevARREEVAVEAqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERsRL 1432
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAE----------AIKKEALLEA-------KEEIHKLRNEFEKELRERRNELQKLEK-RL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1433 RIEEEIrvVRLQLEATERQRGGAEGELQALRARAEEAEAQkrqaQEEAERLRRQVQDETQR-----KRQAEAELALRVqa 1507
Cdd:PRK12704 92 LQKEEN--LDRKLELLEKREEELEKKEKELEQKQQELEKK----EEELEELIEEQLQELERisgltAEEAKEILLEKV-- 163
|
170 180
....*....|....*....|....*....
gi 1920237974 1508 EAEAAREKQRALQALEElrlQA-EEAERR 1535
Cdd:PRK12704 164 EEEARHEAAVLIKEIEE---EAkEEADKK 189
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
933-1594 |
3.00e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 933 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQK 1012
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1013 AQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1092
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1093 EEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQE-------VGERLQQRHGERDVEVERWRERV 1165
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRIISAHGRLG 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1166 TLLLERWQAVLAQTDVRQRELEQLG-----RQLRYYRESADPLGAWLRDAKQRQEQIQAVPLA---NSQAVREQLRQEKA 1237
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATAdeveeRQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleIDPILNLAQLDKAT 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1238 LLEDIERHGEKV----EECQRFAKQYINAiKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTL 1313
Cdd:pfam02463 613 LEADEDDKRAKVvegiLKDTELTKLKESA-KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1314 TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVA 1392
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSrLKKEEKEEEKSELSL 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1393 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrLQLEATERQRGGAEGELQALRARAEEAEAQ 1472
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1473 KRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1552
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1920237974 1553 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1594
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1662-1874 |
3.01e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRRE 1736
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1737 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1793
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1794 AEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRlLEEQAAQHKA 1873
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-ADAKGAKQDE 1776
|
.
gi 1920237974 1874 D 1874
Cdd:NF012221 1777 S 1777
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1662-1855 |
3.08e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1741
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1742 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1821
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 1920237974 1822 KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 1855
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2141-2315 |
3.36e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEE---LFSL 2217
Cdd:PRK09510 80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEakrAAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2218 RVQMEELGKLKARIEAENRALVLRDK----DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAE 2293
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEAKKkaeaEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAE 239
|
170 180
....*....|....*....|..
gi 1920237974 2294 KmlKEKMQAVQEATRLKAEAEL 2315
Cdd:PRK09510 240 K--AAAAKAAEKAAAAKAAAEV 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1753-1950 |
3.54e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1753 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAVRQRAEAERVLAEKLAAISEATRL 1832
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1833 KTEAEIALKEKEAENerlrrlAEDEAfQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 1912
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237974 1913 ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAE 1950
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1665-1912 |
3.62e-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: 46.21 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRREL 1737
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1738 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEE--DAVRQRAE 1814
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEarNQLRDRDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1815 AERVLAEKLaaiSEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1894
Cdd:pfam19220 277 AIRAAERRL---KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
|
250
....*....|....*...
gi 1920237974 1895 GLveDTLRQRRQVEEEIL 1912
Cdd:pfam19220 354 RI--AELTKRFEVERAAL 369
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1669-2385 |
3.73e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1669 RQRELAEQEleKQRQLAEGTAQQRLAAEQ-ELIRLRAeTEQGEQQRQLLEeelaRLQREAAAATQKRR---ELEAELAKV 1744
Cdd:PRK10246 251 RLDELQQEA--SRRQQALQQALAAEEKAQpQLAALSL-AQPARQLRPHWE----RIQEQSAALAHTRQqieEVNTRLQST 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1745 RAEMEVLLASKARAEEESRSTSEKSKQRLeAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQRAEAERvlaEKLA 1824
Cdd:PRK10246 324 MALRARIRHHAAKQSAELQAQQQSLNTWL-AEHDRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQLTHAE---QKLN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1825 AISEATRLKTEAEIAlkekeaenERLRRLAEDEAFQRRLLEEQaAQHkADIEARLAQLrKASESELERQKGLVEDTLRQR 1904
Cdd:PRK10246 398 ALPAITLTLTADEVA--------AALAQHAEQRPLRQRLVALH-GQI-VPQQKRLAQL-QVAIQNVTQEQTQRNAALNEM 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1905 RQVEEEilalkgsfekaaagKAElelELGRIRGTAEDTLRSKEQAEQEAarQRQLAAEEERRRREAEERVQKSLAAEEEA 1984
Cdd:PRK10246 467 RQRYKE--------------KTQ---QLADVKTICEQEARIKDLEAQRA--QLQAGQPCPLCGSTSHPAVEAYQALEPGV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1985 ARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERL 2063
Cdd:PRK10246 528 NQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNITLQPQDDIQPWL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2064 rseaeaarraaeeaeaareraereaaqsrrqvEEAERLKQsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaEQAALRQ 2143
Cdd:PRK10246 603 --------------------------------DAQEEHER---------------------------------QLRLLSQ 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2144 KQAADAEMEKH----KQFAEQALRQKAQVEQELTALRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRGQVE--EEL 2214
Cdd:PRK10246 618 RHELQGQIAAHnqqiIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQqlTPL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2215 FSLRVQMEELGKLKARIEAEN------RALVLRDKDSA--QRLLQEEAEKMKQVAEEAARL--SVAAQEAARLRQLAEED 2284
Cdd:PRK10246 698 LETLPQSDDLPHSEETVALDNwrqvheQCLSLHSQLQTlqQQDVLEAQRLQKAQAQFDTALqaSVFDDQQAFLAALLDEE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2285 LAQQralAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQK--TLETERQRQLEM 2362
Cdd:PRK10246 778 TLTQ---LEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLREntTRQGEIRQQLKQ 854
|
730 740
....*....|....*....|....
gi 1920237974 2363 SAEA-ERLRLRVAEMSRAQARAEE 2385
Cdd:PRK10246 855 DADNrQQQQALMQQIAQATQQVED 878
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1394-1529 |
3.79e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.19 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1394 EAQEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQleateRQRGGAEGELQALRARAEEAE 1470
Cdd:COG1566 87 QAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEARAALDAAQ 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1471 AQKRQAQEEAERLRRQVQDETQrKRQAEAELAlrvQAEAEAAREKQRalqaLEELRLQA 1529
Cdd:COG1566 162 AQLEAAQAQLAQAQAGLREEEE-LAAAQAQVA---QAEAALAQAELN----LARTTIRA 212
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1662-1833 |
3.82e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLeeelarlqreaaaatqkrrELEAE 1740
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLL-------------------ELQAE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1741 LAKVRAemevllASKARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVL 1819
Cdd:PTZ00491 708 SAAVES------SGQSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAK 778
|
170
....*....|....
gi 1920237974 1820 AEKLAAIsEATRLK 1833
Cdd:PTZ00491 779 AKELADI-EATKFE 791
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3001-3038 |
3.83e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.83e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1920237974 3001 RRALRGSGVIAGVWLEEAGQKLSIYEALRKDLLQPEAA 3038
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2148-2344 |
3.86e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2148 DAEMEKHKQFAEQALR---QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQR------GQVEEELFSLR 2218
Cdd:PRK11281 55 EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2219 VQMEELGklKARIEAENRALVLRDK--------DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAeedLAQQRA 2290
Cdd:PRK11281 135 DQLQNAQ--NDLAEYNSQLVSLQTQperaqaalYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL---LNAQND 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2291 LAEKMLK--EKMQAVQEATR--LKAEAELLQQQKELAQE--QARRLQEDKEQMAQQLAQE 2344
Cdd:PRK11281 210 LQRKSLEgnTQLQDLLQKQRdyLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQEAQSQD 269
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1661-1842 |
4.02e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1661 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRRELEA 1739
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1740 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDavrqrAEAERV 1818
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 1920237974 1819 LAEKLAAISEATRLKTEAEIALKE 1842
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3409-3445 |
4.26e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.26e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 3409 KLLSAEKAVTGYRDPYSGSTISLFQAMKKGLVLREHG 3445
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1302-1582 |
4.29e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1302 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQrAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1381
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEEL-SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1382 QEEVARREEVAVEAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGE 1458
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1459 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE-KQRALQALEELRLQAE- 1530
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 1531 EAERRLRQAEAERARQVQVALETAQR-SAEAELQSEHASFAEKTAQLERTLKE 1582
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1354-1485 |
4.32e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.88 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1354 EKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1431
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1432 LRIEEEIRVVRLQLEATERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1485
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2241-2411 |
4.41e-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: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2241 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR-LKAEAELLQQQ 2319
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAkAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2320 KELAQEQARrlqEDKEQMAQQLAQetqgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGE 2399
Cdd:TIGR02794 145 KEEAAKQAE---EEAKAKAAAEAK-----KKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
|
170
....*....|..
gi 1920237974 2400 RLYRTELATQEK 2411
Cdd:TIGR02794 217 AAAAAAAEAERK 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1416-1583 |
4.43e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1416 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvQDETQRKR 1495
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1496 QAEAelalrVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVQ--VALETAQRSAEAELQSEHASFAEK 1572
Cdd:COG1579 90 EYEA-----LQKEIESLKRRISDLeDEILELMERIEELEEELAELEAELAELEAelEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|.
gi 1920237974 1573 TAQLERTLKEE 1583
Cdd:COG1579 165 REELAAKIPPE 175
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1662-1891 |
4.60e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL--------ARLQR 1725
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARpdnsaviaAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1726 EAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1800
Cdd:PRK05035 527 KAQARARQAEKQAAAaadpkKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1801 RQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAedeafqrrlleeqAAQHKAdiEARLA 1880
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVA-------------AAIARA--KARKA 660
|
250
....*....|.
gi 1920237974 1881 QLRKASESELE 1891
Cdd:PRK05035 661 AQQQANAEPEE 671
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1586-2041 |
4.88e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.55 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1586 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEE 1665
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1666 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR 1745
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1746 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA 1825
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1826 ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRR 1905
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1906 QVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 1985
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1986 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2041
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1412-1546 |
4.93e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1412 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDET 1491
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 1492 QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1546
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2428-2558 |
4.95e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2428 DAERLREAIAELEHEKDKLKQEAQLLqlkseemqtvrqEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQDE 2507
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2508 V--AKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGV-------RRQQEELQ 2558
Cdd:PRK00409 579 IkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKekkkkkqKEKQEELK 638
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1329-1594 |
5.15e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.57 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1329 EEEERLAEQQRAEERER----------LAEVEAALEKQR---QLAEAHAQAKAQAEREAQGLQRR----MQEEVARREEV 1391
Cdd:PRK10811 507 EEAMALPSEEEFAERKRpeqpalatfaMPDVPPAPTPAEpaaPVVAAAPKAAAATPPAQPGLLSRffgaLKALFSGGEET 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1392 AVEAQEQKRSIQEElqhlRQSSEaeiQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1471
Cdd:PRK10811 587 KPQEQPAPKAEAKP----ERQQD---RRKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1472 QKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvQAEAEAarekqralQALEELRLQAEEAERRLRQAEAERAR------ 1545
Cdd:PRK10811 660 EVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA--------LNVEEQSVQETEQEERVQQVQPRRKQrqlnqk 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1546 ---QVQVALETAQRSAEAELQSEHASfAEKTAQLERTLKEEHVAVVQLREEA 1594
Cdd:PRK10811 729 vriEQSVAEEAVAPVVEETVAAEPVV-QEVPAPRTELVKVPLPVVAQTAPEQ 779
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1403-1761 |
5.17e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1403 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1482
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1483 LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAEL 1562
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1563 QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLT 1642
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1643 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1722
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920237974 1723 LQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1761
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3370-3405 |
5.61e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.61e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1920237974 3370 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3405
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2268-2546 |
5.75e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2268 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAqETQG 2347
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2348 FQKTLETERQRQLEMSAEAERlrlrvaemsraqARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2427
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR------------DAILEESRAVTKELTTLAQGL--------------DALDSQATYAGE 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2428 DAERLREAIAE--LEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSllqrerciEQEKAKLEQLFQ 2505
Cdd:NF012221 1642 SGDQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQDID 1713
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237974 2506 DEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRR-QHEA 2546
Cdd:NF012221 1714 DAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1652-1815 |
5.94e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1652 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREaaaat 1731
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE----- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1732 QKRRELEAELaKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAVRQ 1811
Cdd:COG2268 301 REEAELEADV-RKPAE-----AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEA 372
|
....
gi 1920237974 1812 RAEA 1815
Cdd:COG2268 373 AAKP 376
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3041-3074 |
6.19e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.19e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237974 3041 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPE 3074
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1690-1958 |
6.44e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1690 QQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKS 1769
Cdd:PRK11637 53 QQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1770 KQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedavrqraeAERVLAeKLAAISEAtRLKTEAEialkekeaener 1849
Cdd:PRK11637 127 AAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQETIAE------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1850 LRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVedtlrqrrqveeeilALKGSFEKAAAGKAELE 1929
Cdd:PRK11637 175 LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT---------------GLESSLQKDQQQLSELR 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1920237974 1930 LELGRIRGT-AEDTLRSKEQAEQEA-------ARQRQ 1958
Cdd:PRK11637 240 ANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1986-2475 |
7.07e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1986 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2065
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2066 EAeaarraaeeaeaareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArraqaeqaalRQKQ 2145
Cdd:COG4717 144 LP-------------------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLE----------QLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2146 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA-EVTEAARQRGQVEEELFSLRVQMEEL 2224
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2225 GKLKARI------EAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2298
Cdd:COG4717 269 LSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2299 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKtleTERQRQLEMSAEAERLRLRVAEMSR 2378
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL---KEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2379 AQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAER--LREAIAELEHEKDKLKQEAQLLQLK 2456
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELeeLKAELRELAEEWAALKLALELLEEA 505
|
490
....*....|....*....
gi 1920237974 2457 SEEMQTVRQEQLLQETQAL 2475
Cdd:COG4717 506 REEYREERLPPVLERASEY 524
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1661-1783 |
7.24e-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: 44.81 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1661 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1734
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1735 RELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1783
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1318-1582 |
7.53e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1318 IRFISETLRRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREAQGLQrrmqeevarreevavEAQ 1396
Cdd:pfam00038 20 VRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLR---------------LAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1397 EQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQA 1476
Cdd:pfam00038 85 EDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1477 QEEAERLRRQVQDETQ-------RKRQAEAELA-LRVQAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEAERA 1544
Cdd:pfam00038 141 EEEVRELQAQVSDTQVnvemdaaRKLDLTSALAeIRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEIT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1545 ---RQVQ-------------VALETAQRSAEAELQSEHASFAEKTAQLERTLKE 1582
Cdd:pfam00038 221 elrRTIQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2145-2468 |
7.77e-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: 45.29 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2145 QAADAEMEKHKQFAEQALRQKAQVEQELtalRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2224
Cdd:pfam13868 16 LAAKCNKERDAQIAEKKRIKAEEKEEER---RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2225 GKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2304
Cdd:pfam13868 93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE-FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2305 EATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGF---QKTLETERQRQLEMSAEAERLRLRVAEMSRA 2379
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRaqQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2380 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2459
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR-LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
|
....*....
gi 1920237974 2460 MQTVRQEQL 2468
Cdd:pfam13868 331 IEEERQKKL 339
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1076-1731 |
7.85e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1076 SLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAEAQqpvfdalRDELR-GAQEVGERLQQRHGE 1153
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAENA-------RLEMHfKLKEDHEKIQHLEEE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1154 RDVEVERWRERVTLLLerwqavlAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakQRQEQIQAVPLANSQAVREQLR 1233
Cdd:pfam05483 231 YKKEINDKEKQVSLLL-------IQITEKENKMKDLTFLLEESRDKANQL--------EEKTKLQDENLKELIEKKDHLT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1234 QEkalLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYK-AQLEPVASPAK---------KPKVQSGSESIIQEYVDL 1303
Cdd:pfam05483 296 KE---LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAahsfvvtefEATTCSLEELLRTEQQRL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1304 RTRYSELSTLTSQYIRFISEtLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAEREAQGLQRRMQE 1383
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSE-LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-EKIAEELKGKEQELIFLLQAREK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1384 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEiqaKARQVEAAERSRLRIEEEIRVVR------LQLEATERQRGGAEG 1457
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE---KLKNIELTAHCDKLLLENKELTQeasdmtLELKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1458 ELQALRARAEEAEAQKRQAQEEAERLRR---QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAE 1533
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEnKCNNLKKQIENKN 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1534 RRLRQAEAE-RARQVQVALETAQRSA--------EAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaea 1604
Cdd:pfam05483 608 KNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKA------- 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1605 eraraeaerelerwQLKANEALRLRLQAEEVAQQKsltqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL 1684
Cdd:pfam05483 681 --------------KAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1920237974 1685 AEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1731
Cdd:pfam05483 736 EQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1662-2043 |
8.60e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1741
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1742 AKVRAEMEVLLASKARAEEESRSTSEKSK--QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1819
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKaeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1820 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVED 1899
Cdd:COG3064 180 AALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1900 TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 1979
Cdd:COG3064 260 LGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEA 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1980 AEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2043
Cdd:COG3064 340 ALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2193-2344 |
8.62e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2193 LQRLKAEVTEAARQR----GQVEEELfsLRVQMEELGKLKaRIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLS 2268
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkkkeQQQAEEL--QQKQAAEQERLK-QLEKE-RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2269 VAAQEAARLRQLAEEDLAQQrALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQE 2344
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAKKAaaeAKKKAEAEAAAKAAAEAKKKA---EAEAKKKAAAEAKK 217
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1326-1514 |
8.63e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1326 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEE 1405
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1406 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1485
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180
....*....|....*....|....*....
gi 1920237974 1486 QVQDETQRKRQAEAELALRVQAEAEAARE 1514
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRDGDDGEGRGG 260
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2164-2503 |
8.89e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2164 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT-------EAARQRGQVEEELFSLRVQMEELGKLKARIEAENR 2236
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2237 AL-----VLRDKDSAQRLLQEEAEKMK----QVAEEAARLSVAAQEAARLRQLAEE---DLAQQRALAEKMLKEKMQAVQ 2304
Cdd:TIGR04523 198 KLelllsNLKKKIQKNKSLESQISELKkqnnQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2305 EATR-----------LKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLAQETQGFQKTLETERQR 2358
Cdd:TIGR04523 278 QNNKkikelekqlnqLKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2359 QLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAE 2438
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 2439 LEHEKDKLKQEAQLLQLKSEEMQTVRqEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2503
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2144-2432 |
9.03e-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: 45.71 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2144 KQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAaRQRGQVEEELfslRVQMEE 2223
Cdd:COG3096 402 QQALDVQQTRAIQY-QQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAA---RRQFEK 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2224 LGKLKARIEAEnralVLRDK--DSAQRLLQEEAEKMKQvaeeAARLSVAAQEAARLRQLAEEdlaQQRA--LAEKMLKEK 2299
Cdd:COG3096 477 AYELVCKIAGE----VERSQawQTARELLRRYRSQQAL----AQRLQQLRAQLAELEQRLRQ---QQNAerLLEEFCQRI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2300 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRA 2379
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL-EQLRARIKELAARAPAWLAAQDALERLR----EQSGE 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 2380 QARAEEDARRFRKQAedigerLYRTELATQEKvmlvQTLETQRQQSDRDAERL 2432
Cdd:COG3096 621 ALADSQEVTAAMQQL------LEREREATVER----DELAARKQALESQIERL 663
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2004-2455 |
9.08e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.73 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2004 EARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2083
Cdd:COG4995 3 ALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2084 AEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALR 2163
Cdd:COG4995 83 AALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2164 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2243
Cdd:COG4995 163 AALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2244 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2323
Cdd:COG4995 243 LAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2324 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYR 2403
Cdd:COG4995 323 LLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2404 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2455
Cdd:COG4995 403 LAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQL 454
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1327-1443 |
9.49e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1327 RMEEEERLAEQQRAEERERLAEVEA---ALEKQ-RQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-----REEVAVEAQE 1397
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKlkeELEEKkEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiikelRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237974 1398 QKRS-IQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1443
Cdd:PRK00409 604 VKAHeLIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1665-1946 |
9.64e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1744
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1745 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1824
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1825 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 1904
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237974 1905 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSK 1946
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1335-1496 |
9.88e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1335 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1414
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1415 AEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1494
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 1920237974 1495 RQ 1496
Cdd:PRK12678 216 EE 217
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4369-4406 |
1.10e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1920237974 4369 QRFLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTA 4406
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1318-1561 |
1.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1318 IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQE 1397
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1398 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR-------AraeEAE 1470
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1471 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA 1550
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250
....*....|.
gi 1920237974 1551 LETAQRSAEAE 1561
Cdd:COG3883 255 AGAAAGSAGAA 265
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2355-2600 |
1.13e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2355 ERQRQLEMSAEA-ERLRLRVAEMSRAQARAEEDARRFRKQAEdigerlYRTELATQEKVMLVQTLETQRQQsdrdAERLR 2433
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERQLKSLERQAEKAERYKE------LKAELRELELALLVLRLEELREE----LEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2434 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQR-ERCIEQEKAKLEQLFQDEVAKAQ 2512
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKELYALANEISRlEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2513 ALREeqqrqqqqmqqekqqLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2592
Cdd:TIGR02168 324 QLEE---------------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
....*...
gi 1920237974 2593 LARSEEIA 2600
Cdd:TIGR02168 389 AQLELQIA 396
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
603-695 |
1.18e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.16 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 603 HGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQA 682
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1920237974 683 ALQTQWSWMLQLC 695
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1394-1747 |
1.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1394 EAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK 1473
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1474 RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA---RQVQVA 1550
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslqEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1551 LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRL 1630
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1631 QAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1710
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 1920237974 1711 QQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE 1747
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1336-1463 |
1.23e-03 |
|
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: 44.11 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1336 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAqAEREaqglqRRMQEEVARREEVavEAQEQKRSIQEELQHLRQSSEA 1415
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEA-AEQE-----RKLLEEQQRELEQ--KLEDQERSYEEHLRQLKEKMEE 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1920237974 1416 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1463
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2141-2598 |
1.23e-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: 45.12 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2216
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2217 LRVQMEELGKLKARIEAENRALVLRDKDSaqrllqEEAEKMKqvaEEAARLSVAAQEAARLRqlaeEDLAQQRALAEKML 2296
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDS------EIVKNSK---SELARIPELEKELERLR----EHNKHLNENIENKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2297 KEKMQAVQEATRLkaeaellqQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKT-------------LETERQRQLEMS 2363
Cdd:pfam05557 225 LLKEEVEDLKRKL--------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTglnlrspedlsrrIEQLQQREIVLK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2364 AEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE-----------LATQEKVMLVQTLE------TQRQQSD 2426
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKalvrrlqrrvlLLTKERDGYRAILEsydkelTMSNYSP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2427 RDAERLREA----------IAELEHEKDKLKQEA----QLLQLKSEEMQTVRQeqllQETQALQQSFLSEKDSLLQRERC 2492
Cdd:pfam05557 377 QLLERIEEAedmtqkmqahNEEMEAQLSVAEEELggykQQAQTLERELQALRQ----QESLADPSYSKEEVDSLRRKLET 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2493 IEQEKAKLEQlfQDEVAKAQALREEQQRQQQQMQQEKQQLaasmeearrRQHEAEEGVRRQQEELQRLAqqqqqqeklla 2572
Cdd:pfam05557 453 LELERQRLRE--QKNELEMELERRCLQGDYDPKKTKVLHL---------SMNPAAEAYQQRKNQLEKLQ----------- 510
|
490 500
....*....|....*....|....*.
gi 1920237974 2573 EENQRLRERLQHLEEERRAALARSEE 2598
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPET 536
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1466-1850 |
1.23e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1466 AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAR---EKQRALQALEELRLQAEEAERRLRQAEAE 1542
Cdd:PRK10929 104 TDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQLTALQAESA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1543 RARQVQVALETAQRSAE-----AELQSEhaSFAEKTAQLERTLkeehvavvqlreeatrraqqqaeaeraraeaereler 1617
Cdd:PRK10929 184 ALKALVDELELAQLSANnrqelARLRSE--LAKKRSQQLDAYL------------------------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1618 wqlkanEALRLRLQAEevaqqksltqaeaekqkeeaerearrrgkaeeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQ 1697
Cdd:PRK10929 225 ------QALRNQLNSQ-----------------------------------RQRE-AERALESTELLAEQSGDLPKSIVA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1698 ELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRREleaELAKVRAEMEVLLASKARAE----EESRSTSEKSKQRL 1773
Cdd:PRK10929 263 QFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQVRQ---ALNTLREQSQWLGVSNALGEalraQVARLPEMPKPQQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1774 EAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---------------ISEATRLK--- 1833
Cdd:PRK10929 339 DTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTqrellnsllsggdtlILELTKLKvan 413
|
410
....*....|....*...
gi 1920237974 1834 TEAEIALKE-KEAENERL 1850
Cdd:PRK10929 414 SQLEDALKEvNEATHRYL 431
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1459-1558 |
1.24e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1459 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElALRVQAEAEAAREKQRALQALEelrlqaEEAERR 1535
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 1920237974 1536 LRQAEAERARQVQVALETAQRSA 1558
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1661-2043 |
1.27e-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: 45.00 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1661 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1733
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1734 RRELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRqlaEEDA 1808
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPR---DEEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1809 VRQrAEAErVLAEKlaaiSEATRLKteaEIALKEKEAENERLRRLaedEAFQRRLLEEQAAQHKADIEARLAqlRKASES 1888
Cdd:NF033838 206 IKQ-AKAK-VESKK----AEATRLE---KIKTDREKAEEEAKRRA---DAKLKEAVEKNVATSEQDKPKRRA--KRGVLG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1889 ELERQKGLVEDTLRQRRQVEEEIL---ALKGSFEKAAAGKAELELElGRIRGTAEDTLR-----SKEQAEQEAARqrqla 1960
Cdd:NF033838 272 EPATPDKKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKVEEAK-KKAKDQKEEDRRnyptnTYKTLELEIAE----- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1961 aeEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA---KVEEARRLRERAEQESARQLQLAQEAAQKrlQAEEKA 2037
Cdd:NF033838 346 --SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEEDKVKEK--PAEQPQ 421
|
....*.
gi 1920237974 2038 HAFAVQ 2043
Cdd:NF033838 422 PAPAPQ 427
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1407-1695 |
1.35e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1407 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqleateRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1486
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1487 VQDETQRKRQAEAELALRVQAEAEAAREK----------QRALQALEELR-LQAEEAERRLRQAEAERARQVQVALETAQ 1555
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKAKKAAATQPivikagarpdNSAVIAAREARkAQARARQAEKQAAAAADPKKAAVAAAIAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1556 RSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERElerwqlkANEALRLRLQAEEV 1635
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------AVAAAIARAKAKKA 629
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1636 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1695
Cdd:PRK05035 630 EQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1343-1594 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1343 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1422
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1423 QVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1502
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1503 LRVQAEAEAAREKQRAlqaleELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELqsehasfAEKTAQLERTLKE 1582
Cdd:pfam13868 172 EAEREEIEEEKEREIA-----RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-------AEKKARQRQELQQ 239
|
250
....*....|..
gi 1920237974 1583 EHVAVVQLREEA 1594
Cdd:pfam13868 240 AREEQIELKERR 251
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2750-2786 |
1.41e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 2750 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 2786
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1763-1911 |
1.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1763 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1841
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1842 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1911
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1331-1576 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1331 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQ----------EEVARREEVAVEAQEQKR 1400
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAelkeelrqsrEKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1401 SIQEE---LQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1477
Cdd:pfam07888 112 ELSEEkdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1478 EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVAleTAQRS 1557
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA--AQRDR 269
|
250
....*....|....*....
gi 1920237974 1558 AEAELQSEHASFAEKTAQL 1576
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQL 288
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
38-141 |
1.54e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 38 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 95
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1920237974 96 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 141
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2194-2388 |
1.75e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2194 QRLKAEVTEAARQRGQVEEElfslrvqmeelgklkarieaenralvlrdkdsaQRLLQEEAEKMKQVAEEAARLSVAAQE 2273
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQ---------------------------------RRLQQEQLERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2274 AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKE---QMAQQLAQETQG 2347
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQrqkELEMQLAEEQKR 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237974 2348 FQKTLETERQRQLEMSAEAERLRLRVAEMSRaqARAEEDAR 2388
Cdd:pfam15709 468 LMEMAEEERLEYQRQKQEAEEKARLEAEERR--QKEEEAAR 506
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2304-2382 |
1.83e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.93 E-value: 1.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 2304 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQETqgfqKTLETERQRQLEMSAEAERLRLRVAEMSRAQAR 2382
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQA----KALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1444-1907 |
1.92e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1444 QLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE 1523
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1524 ELRLQAEEAERRLRQAEAERARQVQValETAQRSAE--AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1601
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKA--EEAKRKAEeeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1602 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1681
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1682 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1761
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1762 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1841
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1842 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQV 1907
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1403-1593 |
2.07e-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: 42.73 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1403 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1482
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1483 LRRQVQDetqRKRQAEAELALRVQAEA----EAAREKQRALQALEELRLQAE-EAERRLRQAEAERARQVQVALETaqrs 1557
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSreveEAKRAFEEKLESFEQLQAQFEqEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237974 1558 aeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREE 1593
Cdd:pfam15665 152 ----QRAQSASSLAEQEKLEELHKAELESLRKEVED 183
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1329-1593 |
2.09e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1329 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA-----------QGL-----------QRRMQEEVA 1386
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpsgqggldeeEAFldrtakreerrQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1387 RREEVAVEAQEQKRSIQEELQHlRQSSEAEIQAKARQVEaAERSRLRIEEEIRVVRL---QLEATERQRGGAEGELQALR 1463
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKEN-NEEEENSSWEKEEKRD-SRLGRYKEEETEIREKEyqeNKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1464 ARAEEAEAQKRQAQEEAERLRRQVQDE---------------TQRKRQA--EAELALRVQAEAEAAREKQRALQALE-EL 1525
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvfldqkrghPEVKSQNgeEEVTKLKVTTKRRQGGLSQSQEREEEaEV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1526 RLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE--KTAQLERTLKEEHVAVVQLREE 1593
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREErrKLLEEEEQRRKQEEAERKLREE 312
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2416-2599 |
2.14e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2416 QTLETQRQQSDR----DAERLREAIAELEHEKDKLKqeaqllqlKSEEMQTVRQEQLLQETQ--ALQQSFLSEKDSLLQR 2489
Cdd:pfam17380 281 QKAVSERQQQEKfekmEQERLRQEKEEKAREVERRR--------KLEEAEKARQAEMDRQAAiyAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2490 ERcIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEK 2569
Cdd:pfam17380 353 IR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190
....*....|....*....|....*....|.
gi 1920237974 2570 LLAEENQRL-RERLQHLEEERRAALARSEEI 2599
Cdd:pfam17380 432 ARQREVRRLeEERAREMERVRLEEQERQQQV 462
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1805 |
2.14e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 848 EAQEAIARLEAQHQALVAlwhQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQDA 927
Cdd:pfam01576 219 DLQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELE-AQISELQEDLESERAARNKAEKQR 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 928 GGFGPE-DRLQAEREYGSCSRHYQQLLQSleQGEQEESRCQRCISElkdirlqleacETRtVHRLRLPLDKEPARECAQR 1006
Cdd:pfam01576 295 RDLGEElEALKTELEDTLDTTAAQQELRS--KREQEVTELKKALEE-----------ETR-SHEAQLQEMRQKHTQALEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1007 ITEQQKaQAEVDGLGKGVARLSAEAEkVLALPEPSPAAPTLRSELELTLGKLE-QVRSLSAIYLEKLKtislvirstQEA 1085
Cdd:pfam01576 361 LTEQLE-QAKRNKANLEKAKQALESE-NAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESER---------QRA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1086 EEVLRAHEEQLkEAQAVPATLPELEATKAALKKLRAQAEAQ-QPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1164
Cdd:pfam01576 430 ELAEKLSKLQS-ELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1165 VtlllerwqavlaqtdVRQRELEqlgRQLRyyresadPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIEr 1244
Cdd:pfam01576 509 E---------------EAKRNVE---RQLS-------TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE- 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1245 hgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK----VQSGSESIIQEYVDLRTRYS----ELSTLTSQ 1316
Cdd:pfam01576 563 --EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqMLAEEKAISARYAEERDRAEaearEKETRALS 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1317 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglqrRMQEEVARREEVAVEAQ 1396
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE--------EMKTQLEELEDELQATE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1397 EQKRSIQEELQHLRQSSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEA 1469
Cdd:pfam01576 713 DAKLRLEVNMQALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1470 EAQKRQAQEEAERLRRQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERA 1544
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERD 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1545 R-QVQVALETAQRSAeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQqaeaeraraeaerelerwqlkaN 1623
Cdd:pfam01576 865 ElADEIASGASGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQ----------------------V 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1624 EALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAeqELIRLR 1703
Cdd:pfam01576 920 EQLTTELAAERSTSQKS------------------------ESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALE 973
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1704 AETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAGRFREL 1783
Cdd:pfam01576 974 AKIAQ-------LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVE----DERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
970 980
....*....|....*....|..
gi 1920237974 1784 AEEAArlRALAEEAKRQRQLAE 1805
Cdd:pfam01576 1043 EEEAS--RANAARRKLQRELDD 1062
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1335-1588 |
2.16e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1335 AEQQRAEERERlaeVEAALEkqrqlaEAHAQAKAQAEREAQGL---------------------QRRMQEEVARREEVAV 1393
Cdd:PHA03247 1586 AKQQRAEATDR---VTAALR------EALAAHERRAQSEAESLanlktllrvaaipataaktldQARSVAEIVDQIELLL 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1394 EAQEQKRSIQEE----LQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvVRLQLEATERQRggaegeLQALRARAEEA 1469
Cdd:PHA03247 1657 EQTEKAAELDVAavdwLEHARRVFEAHPLTAARGGGPDPLARLH-------ARLDALGETRRR------TEALRRSLEAA 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1470 EAQKRQAQEEAERLRRQvqdetqrkrqaeaelALRVQAEAEAAREKQRALQALEE--LRLQAEEAERRLrqaeAERARQV 1547
Cdd:PHA03247 1724 EAEWDEVWGRFGRVRGG---------------AWKSPEALRAAREQLRALQTATNtvLGLRADAHYERL----PAKYQGA 1784
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237974 1548 qVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVAVV 1588
Cdd:PHA03247 1785 -LGAKSAERAGAVE---ELGAAVARHDGLLARLREEVVARV 1821
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2020-2455 |
2.17e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 44.19 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2020 LQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAE 2099
Cdd:COG4995 1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2100 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQL 2179
Cdd:COG4995 81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2180 EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQ 2259
Cdd:COG4995 161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2260 VAEEAARLSvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2339
Cdd:COG4995 241 LALAAAAAA-LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2340 QLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEM-SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2418
Cdd:COG4995 320 LAALLLLLAALALLALLLLLAAAALLAAALAAALALAaALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAA 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 1920237974 2419 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2455
Cdd:COG4995 400 LLALAAAQLLRLLLAALALLLALAAYAAARLALLALI 436
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1459-1583 |
2.27e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1459 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEaarekqralQALEELRLQAEEAERRLRQ 1538
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ---------QAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237974 1539 AEAERARQVqvaletaqrsAEAELQSEHASFAEKTAQLERTLKEE 1583
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1698-2045 |
2.29e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1698 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA 1777
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1778 GRFRELAEEAARLRAlAEEAKRQRQLAEEDAVrqRAEAERVLaeklaaiseatrlkteaeialkEKEAENERLRRLAEDE 1857
Cdd:pfam07888 108 ASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------------ERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1858 AFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG 1937
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1938 TAE-------------------DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE----- 1993
Cdd:pfam07888 242 LQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrie 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1994 ----EVERLKAKVEEARRLRERAEQESARQ--LQLAQEAAQKRLQAEEKAhAFAVQQK 2045
Cdd:pfam07888 322 klsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1353-1559 |
2.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1353 LEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAaersrl 1432
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREEL-QREEERLVQKEEQLDA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1433 RIEEeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELALRVQAEAEaa 1512
Cdd:PRK12705 96 RAEK--------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237974 1513 REKQRALQALEelrlqaEEAerrlrQAEAERARQVQVAlETAQRSAE 1559
Cdd:PRK12705 157 EEKAQRVKKIE------EEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1347-1554 |
2.38e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1347 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ--RRMQEEVARREEVAVEAQEQKRSIQE-----------ELQHLRQSS 1413
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1414 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLEATERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1480
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1481 ERLRRQVQDETQRKRQAEAELAL-RVQAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEAERARQVQVALETA 1554
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALAaTHGYNPRDFRKRAEQALAANAKTATLALEAA 1381
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1444-1559 |
2.39e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1444 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAL 1522
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237974 1523 EELR---------LQAEEAERRLRQAE-AERARQVQVALetAQRSAE 1559
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKiADLGRRLNVAL--AQRVQE 191
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
39-147 |
2.52e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.13 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 39 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 109
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237974 110 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1323-1595 |
2.64e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.94 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAQGLQRRMQEevARREEVAVEAQEQKRSI 1402
Cdd:pfam03528 96 DEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQ-WNQYRESAEREIADLRRRLSE--GQEEENLEDEMKKAQED 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1403 QEELQHLRQSSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALraraeeaEAQKRQAQEEAE 1481
Cdd:pfam03528 173 AEKLRSVVMPMEKEIAAlKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVL-------NTQKSVLQEDAE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1482 RLRRQVQDETQRkrqaeaeLALRVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVqvalETAQRSAEA 1560
Cdd:pfam03528 246 KLRKELHEVCHL-------LEQERQQHNQLKHTWQKANdQFLESQRLLMRDMQRMESVLTSEQLRQV----EEIKKKDQE 314
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237974 1561 ELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAT 1595
Cdd:pfam03528 315 EHKRARTHKEKETLKSDREHTVSIHAVFSPAGVET 349
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1665-1809 |
2.66e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1665 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1744
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1745 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV 1809
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAI 356
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2141-2305 |
2.66e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2141 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2220
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2221 mEELGKLKARIEAENRALVLRDkDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2300
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 1920237974 2301 QAVQE 2305
Cdd:COG1579 167 ELAAK 171
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1377-2042 |
2.70e-03 |
|
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: 43.97 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1377 LQRRMQeevARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL---RIEEEIRVVR-LQLEATERQR 1452
Cdd:pfam07111 21 LERRLD---TQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQelrRLEEEVRLLReTSLQQKMRLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1453 GGA-EGELQALRARAEEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKqralqALEELRLQAE 1530
Cdd:pfam07111 98 AQAmELDALAVAEKAGQAEAEGlRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-----ALSSLTSKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1531 EAERRLRQAEAERARQVQvALETAQRsaEAELQSEHASFAEKTAQLERTLKEEHVAVV--QLREEATRRAQQQAEAERAR 1608
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAK-QLAEAQK--EAELLRKQLSKTQEELEAQVTLVESLRKYVgeQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1609 AEAERELERWQLKAN-EALRLRLQaeevaqqkSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1687
Cdd:pfam07111 250 TMQHLQEDRADLQATvELLQVRVQ--------SLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1688 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQReaaAATQKRRELEAELAKVRA-EMEVLLASKARAEEESRSTS 1766
Cdd:pfam07111 322 LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQR---ALQDKAAEVEVERMSAKGlQMELSRAQEARRRQQQQTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1767 EKSKQRLEAEAGRFRELAEEAARLRaLAEEAKRQRQLAEE--DAVRQRAEAERVLAEKLAAIS---EATRLKTEAEIALK 1841
Cdd:pfam07111 399 AEEQLKFVVNAMSSTQIWLETTMTR-VEQAVARIPSLSNRlsYAVRKVHTIKGLMARKVALAQlrqESCPPPPPAPPVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1842 EKEAENERLRRlaedeafQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKA 1921
Cdd:pfam07111 478 DLSLELEQLRE-------ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1922 AAGKAELELELGRIRGTAEDTLRSKEQAEQEA-----ARQRQLAAEEERRRREAEERVQK---SLAAEEEAARQRKAALE 1993
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEIYGQALQEKvaeveTRLREQLSDTKRRLNEARREQAKavvSLRQIQHRATQEKERNQ 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1994 EVERLK--AKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEKAHAFAV 2042
Cdd:pfam07111 631 ELRRLQdeARKEEGQRLARRVQElERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
506-600 |
2.74e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 506 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQL---SPATRGAYRDCLGRLD 582
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1920237974 583 LQYAKLLSSSKARLRSLE 600
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
50-140 |
2.80e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.36 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 50 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 122
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1920237974 123 DDIADGNPKLTLGLIWTI 140
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2260-2503 |
2.98e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2260 VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--KEKMQAVQEATRLKAEAELLQQQKELAQEQAR--------- 2328
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlaKEEDLKRQNAVLQEAQVELDALQNQLALARAEmenikavat 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2329 ----RLQEDKEQMAQQLAQETQGFQKTL-ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfrkqaedigerlyR 2403
Cdd:pfam03528 86 vsenTKQEAIDEVKSQWQEEVASLQAIMkETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRR-------------R 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2404 TELATQEkvmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA--------- 2474
Cdd:pfam03528 153 LSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAekscrtdle 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237974 2475 -------LQQSFLSEKDSLLQRE-----RCIEQEKAKLEQL 2503
Cdd:pfam03528 228 myvavlnTQKSVLQEDAEKLRKElhevcHLLEQERQQHNQL 268
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1407-1896 |
2.99e-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: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1407 QHLRQSSEAEIQAKARqVEAAERSRLRIEEEIRVVRLQLEATERQRGGA--EGELQALRARAEEAEAQKRQAQEEAERLR 1484
Cdd:COG3064 2 QEALEEKAAEAAAQER-LEQAEAEKRAAAEAEQKAKEEAEEERLAELEAkrQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1485 RQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEELRLQAEEaerrlRQAEAERARQVQVALETAQRSAEAELQS 1564
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKA-KAAKEAEAAAAAEKAAAAAEKEKAEEAK-----RKAEEEAKRKAEEERKAAEAEAAAKAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1565 EHASFAEKTAQLERTLKEEhVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1644
Cdd:COG3064 155 EAARAAAAAAAAAAAAAAR-AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1645 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1724
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1725 REAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1804
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1805 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRK 1884
Cdd:COG3064 394 AAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDG 473
|
490
....*....|..
gi 1920237974 1885 ASESELERQKGL 1896
Cdd:COG3064 474 GAVLADLLLLGG 485
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1332-1593 |
3.05e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1332 ERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAkaqaereaqgLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRq 1411
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEHASSLASSGLKKDSKLK- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1412 SSEAEIQA-------------KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK----- 1473
Cdd:pfam10174 521 SLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1474 ----------RQAQEEAERLR--RQVQDETQRKRQAEAELALRVQ-AEAEAAREKQRA--LQALEELRLQAEEAERRLRQ 1538
Cdd:pfam10174 601 kiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSS 680
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1539 AE--------------AERARQVQVALETAQRSAEAELQSEHASFA--EKTAQLERTLKEEhvaVVQLREE 1593
Cdd:pfam10174 681 TQqslaekdghltnlrAERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE---VMALKRE 748
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1410-1563 |
3.37e-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: 43.18 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1410 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1487
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1488 QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1563
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2266-2384 |
3.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2266 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2342
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 2343 ------QETQGFQKTLETERQRQLEMSAEAERLR-------LRVAEMSRAQARAE 2384
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKEI 158
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3744-3775 |
3.57e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.57e-03
10 20 30
....*....|....*....|....*....|..
gi 1920237974 3744 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLI 3775
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1050-1266 |
3.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1050 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPV 1129
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1130 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDvrqrELEQLGRQLRYYResadpLGAWLRD 1209
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----AAEDLARLELRAL-----LEERFAA 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1210 AKQRqeqiqavplANSQAVREQLRQE-KALLEDIERHGEKVEEC-QRFAKQYINAIKDY 1266
Cdd:COG4913 758 ALGD---------AVERELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1679-1952 |
3.58e-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: 43.31 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1679 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASK 1755
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1756 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAVRQRAEA 1815
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1816 ErvLAEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRLLE--EQAAQHKADIEARLAQLRKASES 1888
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1889 ELERQKGLVEDTLRQRrqVEEeilalkgsFEKAaagKAELELELGRIRgtaedtlrsKEQAEQE 1952
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTL---------QEIAELE 278
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1169-1442 |
3.62e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1169 LERWQAVLAQTDVRQRELEQLGRQLryyrESADplgawlRDAKQRQEQIQAVPLANSQAVREQLrqEKALLEDIERhgeK 1248
Cdd:PRK11281 65 LEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES---R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1249 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSelSTLTSQyiRFISETLR-R 1327
Cdd:PRK11281 130 LAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPSQRvL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1328 MEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAEREAQGLQRRM-QEEVARREEVAVEAQEQKRS-- 1401
Cdd:PRK11281 197 LQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQEAInSKRLTLSEKTVQEAQSQDEAar 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1402 ------IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1442
Cdd:PRK11281 274 iqanplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2713-2746 |
3.64e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.64e-03
10 20 30
....*....|....*....|....*....|....
gi 1920237974 2713 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPE 2746
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2246-2379 |
3.67e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2246 AQRLLQE-----EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELL 2316
Cdd:PTZ00491 672 AELLEQEargrlERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRI 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 2317 QQQKELAQEQARRLQEdkeqmaqqLAQETQgfQKTLETERQRQLeMSAEAERL--------RLRVAEMSRA 2379
Cdd:PTZ00491 749 EAEAELEKLRKRQELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFerivealgRETLIAIARA 808
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1458-1592 |
3.70e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1458 ELQALRARAEEAEAQKRQAQEEAERLRRQVQdetqrkrqaE-AELALRVQAEAEAAREKQRaLQALEELRLQAEEAERRL 1536
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLE---------ElEAAALQPGEEEELEEERRR-LSNAEKLREALQEALEAL 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1537 RQAEAerarQVQVALETAQRSAEaELQSEHASFAEKTAQLERtlkeehvAVVQLRE 1592
Cdd:COG0497 236 SGGEG----GALDLLGQALRALE-RLAEYDPSLAELAERLES-------ALIELEE 279
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2258-2599 |
3.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2258 KQVAEEAARLSVAA--QEAARLRQLAEEDLAQQRALAEKmlkekmqavqEATRLKAEAELLQQQKELAQEQARR--LQED 2333
Cdd:PRK04863 260 KHLITESTNYVAADymRHANERRVHLEEALELRRELYTS----------RRQLAAEQYRLVEMARELAELNEAEsdLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2334 KEQMA--QQLAQETQGFQKTLE------TERQRQLEMSAEAERLRLRVAEMSRAQA-RAEEDARRFRKQAEDIGERL--- 2401
Cdd:PRK04863 330 YQAASdhLNLVQTALRQQEKIEryqadlEELEERLEEQNEVVEEADEQQEENEARAeAAEEEVDELKSQLADYQQALdvq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2402 YRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqLLQLksEEMQTVRQEQLLQETQALQ--QSF 2479
Cdd:PRK04863 410 QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE--LLSL--EQKLSVAQAAHSQFEQAYQlvRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2480 LSEKDsllqRERCIEQEKAKLEQL--FQDEVAKAQALReeqqrqqqqmqqekqqlaASMEEARRRQHEAEEGVRRQQEEL 2557
Cdd:PRK04863 486 AGEVS----RSEAWDVARELLRRLreQRHLAEQLQQLR------------------MRLSELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237974 2558 QRLAQQQQQQEkLLAEENQRLRERLQHLEEERRAALARSEEI 2599
Cdd:PRK04863 544 KRLGKNLDDED-ELEQLQEELEARLESLSESVSEARERRMAL 584
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1795-2044 |
3.91e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1795 EEAKRQRQLAEEDAVRQRAEAERVLAEKLAA-ISEATRLKTEAEIALKEKEAENerlrrlaedeafqrrlLEEQAAQHKA 1873
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGAeISKLEEENREKEKALPKNDDMT----------------IEEAKRRAAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1874 DIEARLAQLRKASESELERQkglvedtlrqrrqVEEEILALKGSFEKAAAGKAElELELGRIRGTAEDTLRSKEQAEQEA 1953
Cdd:PRK07735 66 AAKAKAAALAKQKREGTEEV-------------TEEEKAKAKAKAAAAAKAKAA-ALAKQKREGTEEVTEEEKAAAKAKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1954 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2033
Cdd:PRK07735 132 AAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAA 211
|
250
....*....|.
gi 1920237974 2034 EEKAHAFAVQQ 2044
Cdd:PRK07735 212 KAKAAALAKQK 222
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1433-1563 |
3.97e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1433 RIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAA 1512
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1513 REKQRAL-----QALEELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQ 1563
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKKD-----TLKARAKAAKAQEK 150
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2301-2598 |
3.99e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2301 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRvaemsrAQ 2380
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK------RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2381 ARAEEDARRFRKQAEDIGErlyrtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELE------------------HE 2442
Cdd:pfam02029 80 QEALERQKEFDPTIADEKE-----SVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEirekeyqenkwstevrqaEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2443 KDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2522
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2523 QQMQQEKQQLAA--SMEEARRRQHEAEEgvrrqqEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA-------AL 2593
Cdd:pfam02029 235 EREEEAEVFLEAeqKLEELRRRRQEKES------EEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRrkqeeaeRK 308
|
....*
gi 1920237974 2594 ARSEE 2598
Cdd:pfam02029 309 LREEE 313
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1359-1546 |
4.16e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.92 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1359 LAEAHAQAKAQAEREAQGLQRRMQEEVARreevaveAQEQKRSIQEELQHLRQsseaeiqakarqveaaERSRLRIEEEI 1438
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVER-------AEERLRDAREALLAFRN----------------RNGILDPEATA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1439 RVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL-RVQAEaeaarekqr 1517
Cdd:COG3524 217 EALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLaSLLAE--------- 287
|
170 180 190
....*....|....*....|....*....|.
gi 1920237974 1518 alqaLEELRLQAEEAERRLRQAEA--ERARQ 1546
Cdd:COG3524 288 ----YERLELEREFAEKAYTSALAalEQARI 314
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1425-1542 |
4.23e-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: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1425 EAAerSRLRIE-----EEIRVVRLQLEATERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1499
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA 461
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237974 1500 elalRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1542
Cdd:COG0542 462 ----RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1360-1548 |
4.43e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1360 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEir 1439
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1440 vvRLQLEATERQRGGAEGELQALRARAEEAEA--QKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKQR 1517
Cdd:PRK12678 145 --AGEGGEQPATEARADAAERTEEEERDERRRrgDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRREERGRR 221
|
170 180 190
....*....|....*....|....*....|.
gi 1920237974 1518 ALQALEELRLQAEEAERRLRQAEAERARQVQ 1548
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2090-2276 |
4.43e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2090 QSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2169
Cdd:pfam15709 360 QRRLQQEQLERAEK-MREELELEQQRRFEEIRLRK--------------QRLEEERQRQEEEERKQRLQLQAAQERARQQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2170 QEltALRLQLEETDHQKsildeelQRLKAEVTEAARQRGQVEEElfslrvQMEELGKLKARIEAENRALVLRDKDSAQRL 2249
Cdd:pfam15709 425 QE--EFRRKLQELQRKK-------QQEEAERAEAEKQRQKELEM------QLAEEQKRLMEMAEEERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|..
gi 1920237974 2250 LQEEAEKMKQVAEEAARLSVA-----AQEAAR 2276
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1471-1943 |
4.43e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1471 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQR--ALQALEELRLQAEEAERRLRQAEAERARQvQ 1548
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELeaKRQAEEEAREAKAEAEQRAAELAAEAAKK-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1549 VALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA----VVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1624
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAekekAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1625 ALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRA 1704
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1705 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1784
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1785 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1864
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237974 1865 EEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1943
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2161-2594 |
4.58e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2161 ALRQKAQVEQ-ELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEaeNRALV 2239
Cdd:pfam10174 335 AKEQRAAILQtEVDALRLRLEE---KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE--NLQEQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2240 LRDKDsaqRLLQEEAEKMKQVAEEAARLSVA---AQEAARLRQLAEEDLAQQRALAEKMLKEKMQAV-QEATRLKAEAEL 2315
Cdd:pfam10174 410 LRDKD---KQLAGLKERVKSLQTDSSNTDTAlttLEEALSEKERIIERLKEQREREDRERLEELESLkKENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2316 LQQQKelaQEQARRLQEDKEQmAQQLAQ---ETQGFQKTLETERQRQLEmsaEAERLrlrVAEMSRAQaRAEEDARrfrk 2392
Cdd:pfam10174 487 LQPEL---TEKESSLIDLKEH-ASSLASsglKKDSKLKSLEIAVEQKKE---ECSKL---ENQLKKAH-NAEEAVR---- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2393 QAEDIGERLYRTELATQEKVMlvqtlETQRQQSDrdAERLREAIAELEHEK-DKLKQEAQLLQLKSEEMQTvrQEQLLQE 2471
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE-----ESGKAQAE--VERLLGILREVENEKnDKDKKIAELESLTLRQMKE--QNKKVAN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2472 TQALQQsflsekdsllqrercieQEKAKLEQLFQDevakaqALREEQQRQQQQMQQEKQQLAASMEEARRrqhEAEEGVR 2551
Cdd:pfam10174 623 IKHGQQ-----------------EMKKKGAQLLEE------ARRREDNLADNSQQLQLEELMGALEKTRQ---ELDATKA 676
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1920237974 2552 RQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2594
Cdd:pfam10174 677 RLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAIS 719
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1663-1763 |
4.66e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1663 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1742
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 1920237974 1743 KvRAEMEVLLaskarAEEESR 1763
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1705-1927 |
4.73e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1705 ETEQGEQQRQLLEEELARLQ-----------REAAAATQKRRELEAELAKVRAEMEV-----LLASKARAEEESRSTSEK 1768
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAAAAkakaaALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1769 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--AVRQRAEAERVLAEKLAAISEATRLKTEAEIAL---KEK 1843
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkaAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKakaKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1844 EAENERLRRLAEDEAFQRRLLEEQAAQH-KADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEE-ILALKGSFEKA 1921
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKAKAAAA 250
|
....*.
gi 1920237974 1922 AAGKAE 1927
Cdd:PRK07735 251 ARAKTK 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2302-2556 |
4.73e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2302 AVQEATRLKAEAELLQQQKEL--AQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2379
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2380 QARAEEDARRFRKQ------------AEDIGE---RLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKD 2444
Cdd:COG3883 85 REELGERARALYRSggsvsyldvllgSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2445 KLKQEAQLLQLKSEEmqtvrQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQ 2524
Cdd:COG3883 165 ELEAAKAELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 1920237974 2525 MQQEKQQLAASMEEARRRQHEAEEGVRRQQEE 2556
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1104-1514 |
4.76e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.75 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1104 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerLQQRHGERDVEVERWRERvtllLERWQAVLAQTDVRQ 1183
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAG-------LTRRLSAAEGELEELVAR----LAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1184 RELEQLGRQLRYYRESADplgawlRDAKQRQEQIQAVPLANsQAVREQLRQEKALLEDIERHGEKVEECQRFAKQyinai 1263
Cdd:pfam19220 107 EELRIELRDKTAQAEALE------RQLAAETEQNRALEEEN-KALREEAQAAEKALQRAEGELATARERLALLEQ----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1264 kdyelqlvtykaqlepvaspaKKPKVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRA 1340
Cdd:pfam19220 175 ---------------------ENRRLQALSEEQAAELAELTRRLAELETQldaTRARLRALEGQLAAEQAERERAEAQLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1341 EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAK 1420
Cdd:pfam19220 234 EAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLERR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1421 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaeAE 1500
Cdd:pfam19220 310 TQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER---AE 386
|
410
....*....|....
gi 1920237974 1501 LALrVQAEAEAARE 1514
Cdd:pfam19220 387 RAL-AQGALEIARE 399
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2255-2349 |
4.77e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.27 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2255 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2328
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 1920237974 2329 RLQEDKEQMAQQLAQETQGFQ 2349
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2222-2350 |
4.78e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2222 EELGKLKARIEAENRALVLRDKDSAQrlLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2301
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 2302 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAQETQGFQK 2350
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1868-2044 |
4.85e-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: 42.83 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1868 AAQHKADIEARLAQLRKasesELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKE 1947
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1948 QAEQEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2013
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 1920237974 2014 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2044
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1782-1910 |
4.86e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1782 ELAEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1860
Cdd:COG2268 196 EIIRDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 1861 RRLLEEQAAQHKADIEARLAQLRKA-SESELERQKGLVEDTLRQRRQVEEE 1910
Cdd:COG2268 276 EREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1302-1563 |
4.99e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.72 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1302 DLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQaKAQAEREAQGLQRRM 1381
Cdd:COG1538 77 EVAQAYFDLLAAQEQ-LALAEENLALAEELLELARARYEAGLASRLDVLQA---EAQLAQARAQ-LAQAEAQLAQARNAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1382 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA------EIQAKARQVEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1455
Cdd:COG1538 152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEalerrpDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1456 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1516
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1517 RALQALEEL-------RLQAEEAERRLRQAEAERarqvqVALETAQRSAEAELQ 1563
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1453-1593 |
5.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1453 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkrqaEAELALRVQAEAEAAREKQralqaleelRLQAEEa 1532
Cdd:PRK12705 19 GVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK-----ELLLRERNQQRQEARRERE---------ELQREE- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 1533 ERRLRQAEAERARQVQVALETAQRS-AEAELQSEHASFAEKTAQLERTLKEehvaVVQLREE 1593
Cdd:PRK12705 84 ERLVQKEEQLDARAEKLDNLENQLEeREKALSARELELEELEKQLDNELYR----VAGLTPE 141
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1329-1516 |
5.38e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1329 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER--------EAQGLQRRMQ-----EEVARREEVAVEA 1395
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegEIEAKEADHKgeteaEEVEHEGETEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1470
Cdd:TIGR00927 726 TEDEGEIEtgEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237974 1471 AQKRQAQEEAERlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1516
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1327-1514 |
5.40e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1327 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQglqrrmQEEVARREEVAVEAQEQKRSIQEEL 1406
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ------QEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1407 QHLRQSSEAEIQAKARQVeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1486
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 1920237974 1487 VQDETQR-KRQAEAElalrVQAEAEAARE 1514
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1455-1564 |
5.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1455 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE-ELRLQ 1528
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREeELEKK 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237974 1529 AEEAERRLRQAEAERARqvqvaLETAQRSAEAELQS 1564
Cdd:PRK12704 116 EKELEQKQQELEKKEEE-----LEELIEEQLQELER 146
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1776-1885 |
5.61e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1776 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAVRQRAEAERVLAEKLAAISEATRLKTEAEIA-LKEKEAE 1846
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237974 1847 NErlrrlAEDEAFQRRLLEEQAAQHKAD-IEARL---AQLRKA 1885
Cdd:PRK11448 210 TS-----QERKQKRKEITDQAAKRLELSeEETRIlidQQLRKA 247
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1321-1429 |
6.07e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 41.90 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1321 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEahaqakaqAEREAQGLQRRMQEEVARReevavEA 1395
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIE--------AEKDAEVAKIQMQQKIMEK-----EA 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237974 1396 QEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAER 1429
Cdd:cd03406 224 EKKISEIEDEMHLAREKAraDAEYYRALREAEANKL 259
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2159-2600 |
6.11e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2159 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRA 2237
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2238 LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQQRALAEKMLKEKMQAVQEATRLKA 2311
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2312 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQetqgFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFR 2391
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2392 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSdRDAERLREAIAELEHEKDK--LKQEAQLLQLKSE----------- 2458
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARAS-EERVRGGRAVEEVLKASIQgvHGTVAQLGSVGERyataievaagn 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2459 ---------EMQTVRQEQLLQETQALQQSFL-------SEKD-SLLQRERCI----------EQEKAKLEQLFQDEV--- 2508
Cdd:TIGR02169 548 rlnnvvvedDAVAKEAIELLKRRKAGRATFLplnkmrdERRDlSILSEDGVIgfavdlvefdPKYEPAFKYVFGDTLvve 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2509 ----------------------------------------------AKAQALREEQQRQQQQMQQEKQQLA---ASMEEA 2539
Cdd:TIGR02169 628 dieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepAELQRLRERLEGLKRELSSLQSELRrieNRLDEL 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237974 2540 RRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEenqrLRERLQHLEEERRAALARSEEIA 2600
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE----LEEDLSSLEQEIENVKSELKELE 764
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1713-2025 |
6.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1713 RQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1792
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1793 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1872
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1873 ADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 1952
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237974 1953 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2025
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1326-1733 |
6.24e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1326 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1404
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1405 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1484
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1485 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS 1564
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1565 EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1644
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1645 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1724
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 1920237974 1725 REAAAATQK 1733
Cdd:COG3064 424 LALAGAAGA 432
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
46-258 |
6.25e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 42.62 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 46 KTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQIALDYLRHRQV 115
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 116 KLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMV------EGCQGLRCDN 182
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGlkgdkeEGIRSFGDPA 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 183 FTTSWRDGRLFNAIIHrhkPTLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSIITYV 255
Cdd:COG5069 532 GSVSGVFYLDVLKGIH---SELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVLTFI 606
|
...
gi 1920237974 256 SSL 258
Cdd:COG5069 607 ESL 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1919-2401 |
6.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1919 EKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERvQKSLAAEEEAARQRKAALEEVERL 1998
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1999 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaARRAAEEAE 2078
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-----LQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2079 AARERAEREAAQSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFA 2158
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2159 EQAL---------RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAArqrgqveEELFSLRVQMEELGKLKA 2229
Cdd:COG4717 282 VLGLlallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2230 RIE-AENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmqAVQEATR 2308
Cdd:COG4717 355 EAEeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2309 LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQ-ETQGFQKTLETERQRQLEMSAEAER--LRLRVAE--MSRAQARA 2383
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEewAALKLALelLEEAREEY 509
|
490
....*....|....*....
gi 1920237974 2384 EEDAR-RFRKQAEDIGERL 2401
Cdd:COG4717 510 REERLpPVLERASEYFSRL 528
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2158-2411 |
6.48e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2158 AEQALRQKAQVEQELTALRLQLEETDHQK----------SILDEELQRLKAEVTEAARQRGQVEEELF-SLRVQMEELGK 2226
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATEGLCVHSLSkELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2227 LKARIEAEnRALVLRDKDSAQRLLQEEAEKM---KQVAEEAARLSVAAQEAARLRQLAEED------------------- 2284
Cdd:PLN02939 238 LKDDIQFL-KAELIEVAETEERVFKLEKERSlldASLRELESKFIVAQEDVSKLSPLQYDCwwekvenlqdlldratnqv 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2285 ------LAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTL---- 2352
Cdd:PLN02939 317 ekaalvLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklk 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237974 2353 ETERQRQLEMSAEA------ERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEK 2411
Cdd:PLN02939 397 EESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1104-1547 |
6.60e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1104 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQ 1183
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1184 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAI 1263
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1264 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEER 1343
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1344 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQ 1423
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1424 VEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL 1503
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1920237974 1504 RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1547
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
998-1595 |
6.65e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 998 EPARECAQRITEQQKAQAEVDGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIYlEKLKTISL 1077
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHTR-QQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1078 VIRSTQEAEEVLRAHeeQLKEAQAVPATLPELeatkaalkklrAQAEAQQPVFDALRDELRG-----AQEVGERLQQRhg 1152
Cdd:PRK10246 319 RLQSTMALRARIRHH--AAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1153 erdveveRWRERVTLLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLRDAKQRQEQIQAvplANSQA 1227
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1228 VREQLRQEKALLEDIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1280
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1281 ASPAKKPKVQSGSESIIQEYVDLRtrySELSTLTSQYIRFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1360
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1361 EAHAQ-AKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQV--EAAERSRL--RIE 1435
Cdd:PRK10246 596 DDIQPwLDAQEEHERQLRLLSQRHEL---QGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLpqEDEEASWLatRQQ 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1436 EEIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DETQRKRQAEA 1499
Cdd:PRK10246 673 EAQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1500 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLrqaeaERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1579
Cdd:PRK10246 753 QFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQI 827
|
650
....*....|....*.
gi 1920237974 1580 LKEEHVAVVQLREEAT 1595
Cdd:PRK10246 828 QQELAQLAQQLRENTT 843
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1415-1568 |
6.65e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1415 AEIQAKARQVEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElqALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1494
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA--AAATPAAPAAAARRAARAAAAARQAEQPAAEAAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237974 1495 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHAS 1568
Cdd:PRK12678 100 AKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERR 173
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3669-3707 |
6.71e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 6.71e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1920237974 3669 YLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVARQL 3707
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1690-2101 |
6.94e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1690 QQRLAAEQELIRLRAETEQGEQQRQLL---EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS 1766
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLdelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1767 EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE 1846
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1847 NERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKA 1926
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1927 ELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2006
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2007 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2086
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410
....*....|....*
gi 1920237974 2087 EAAQSRRQVEEAERL 2101
Cdd:COG5278 483 ALAEAEAAAALAAAA 497
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
43-145 |
7.09e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 39.59 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 43 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1920237974 119 NIRNDDIADGNPKLTLGLIWTIILHFQ 145
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2189-2284 |
7.16e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2189 LDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALvlrdkdsAQRLLQEEAEKMKQVAEEAARLS 2268
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL-------EAQLEQLQEKAAETSQERKQKRK 219
|
90
....*....|....*.
gi 1920237974 2269 VAAQEAARLRQLAEED 2284
Cdd:PRK11448 220 EITDQAAKRLELSEEE 235
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2219-2514 |
7.42e-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: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2219 VQMEE---LGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAE 2293
Cdd:pfam15964 341 VQMTEeanFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2294 KMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAQETQgfqKTLETERQRQLEMS-AEAERLRL 2371
Cdd:pfam15964 421 KVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH---REYRTKTGRQLEIKdQEIEKLGL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2372 RVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE----LATQEKVMLVQTL----ETQRQQSDRDAERLREAIAELE--H 2441
Cdd:pfam15964 496 ELSESKQRLEQAQQDAARAREECLKLTELLGESEhqlhLTRLEKESIQQSFsneaKAQALQAQQREQELTQKMQQMEaqH 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2442 EKD----------------KLKQEAQLLQLKSEEM-QTVRQE--QLLQETQALQQSFLSEK-------DSLLQRERCIEQ 2495
Cdd:pfam15964 576 DKTvneqyslltsqntfiaKLKEECCTLAKKLEEItQKSRSEveQLSQEKEYLQDRLEKLQkrneeleEQCVQHGRMHER 655
|
330
....*....|....*....
gi 1920237974 2496 EKAKLEQLFQDEVAKAQAL 2514
Cdd:pfam15964 656 MKQRLRQLDKHCQATAQQL 674
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1316-1510 |
7.52e-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: 41.83 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1316 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqakAQAEREAQgLQRRMQEEVARREEVAVEA 1395
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD---------EKAERDEL-RAKLYQEEQERKERQKERE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1396 QEQKRsiQEELQHLRQSSEAEIQAKARQvEAAERSRLRIEEEiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1475
Cdd:pfam13868 226 EAEKK--ARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 1920237974 1476 AQEEAERLRRQVQDETQRKRQAEAELALRVQAEAE 1510
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1162-1433 |
7.59e-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: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1162 RERVTLLLERWQAVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKAL 1238
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1239 LEDIERHGEKVEECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESIIQEYvdlrtRYSELSTLTSQYI 1318
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1319 RFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQ 1398
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237974 1399 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR 1433
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2093-2474 |
7.63e-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: 42.19 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2093 RQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAeQALRQKAQVEQEL 2172
Cdd:pfam07888 73 RQRRELES--------------------RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD-ALLAQRAAHEARI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2173 TALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLL 2250
Cdd:pfam07888 132 RELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2251 QEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ---- 2324
Cdd:pfam07888 212 QDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltlq 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2325 --EQARRLQEDKEQMaqqlAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEmsraqaraeedARRFRKQAEdigerly 2402
Cdd:pfam07888 288 laDASLALREGRARW----AQERETLQQSAEADKDRIEKLSAELQRLEERLQE-----------ERMEREKLE------- 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2403 rTELATQEKVMLVQTLETQRQQSDrdaerLREAIAELEHEKDKLKQEAQllqlksEEMQTVRQEQLLQETQA 2474
Cdd:pfam07888 346 -VELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAEKQ------ELLEYIRQLEQRLETVA 405
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1736-1857 |
7.69e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 42.61 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1736 ELEAELAKVRAEM--EVLLASKARAEEesrstseKSKQRLEAEAGRFR---ELAEEAARLRALAEEAKRQRQLAEEDAVR 1810
Cdd:pfam04147 155 EEEPERKKSKKEVmeEVIAKSKLHKYE-------RQKAKEEDEELREEldkELKDLRSLLSGSKRPKPEQAKKPEEKPDR 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 1811 QRAEAE-----RVLA-EKLAAISEatRLKTEAEIALKEKE----AENERLRRLAEDE 1857
Cdd:pfam04147 228 KKPDDDydklvRELAfDKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRMRGEE 282
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1662-1802 |
7.85e-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: 41.51 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1662 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA-- 1739
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237974 1740 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1802
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1670-1763 |
8.04e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1670 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEME 1749
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 1920237974 1750 VLLASKARAEEESR 1763
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2171-2514 |
8.59e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2171 ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELG----KLKARIEA-ENralvlrDKDS 2245
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkynDLKKQKEElEN------ELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2246 AQRLLQEEAEKMKQVAEEAAR----LSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ 2319
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKlellLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2320 -KELAQEQarrlQEDKEQMAQQLAQETQGFQKTLETERQRQlEMSAEAERLRlrvaemsraqaraeedarrfRKQAEDIG 2398
Cdd:TIGR04523 255 lNQLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN--------------------NQKEQDWN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2399 ERLyRTELATQEKVmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlkseemqtvrqEQLLQETQALQQs 2478
Cdd:TIGR04523 310 KEL-KSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ-----------RELEEKQNEIEK- 374
|
330 340 350
....*....|....*....|....*....|....*.
gi 1920237974 2479 FLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQAL 2514
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3668-3704 |
8.65e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.65e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237974 3668 RYLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVA 3704
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1323-1436 |
8.66e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.02 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1323 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVAVEAQEQKR 1400
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237974 1401 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1436
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1921-2439 |
8.69e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1921 AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 2000
Cdd:COG3899 736 PPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGEL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2001 KVEEARRLRERAEQESAR----QLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEE 2076
Cdd:COG3899 816 ALALAERLGDRRLEARALfnlgFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAAR 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2077 AEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQ 2156
Cdd:COG3899 896 LLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2157 FAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENR 2236
Cdd:COG3899 976 AAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAA 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2237 ALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlkekmqavqeatRLKAEAELL 2316
Cdd:COG3899 1056 AAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAAL---------------AALALAAAL 1120
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2317 QQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAED 2396
Cdd:COG3899 1121 AALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALL 1200
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1920237974 2397 IGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAEL 2439
Cdd:COG3899 1201 ALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2169-2599 |
8.70e-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: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2169 EQELTALRLQLEETDHQKSILDEELQRLKAEVTeAARQRGQV-EEELFSLRVQMEElgklKARIEAEnRALVLRDKDSAQ 2247
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKQHIEVLKESLT-AKEQRAAIlQTEVDALRLRLEE----KESFLNK-KTKQLQDLTEEK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2248 RLLQEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEkmLKEKMQAVQEATRLKAEAelLQQQKELAQEQA 2327
Cdd:pfam10174 376 STLAGEIRDLKDMLDVKERKINVLQK--KIENLQEQLRDKDKQLAG--LKERVKSLQTDSSNTDTA--LTTLEEALSEKE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2328 R---RLQEDKEQMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2404
Cdd:pfam10174 450 RiieRLKEQREREDRERLEE-------LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2405 ELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAelehekDKLKQEAQLLQLKSEEMQTVRqeqllqetqalqqsflSE 2482
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKkaHNAEEAVRTNPEIN------DRIRLLEQEVARYKEESGKAQ----------------AE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 2483 KDSLLQRERCIEQEK-------AKLEQLFQDEVaKAQALREEQQRQQQQMQQEKQqlAASMEEARRRQHEAEEGVRRQQ- 2554
Cdd:pfam10174 581 VERLLGILREVENEKndkdkkiAELESLTLRQM-KEQNKKVANIKHGQQEMKKKG--AQLLEEARRREDNLADNSQQLQl 657
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237974 2555 ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEE---ERRAALarsEEI 2599
Cdd:pfam10174 658 eelmGALEKTRQELDATKARLSSTQQSLAEKDGHLTNlraERRKQL---EEI 706
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1202-1402 |
9.14e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1202 PLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1280
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1281 ASPAKKPKVQSGSESIIQEYVDLRTRYSE-------LSTLTSQ-------YIRFISE----------------TLRRMEE 1330
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEhtglqliLSGEESQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1331 EERLAEQQ----------------RAEERERLAEVEAALEK-QRQLAE--------------AHAQAKAQAEREAQGLQR 1379
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 1920237974 1380 -RMQEEVARREEVAVEAQEQKRSI 1402
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1326-1421 |
9.19e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.60 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1326 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAEREAQGLqrrmqeevaRREEVAV---EAQEQ 1398
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKL---------AAEALAEaqaEAQAS 102
|
90 100
....*....|....*....|...
gi 1920237974 1399 KRSIQEELQHLRQSSEAEIQAKA 1421
Cdd:PRK07353 103 KEKARREIEQQKQAALAQLEQQV 125
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1467-1530 |
9.31e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.16 E-value: 9.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237974 1467 EEAEAQKRQAQEEAERLRrqvQDETQRKRQAE--AELALRVQAEAEAAREKQRALQALEELRLQAE 1530
Cdd:PLN02316 253 EKRRELEKLAKEEAERER---QAEEQRRREEEkaAMEADRAQAKAEVEKRREKLQNLLKKASRSAD 315
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1690-1952 |
9.41e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1690 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstseKS 1769
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1770 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQR--------------AEAERVLAEKLAaiseatRLKTE 1835
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIK------ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1836 AEIALKEKEAENERLRRLAEDEAFQrrlleEQAAQHKADIEARLAQLRKASES------ELERQKGLVEDTLRQRRQVEE 1909
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELR-----KEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237974 1910 EILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 1952
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1320-1536 |
9.67e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1320 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAqglqRRMQEEVARREEVAVEAQEQK 1399
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRL----EQQTEQAKKLEEKAQAALTKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1400 RsiqeelQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1479
Cdd:pfam04012 81 N------EELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237974 1480 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQaLEELRLQAEEAERRL 1536
Cdd:pfam04012 155 GSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1344-1515 |
9.74e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.32 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1344 ERLAEVEAALEK-QRQLAEAHAQAKAQAEREAQGLQRRMQEEV-ARREEVAVEAQEQKRSIQEELQHLRQsseaeiQAKA 1421
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQKDLeEVRAKLEPYLEELQAKLGQNVEELRQ------RLEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237974 1422 RQVEAAERSRLRIEEEIRVVRlqlEATERQRGGAEGELQALRARAEE-AEAQKRQAQEEAERLRRQVQDETQ----RKRQ 1496
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPyAEELRQKLAERLEELKESLAPYAEevqaQLSQ 154
|
170
....*....|....*....
gi 1920237974 1497 AEAELALRVQAEAEAAREK 1515
Cdd:pfam01442 155 RLQELREKLEPQAEDLREK 173
|
|
| |
