|
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 ... |
19-123 |
7.42e-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: 247.31 E-value: 7.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 256418964 99 RNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
16-134 |
2.95e-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: 240.70 E-value: 2.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 16 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 95
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 256418964 96 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 134
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
15-132 |
9.49e-72 |
|
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: 236.80 E-value: 9.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 15 KDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 94
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 256418964 95 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 132
Cdd:cd21236 91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
136-241 |
9.61e-72 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 235.69 E-value: 9.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 136 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 256418964 216 PEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
137-241 |
1.08e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 256418964 217 EDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
16-133 |
7.54e-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: 211.04 E-value: 7.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 16 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 95
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 256418964 96 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 133
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
137-241 |
9.52e-58 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.59 E-value: 9.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 256418964 217 EDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
135-241 |
5.11e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 176.77 E-value: 5.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 135 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 214
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 256418964 215 DPEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
21-124 |
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 256418964 21 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 99
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 256418964 100 NDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
11-120 |
1.37e-48 |
|
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: 169.86 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 89
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLK 85
|
90 100 110
....*....|....*....|....*....|.
gi 256418964 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21246 86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
137-237 |
2.45e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 256418964 217 EDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
11-120 |
2.96e-45 |
|
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: 160.54 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLr 89
Cdd:cd21193 6 IRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL- 84
|
90 100 110
....*....|....*....|....*....|.
gi 256418964 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21193 85 KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
20-348 |
3.63e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.90 E-value: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 20 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGRLFNAII 175
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 176 HRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 242
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 243 VPGAQDGVRANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE--LPAKEAD-KNRSKV 319
Cdd:COG5069 245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
|
330 340
....*....|....*....|....*....
gi 256418964 320 IYQSLEgAVQAGQLKIPPGYHPLDVEKEW 348
Cdd:COG5069 323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
137-237 |
1.81e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 157.94 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 256418964 217 EDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
17-124 |
4.91e-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: 156.77 E-value: 4.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 92
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 256418964 93 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
17-124 |
2.21e-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: 155.04 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 89
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 256418964 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
124-239 |
2.97e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 149.05 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 256418964 204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
11-120 |
3.87e-41 |
|
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: 149.79 E-value: 3.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 89
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 256418964 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
136-241 |
6.87e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 147.85 E-value: 6.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 136 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 256418964 216 PEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
11-120 |
5.66e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 145.97 E-value: 5.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 89
Cdd:cd21317 21 IKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLK 100
|
90 100 110
....*....|....*....|....*....|.
gi 256418964 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21317 101 EQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
133-237 |
1.60e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 141.35 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 133 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 212
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 256418964 213 LLDPEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
21-122 |
1.88e-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: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 256418964 99 RNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
19-120 |
2.29e-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: 140.22 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 97
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 256418964 98 IRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1326-1948 |
2.64e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 158.56 E-value: 2.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1326 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAElEAQELQRRMQEevarreeaavdaqqqkRSIQEELQHLRQSs 1404
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAE-RYRELKEELKE----------------LEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1405 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1484
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1485 KRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVELQSKRASFAEKT 1564
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1565 AQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA 1644
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1645 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQHEATAA 1721
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1722 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA-----LAEEAKRQRQLAE 1796
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtlLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1797 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA 1876
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1877 SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRsnaedtmrsKEQAELEAARQR 1948
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE---------RELERLEREIEA 778
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
17-124 |
2.71e-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: 140.35 E-value: 2.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 94
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 256418964 95 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
133-237 |
2.73e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.53 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 133 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 212
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 256418964 213 LLDPEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
136-237 |
6.67e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.15 E-value: 6.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 136 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 256418964 216 PEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
16-124 |
1.80e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 135.05 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 16 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 94
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 256418964 95 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1321-2026 |
2.73e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 153.37 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1321 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSiqEELQHL 1400
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1401 RQSSEAEIQAKAQQVEAAERSRmRIEEEIRVVRLQlETTERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1480
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1481 ESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASF 1560
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1561 AEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRlqAEEVaqqkslAQADAEKQ 1640
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--AEEK------KKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1641 KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATA 1720
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1721 ATQKRQeleAELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAA 1800
Cdd:PTZ00121 1479 AEEAKK---ADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1801 RQRAEAERvlTEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE 1880
Cdd:PTZ00121 1546 KKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1881 L--------ERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDtMRSKEQAELEAARQRQLAA 1952
Cdd:PTZ00121 1620 IkaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDEKKAAEALKKEA 1698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1953 EEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2026
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1424-2024 |
3.50e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 151.63 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1424 RIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1503
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1504 REKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLre 1583
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1584 eaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1663
Cdd:COG1196 347 ---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1664 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL 1743
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1744 ASKARAEEESRST---SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEA 1820
Cdd:COG1196 498 EAEADYEGFLEGVkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1821 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQkglVEDTLRQRRQVEE 1900
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT---LAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1901 EIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRK 1980
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 256418964 1981 VALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2024
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
140-241 |
4.77e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 133.71 E-value: 4.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 140 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 256418964 219 VDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
121-237 |
2.04e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.87 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 121 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 200
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 256418964 201 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1453-2053 |
1.09e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 146.62 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1453 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQRKRqaeaelalrVKAEAEAAREKQRALQALDELRLQAEEAERRLRQ 1529
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1530 AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERW 1609
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1610 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1689
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1690 LIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1769
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1770 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLA----AISEATRLKTEAEIALKEKEAENERLRRLA 1845
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1846 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGR 1925
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1926 IRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQ 2005
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 256418964 2006 ESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDR 2053
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1655-2217 |
2.02e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.85 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1655 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK 1734
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1735 VRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKL 1814
Cdd:COG1196 300 LEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1815 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLvEDTLRQ 1894
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1895 RRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEE 1974
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1975 AARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRL 2054
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2055 RSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ 2134
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2135 KQAADAEMEKHKKFAE-QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQME 2213
Cdd:COG1196 698 ALLAEEEEERELAEAEeERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
....
gi 256418964 2214 ELGK 2217
Cdd:COG1196 778 ALGP 781
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
20-125 |
1.85e-33 |
|
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: 127.18 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 96
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1289-1876 |
2.93e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 142.00 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1289 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-------LAEAHAQAKAQ 1360
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1361 AELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTE 1440
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1441 RQRGGAEGELQALRARAE------------------EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1502
Cdd:COG1196 373 ELAEAEEELEELAEELLEalraaaelaaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1503 AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLR 1582
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1583 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQ 1657
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1658 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRA 1737
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1738 EMEVLLASKARAEEESRSTSEKSKQRleaeagrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI 1817
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1818 SEATRLKTEAEIALKEKEAENerLRRLAEDEAFQRRR--LEEQaalhKADIEERLAQLRKA 1876
Cdd:COG1196 763 EELERELERLEREIEALGPVN--LLAIEEYEELEERYdfLSEQ----REDLEEARETLEEA 817
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
137-237 |
5.32e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.21 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 256418964 217 EDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
11-120 |
6.11e-33 |
|
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: 126.70 E-value: 6.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 89
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 256418964 90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
21-124 |
1.65e-32 |
|
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: 123.55 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 256418964 99 RNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
21-124 |
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 256418964 21 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 99
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 256418964 100 NDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1314-1935 |
6.47e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 138.74 E-value: 6.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAELEAQELQR----RMQEEVARREEAAVDAQ 1387
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedaKKAEAVKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1388 QQKRSIQE-------ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRlQLETTERQRGGAEGELQALRAR-AEE 1459
Cdd:PTZ00121 1241 EAKKAEEErnneeirKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1460 AEAQKRQAQEEAERLRRQVQdESQRKRQAEAELALRVKAEAEAAREKQRALQ--------ALDELRLQAEE---AERRLR 1528
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkeeakkKADAAKKKAEEkkkADEAKK 1398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1529 QAEAERARQVQVALETAQRSAEVELQsKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELER 1608
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1609 WQLKANEALRLRLQAEEVAQqkslaQADAEKQKEEAEREARRRGKAEEqAVRQRELAEQELEKQRQLAEGTAQQRLAAE- 1687
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKK-----KADEAKKAAEAKKKADEAKKAEE-AKKADEAKKAEEAKKADEAKKAEEKKKADEl 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1688 --QELIRLRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRlE 1765
Cdd:PTZ00121 1552 kkAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-E 1629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1766 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAA--RQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 1843
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1844 LAEDEAFQRRRLEEQAALHKADIEE--RLAQLRKASESELERQKGlvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELEL 1921
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEakKEAEEDKKKAEEAKKDEE--EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
650
....*....|....
gi 256418964 1922 ELGRIRSNAEDTMR 1935
Cdd:PTZ00121 1788 EDEKRRMEVDKKIK 1801
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
136-234 |
6.91e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 121.76 E-value: 6.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 136 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 256418964 216 PEDVDVPQPDEKSIITYVS 234
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
124-239 |
9.27e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 121.87 E-value: 9.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 124 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 256418964 204 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 239
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
140-241 |
9.82e-32 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 121.22 E-value: 9.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 140 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 256418964 219 VDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
142-237 |
1.26e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 118.22 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 142 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 220
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 256418964 221 VPQPDEKSIITYVSSLY 237
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
140-242 |
2.23e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 117.72 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 140 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 217
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 256418964 218 DVDVPQPDEKSIITYVSSLYDAMPR 242
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
136-234 |
3.05e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 117.24 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 136 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 256418964 216 PEDVDVPQPDEKSIITYVS 234
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
122-249 |
3.82e-30 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 117.49 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 122 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 201
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 256418964 202 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQDG 249
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF---SGAQKA 123
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
17-126 |
4.13e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.30 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 92
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 256418964 93 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 126
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
20-122 |
8.88e-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: 116.04 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
869-946 |
1.49e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 114.24 E-value: 1.49e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 869 LAWQSLSRDIQLIRSWSLVTFRTLKPEEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLVAEREYGSCSRHYQQLLQS 946
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1697-2544 |
3.43e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 129.88 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1697 TEQGEQQRQLLEEELARLQHEATAATqkRQELEAELAKVR------AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR 1770
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEglkpsyKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGK 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1771 FRElAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeaf 1850
Cdd:PTZ00121 1111 AEE-ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE---- 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1851 QRRRLEEqaaLHKADIEERLAQLRKASEselerqkglvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNA 1930
Cdd:PTZ00121 1186 EVRKAEE---LRKAEDARKAEAARKAEE----------ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1931 EdtMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKValEEVERLKAKVEEARRLRERAEQesarq 2010
Cdd:PTZ00121 1253 E--IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK--KKADEAKKKAEEAKKADEAKKK----- 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2011 lqlAQEAAQKRLQAEEKAhafvvqqreeelqqtlqqeqnmldrlrseaeaarraaeeaeeareqaereaaQSRKQVEEAE 2090
Cdd:PTZ00121 1324 ---AEEAKKKADAAKKKA----------------------------------------------------EEAKKAAEAA 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2091 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQL 2170
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKA 1427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2171 EETDHQksildEELQRLKAEVTEAARQRSQVEEelfsvRVQMEELGKlkaRIEAENRALILRDKDNTQRFLEE---EAEK 2247
Cdd:PTZ00121 1428 EEKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEE 1494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2248 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE 2323
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2324 DKeQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKV 2403
Cdd:PTZ00121 1575 DK-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2404 TLVQTL-------EIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ-----EQILQETQALQKSFL 2471
Cdd:PTZ00121 1647 KKAEELkkaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAEELKKAEE 1726
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2472 SEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRK 2544
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1085-1791 |
9.82e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 127.36 E-value: 9.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1085 EQLKEAQAVPATLQELEATKASLKKLRAQAEAQQpvfntLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQ 1164
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEE-----LEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1165 AVLAQTDVRQRELEQLGRQLRYYRESadplsawLQDAKRRQEQIQAvpiancqaareqlrQEKALLEEIERHGEKVEECQ 1244
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEER-------RRELEERLEELEE--------------ELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1245 kfakqyinaikdyelqlitykaqlepvaspakkpkvqsgsesviqeyvdlrtryselttltsqyikfisETLRRMEEEER 1324
Cdd:COG1196 344 ---------------------------------------------------------------------EELEEAEEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1325 LAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmQEEVARREEAAVDAQQQKRSIQEELQHLRQSS 1404
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAEL 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1405 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA--------EAQKRQAQEEAERLRR 1476
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAaarlllllEAEADYEGFLEGVKAA 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1477 QVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1554
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1555 SKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQ 1634
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1635 ADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1714
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER--LEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1715 QHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLralaEEAKRQ 1791
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEALGPVNLLAIEE-----------YEELEERYDFLSEQREDL----EEARET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1758-2441 |
1.59e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.59 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1758 EKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedaaRQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1837
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1838 NERLRRLAEDEAFQRRRLEEQAAlhkadiEERLAQLRKASESELERQkglvEDTLRQRRQVEEEIMALKVSFEKAAAGKA 1917
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYEL------LAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1918 ELELELgrirSNAEDTMRSKEQAELEAARQRQlaaeeeqrrrEAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEAR 1997
Cdd:COG1196 341 ELEEEL----EEAEEELEEAEAELAEAEEALL----------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1998 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAER 2077
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2078 EAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE--MEKHKKFAEQTLRQ 2155
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2156 KAQVEQELTTLRLqleETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2235
Cdd:COG1196 567 KAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2236 NTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2315
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2316 EQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQL----EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgek 2391
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL--- 800
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 256418964 2392 lhrtelaTQEKVTLVQTLeiqrqqsdhdaERLREAIAELEREKEKLKQEA 2441
Cdd:COG1196 801 -------SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
140-239 |
2.75e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.61 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 140 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 218
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 256418964 219 VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
124-248 |
5.53e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 111.33 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 256418964 204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQD 248
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF---SGAQK 119
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
20-122 |
4.13e-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: 108.34 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
124-239 |
9.61e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.89 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 256418964 204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1218-2006 |
1.15e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.93 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1218 AAREQLRQEKALLEEIERHGEKVEECQKFAKQYI---NAIKDYELQLITYkaqlepvaspakkpkvqsgsesviqEYVDL 1294
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSLERQAEKAERYKelkAELRELELALLVL-------------------------RLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1295 RTRYSELTTLTSQYikfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQE 1374
Cdd:TIGR02168 238 REELEELQEELKEA----EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1375 EVARREEAAVDAQQQKRSIQE------ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG 1448
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1449 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqALDELRLQAEEAERRLR 1528
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE--ELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1529 QAEAERarqvqvaletaqRSAEVELQSKRASFAEKTAQLERtLQEEHVTVAQLREEAERRAQQQAEAERAREEAerelER 1608
Cdd:TIGR02168 472 EAEQAL------------DAAERELAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGILGVLSELISVD----EG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1609 WQLKANEALRLRLQA---EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQE----------------- 1668
Cdd:TIGR02168 535 YEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgvakdlvkfdpkl 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1669 --------------------LEKQRQL-----------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1705
Cdd:TIGR02168 615 rkalsyllggvlvvddldnaLELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1706 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfRELAEEAARL 1781
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEI-EELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1782 RALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAeialKEKEAENERLRRLAEDEAFQRRRLEEQAAL 1861
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1862 HKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQ-- 1939
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQle 928
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1940 ---AELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvalEEVERLKAKVEEARRLRERAEQE 2006
Cdd:TIGR02168 929 lrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEE 994
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
11-124 |
1.60e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 107.15 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 11 ISSLKDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDY 87
Cdd:cd21247 10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 256418964 88 LRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21247 90 LKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
20-125 |
2.00e-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: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1317-2361 |
2.38e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.93 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAELEAQELQRRMQEEVARR-EEAAVDAQQQKRSIQ 1394
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIARLvGEATKEAEALKAEAE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1395 EELQhlrqssEAEIQAKAQQVEAAERSRMRIEEEIRVvrlQLETTERQrggAEgelQALRARAEEAEAQKRQAQEEAERL 1474
Cdd:NF041483 334 QALA------DARAEAEKLVAEAAEKARTVAAEDTAA---QLAKAART---AE---EVLTKASEDAKATTRAAAEEAERI 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1475 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELRLQaEEAeRRLRqAEAERARQVQVA----LETAQRSAE 1550
Cdd:NF041483 399 RREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLRAEAVAegerIRGEARREA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1551 VELQSKRASFAEKTAQLERTLQEEHVTVAQLREeaerraqqqaeaerareeaerelERWQLKANE-ALRLRLQAEEVAQQ 1629
Cdd:NF041483 472 VQQIEEAARTAEELLTKAKADADELRSTATAES-----------------------ERVRTEAIErATTLRRQAEETLER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1630 kslAQADAEKQKeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAEteqGEQQRQLLE 1708
Cdd:NF041483 529 ---TRAEAERLR----------AEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTE---AEERLTAAE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1709 EELARLQHEataATQKRQELEAELAKVRAEM-EVLLASKARAEEEsrstSEKSKQRLEAEAGRFRELAEEAA-RLRA-LA 1785
Cdd:NF041483 593 EALADARAE---AERIRREAAEETERLRTEAaERIRTLQAQAEQE----AERLRTEAAADASAARAEGENVAvRLRSeAA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1786 EEAKRQRQLAEEDAARQRAE----AERVLTEKL----AAISEATRLKTEAEIALKEKEAENERLRRLAedeafqRRRLEE 1857
Cdd:NF041483 666 AEAERLKSEAQESADRVRAEaaaaAERVGTEAAealaAAQEEAARRRREAEETLGSARAEADQERERA------REQSEE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1858 QAALHKADIEERLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEIMALKVSFEKAAA-GKAELELELGR 1925
Cdd:NF041483 740 LLASARKRVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADR 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1926 IRSnaeDTMRSKEQAELEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEE-ARRLRERA- 2003
Cdd:NF041483 820 VRS---DAYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEAs 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2004 ------EQESARQLQLAQEAAQK-RLQAEEKAHAFVVQQREEELQQTLQQEQNMlDRLRSEAEAARRAAEEAEEAREQAE 2076
Cdd:NF041483 884 dtlasaEQDAARTRADAREDANRiRSDAAAQADRLIGEATSEAERLTAEARAEA-ERLRDEARAEAERVRADAAAQAEQL 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2077 REAAQS---RKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA------------ADAE 2141
Cdd:NF041483 963 IAEATGeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKdankrrseaaeqADTL 1042
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2142 MEKHKKFAEQtLRQKAQVEQELTTLRLQlEETDHQKSILDEELQRLKAEVT-----EAARQRSQVEEELFSVRVQM---- 2212
Cdd:NF041483 1043 ITEAAAEADQ-LTAKAQEEALRTTTEAE-AQADTMVGAARKEAERIVAEATvegnsLVEKARTDADELLVGARRDAtair 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2213 EELGKLKARIEAENRALilrdkdnTQRFLEEEAEKMKQVAEEAARLSVAAQEaarlrQLAEEDLAQQRALAE---KMLKE 2289
Cdd:NF041483 1121 ERAEELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE-----QLAEAEAKAKELVSDansEASKV 1188
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 2290 KMQAVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAEAERLK 2361
Cdd:NF041483 1189 RIAAVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ 1254
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-2441 |
3.04e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.55 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1459 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELRLQAE-EAERRLR 1528
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1529 QAEAERARQVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaqlreEAERRAQQQAEAERAREEAERE 1605
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE---------AESARAEAEAILRRARKDAERL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1606 LERWQLKANEALRlrlQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQRLA 1685
Cdd:NF041483 224 LNAASTQAQEATD---HAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVVAEAKEAAAKQLA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1686 AeqelirlrAETeQGEQQRQLLEEELARLQHEATA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSK 1761
Cdd:NF041483 298 S--------AES-ANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1762 QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI---------------SEATRLKTE 1826
Cdd:NF041483 369 AARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1827 AEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAALHKADIEErlaqLRKASESELERQKG-LVEDTLRQRRQVEE 1900
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE----LRSTATAESERVRTeAIERATTLRRQAEE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1901 eimALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLA------AEEE 1974
Cdd:NF041483 525 ---TLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAeealadARAE 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1975 AARQRKVALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqNMLD 2052
Cdd:NF041483 602 AERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGE-----------------------NVAV 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2053 RLRSEAEaarraaeeaeeareqaereaaqsrkqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2132
Cdd:NF041483 659 RLRSEAA---------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEAL 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 kqkQAADAEMEKHKKFAEQTL------------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2200
Cdd:NF041483 702 ---AAAQEEAARRRREAEETLgsaraeadqereRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2201 -VEEELFSVRVQM-EELGKLkaRIEAENRAlilrdkDNTQRFLEEEAEKMKqvAEEAARLSVAAQEAARLRQLAEEDLAQ 2278
Cdd:NF041483 779 qVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDANRLRREAQEETEA 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2279 QRALAEKMLKEkmqAVQEATRLKAEAELLQQQ-------------------KELAQEQARRLQEDKEQMAQQLVEETQGF 2339
Cdd:NF041483 849 AKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAQADRLIGEATSE 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2340 QRTLEAE-----RQRQLEMSAEAERLKLRMAEMS-RAQARAEEDAQRFRKQAEEIgeklhrTELATQEKVTLVQTLEIQR 2413
Cdd:NF041483 926 AERLTAEaraeaERLRDEARAEAERVRADAAAQAeQLIAEATGEAERLRAEAAET------VGSAQQHAERIRTEAERVK 999
|
1050 1060
....*....|....*....|....*....
gi 256418964 2414 QQSDHDAERLR-EAIAELEREKEKLKQEA 2441
Cdd:NF041483 1000 AEAAAEAERLRtEAREEADRTLDEARKDA 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1380-2026 |
4.43e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.48 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1380 EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE 1459
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1460 aEAQKRQAQEEAERLRRqvqdeSQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQ-AEEAERRLRQAEAERARQV 1538
Cdd:PTZ00121 1114 -ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1539 QVALETaqRSAEvelQSKRASFAEKtAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALR 1618
Cdd:PTZ00121 1188 RKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1619 L--------------RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEKQRQLAEGT 1679
Cdd:PTZ00121 1262 MahfarrqaaikaeeARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1680 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL-EAELAKVRAEMEVLLASKARAEEESRSTSE 1758
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1759 KSKQRLEA-----EAGRFRELAEEAARLRALAEEAKRQRQL---AEE----DAARQRAEAERVLTEKLAAISEATRLKTE 1826
Cdd:PTZ00121 1422 EAKKKAEEkkkadEAKKKAEEAKKADEAKKKAEEAKKAEEAkkkAEEakkaDEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1827 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA---LHKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEEEIM 1903
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEELKKAEEKKKAEE---AKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1904 ALKVSFEKAAAGKAELELELGRIRSnaEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL 1983
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1984 EEV----ERLKAKVEEARR----LRERAEQESARQLQLAQEAAQKRlQAEE 2026
Cdd:PTZ00121 1657 EENkikaAEEAKKAEEDKKkaeeAKKAEEDEKKAAEALKKEAEEAK-KAEE 1706
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
24-121 |
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 256418964 24 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 99
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 256418964 100 NDDIADGnPKLTLGLIWTIILH 121
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
124-239 |
2.57e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 104.00 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 256418964 204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
142-237 |
2.69e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.00 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 142 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 220
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 256418964 221 VPQPDEKSIITYVSSLY 237
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
136-242 |
8.33e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.59 E-value: 8.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 136 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 212
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 256418964 213 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 242
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
21-124 |
3.58e-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: 100.05 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 21 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 96
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
138-237 |
4.56e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.56 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 138 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 217
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 256418964 218 D-VDVPQPDEKSIITYVSSLY 237
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1313-2029 |
5.49e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 112.23 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1313 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAELEAQELQRRMQEEVAR-REEA 1382
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1383 AVDAQQQKRSIQEELQHLRqsSEAEiQAKAQQVEAAERSRMRIEEEIRVVRLQLE-TTERQRGGAEGELQALRARAEE-- 1459
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1460 --AEAQKRQAQEEAERLRRQVQDESQRKRqaeaelalrvkaeAEAArEKQRALQAldelrlQAEEAERRLRQAEAERARQ 1537
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLR-------------TEAA-ERIRTLQA------QAEQEAERLRTEAAADASA 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1538 VQVALEtaqrSAEVELQSKrasfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeaerelerwqlKANEAL 1617
Cdd:NF041483 649 ARAEGE----NVAVRLRSE-------------------------------------------------------AAAEAE 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1618 RLRLQAEEVAQQ-KSLAQADAEKqkeEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI---RL 1693
Cdd:NF041483 670 RLKSEAQESADRvRAEAAAAAER---VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1694 RAETEQGEQQRqLLEEELARLQHEATAATQKRQELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAEAG 1769
Cdd:NF041483 747 RVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSDAY 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1770 RFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED 1847
Cdd:NF041483 826 AERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADARE 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1848 EAFQRRrlEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAElelelgRIR 1927
Cdd:NF041483 903 DANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------RLR 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1928 SNAEDTMRSKEQAeleAARQRQLAAEEEQRrreaeervqrslaAEEEAARQRKVALEEVERL--KAKVEEARRLRERAEQ 2005
Cdd:NF041483 975 AEAAETVGSAQQH---AERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAAEQ 1038
|
730 740
....*....|....*....|....
gi 256418964 2006 ESARQLQLAQEAAQKRLQAEEKAH 2029
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1656-2494 |
6.24e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.07 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1656 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1735
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1736 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-- 1813
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELes 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1814 -LAAISEATRLKTEAEIALKEKEAENERLRRLaedeafqRRRLEEQAALHKADIEERLAQLrKASESELERQKGLVEDtl 1892
Cdd:TIGR02168 356 lEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEE-- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1893 RQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEdtmrsKEQAELEAARQRQLaaeeeqrrreaeervqrSLAAE 1972
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1973 EEAARQRKVALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA---------QKRLQAEEKAHA 2030
Cdd:TIGR02168 484 LAQLQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlggrlqavvVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2031 FVVQQREEELQQTLqqeqnmLDRLRSEAEAARRAAEEAEEAREQAEREAAqsrkqVEEAERLKQSAEEQAQAQAQAQAAA 2110
Cdd:TIGR02168 564 FLKQNELGRVTFLP------LDSIKGTEIQGNDREILKNIEGFLGVAKDL-----VKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2111 EKLRKEAEQEAARRAQAEQAALKQKQAADAEmeKHKKFAEQTLRQKaqveQELTTLRLQLEETDHQKSILDEELQRLKAE 2190
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITG--GSAKTNSSILERR----REIEELEEKIEELEEKIAELEKALAELRKE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2191 VTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALiLRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQ 2270
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2271 LAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLVEETQgfqrtleaerqr 2349
Cdd:TIGR02168 786 ELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE------------ 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2350 qlEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE 2429
Cdd:TIGR02168 849 --ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2430 LEREKEKLKQE-AKLLQLKSEEMQTVQQEqilqetqALQKSFLSEKDSLLQRERfIEQEKAKLEQL 2494
Cdd:TIGR02168 927 LELRLEGLEVRiDNLQERLSEEYSLTLEE-------AEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
137-237 |
1.13e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 98.27 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 256418964 217 EDVDVPQ-PDEKSIITYVSSLY 237
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
140-240 |
1.40e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 97.92 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 140 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 219
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 256418964 220 DVPQPDEKSIITYVSSLYDAM 240
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
137-241 |
7.98e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.01 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 256418964 217 EDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
991-1536 |
1.44e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 991 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1070
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1071 RSTQGAEEVLKTHEEQLKEAQAvpATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE 1150
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1151 RWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvpiancqAAREQLRQEKALL 1230
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1231 EEIERHGEKVEEcqkfAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyik 1310
Cdd:COG1196 470 EEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1311 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA----HAQAKAQAELEAQELQRRMQEEVARREEAAVDA 1386
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1387 QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1466
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1467 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQA-----------------EEAERRLRQ 1529
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEelleeealeelpeppdlEELERELER 771
|
....*..
gi 256418964 1530 AEAERAR 1536
Cdd:COG1196 772 LEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1326-2030 |
1.68e-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: 107.45 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1326 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQA-KAQAELEAQELQRRMQEEV-ARREEAAVDAQQQKRSIQEELQHLRQ 1402
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILnELERQLKSLERQAeKAERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1403 SSEAEIQAKAQQVEAAERSRMRIEEEIRVvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRR------ 1476
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEE--------------LQKELYALANEISRLEQQKQILRERLANLERqleele 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1477 -QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLR--QAEAERarqvqvaletaQRSAEVEL 1553
Cdd:TIGR02168 323 aQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEelEEQLET-----------LRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1554 QSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1633
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1634 QADAEKQKEeaerearrrgKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQ---------ELIRLRAETEQG--- 1700
Cdd:TIGR02168 472 EAEQALDAA----------ERELAQLQARlDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1701 --------------EQQRQ----LLEEELARL----------------QHEATAATQKRQELEAELAKVRAEMEVLLA-- 1744
Cdd:TIGR02168 542 alggrlqavvvenlNAAKKaiafLKQNELGRVtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSyl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1745 --------SKARAEEESRSTSEK-----------------SKQRLEAEAGRF---RELAEEAARLRALAEEAKRQRQlAE 1796
Cdd:TIGR02168 622 lggvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggviTGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK-AL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1797 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEErLAQLRKA 1876
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1877 SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQlaaeeeq 1956
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------- 852
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1957 rrreAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLqlaQEAAQKRLQAEEKAHA 2030
Cdd:TIGR02168 853 ----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL---RELESKRSELRRELEE 919
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
137-235 |
2.42e-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: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 256418964 216 PEDVDVPQPDEKSIITYVSS 235
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1038-1876 |
5.76e-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: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1038 LRSELELTLGKLEQVRSLSaiylEKLKTISLVIRSTQGAeeVLKTHEEQLKEAQAvpATLQELEATKASLKKLRAQAEAQ 1117
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKA----ERYKELKAELRELELA--LLVLRLEELREELE--ELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1118 QPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAW 1197
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1198 LQDAKRRQEQIQAVPIANC----------QAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQ 1267
Cdd:TIGR02168 346 LEELKEELESLEAELEELEaeleelesrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1268 LEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ 1347
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1348 RQLAEAHAQAKAQAELEAQELQRRMQE-EVARREEAAVDAQQQKR----------SIQEELQHLRQSSE------AEIQA 1410
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAALGGRlqavvvenlnAAKKAIAFLKQNELgrvtflPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1411 KAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAea 1490
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG-- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1491 eLALRVKAEAEAAREKQRalQALDELRLQAEEAERRLRQAEAE--RARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1568
Cdd:TIGR02168 660 -VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1569 RtLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERwQLKANEALRLRLQAeEVAQQKSLAQADAEKQKEEAEREA 1648
Cdd:TIGR02168 737 R-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1649 RRRGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL 1728
Cdd:TIGR02168 814 LLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1729 EAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRA 1804
Cdd:TIGR02168 893 RSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1805 EAERvLTEKLAAISEATRLkteaeiALKEKEAENERLRRLAEdeafqrrrleeqaalHKADIEERLAQLRKA 1876
Cdd:TIGR02168 973 RLKR-LENKIKELGPVNLA------AIEEYEELKERYDFLTA---------------QKEDLTEAKETLEEA 1022
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
768-834 |
7.48e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.55 E-value: 7.48e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 768 QLKPRNpaHPVRGHVPLIAVCDYKQVEVTVHKGDQCQLVGPAQPSHWKVLSGSSSEAAVPSVCFLVP 834
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
20-125 |
7.52e-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: 7.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
20-125 |
8.02e-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: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1521-2395 |
3.02e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.21 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1521 EEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVTVAQLREEAERRAQQQAeaera 1598
Cdd:TIGR02168 175 KETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1599 reeaerelerwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAE-----QELEKQR 1673
Cdd:TIGR02168 247 -----------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1674 QLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllaskaraeeES 1753
Cdd:TIGR02168 305 QILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-----------EL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1754 RSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-LAAISEATRLKTEAEIALK 1832
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1833 EKEAENERLRRLAEdEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVED--TLRQRRQVEEEIMALKVSFE 1910
Cdd:TIGR02168 451 ELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSGLSGILGVLSELI 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1911 KAAAG-KAELELELGRIRSNAedTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERL 1989
Cdd:TIGR02168 530 SVDEGyEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1990 KAKVEEARRL----------RERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAE 2059
Cdd:TIGR02168 608 VKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2060 AARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAAD 2139
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2140 AEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLK 2219
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2220 ARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR 2299
Cdd:TIGR02168 848 EELSEDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2300 LKAEAEL----LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQLEMS------------AEAERLKLR 2363
Cdd:TIGR02168 923 KLAQLELrlegLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-RRLKRLENKikelgpvnlaaiEEYEELKER 1001
|
890 900 910
....*....|....*....|....*....|..
gi 256418964 2364 MAEMSRAQaraeEDAQRFRKQAEEIGEKLHRT 2395
Cdd:TIGR02168 1002 YDFLTAQK----EDLTEAKETLEEAIEEIDRE 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1851-2440 |
8.97e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1851 QRRRLEEQAA---LHKADIEERLAQLRKASE---------SELERQKGLVEdtlRQRRQVEE-------------EIMAL 1905
Cdd:COG1196 156 ERRAIIEEAAgisKYKERKEEAERKLEATEEnlerledilGELERQLEPLE---RQAEKAERyrelkeelkeleaELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1906 KVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvaleE 1985
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR-----L 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1986 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvvQQREEELQQTLQQEQNMLDRLRSEAEAARRAA 2065
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA------EEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2066 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2145
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2146 KKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAE 2225
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2226 NRAL-----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRL 2300
Cdd:COG1196 542 AALAaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2301 KAEAELLQQQKELAQEQARRLQEDKE------QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARA 2374
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLRevtlegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 2375 EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA--------IAELEREKEKLKQE 2440
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppdLEELERELERLERE 775
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
141-238 |
1.15e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 90.10 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 141 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 219
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 256418964 220 DVPQPDEKSIITYVSSLYD 238
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1100-1902 |
1.39e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 100.90 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1100 LEATKASLKKLRAQAEAQQPvFNTLRDELRgaqevgerlqqrhgerDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ 1179
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAER-YKELKAELR----------------ELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1180 LGRQLRYYRESADPLSAWLQDAKRRQEQIQAV------PIANC----QAAREQLRQEKALLEEIERHGEKVEECQKFAKQ 1249
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKElyalanEISRLeqqkQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1250 YINAIKDYELQLITYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEE-ERLAEQ 1328
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLE--AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1329 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR------Q 1402
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1403 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAE----GELQALRARAEEAEAQKRQAQEEAERLRR-- 1476
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVtf 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1477 --------QVQDESQRKRQAEAELALRVKAEAEAAREK-QRALQALDELRLQAEEAERRLRQAEAERARQVQVALE---- 1543
Cdd:TIGR02168 576 lpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1544 ----------TAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1613
Cdd:TIGR02168 656 rpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1614 NEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1693
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1694 RAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1773
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1774 LAEEAARLRALAEEAKRQRQLAEE------DAARQRAEAERVLTEKLAAISEatRLKTEAEIALkEKEAENERLRRLAED 1847
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNLQERLSE--EYSLTLEEAE-ALENKIEDDEEEARR 972
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1848 EAFQ-RRRLEEQAALHKADIEErlaqLRKASE--SELERQKglvEDTLRQRRQVEEEI 1902
Cdd:TIGR02168 973 RLKRlENKIKELGPVNLAAIEE----YEELKEryDFLTAQK---EDLTEAKETLEEAI 1023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1831-2583 |
2.82e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1831 LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE-LERQKGLVEDTlrqrrqveeeimalkvsf 1909
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEaTEEAFGKAEEA------------------ 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1910 EKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQrqlaaeeeqrrreaeervqrslaaEEEAARQRKVALEEVERl 1989
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK------------------------AEEARKAEDAKRVEIAR- 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1990 kaKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAFVVQQREEElqqtlqqeqnmldRLRSEAEAARRAAEEAE 2069
Cdd:PTZ00121 1159 --KAEDARKAEEARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAA-------------RKAEEERKAEEARKAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2070 EAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ--KQAADAEMEKHKK 2147
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKK 1302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2148 FAEQtLRQKAQVEQELTTLRLQLEETDHQKSILDE--ELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAE 2225
Cdd:PTZ00121 1303 KADE-AKKKAEEAKKADEAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2226 NraliLRDKDNTQRfleeEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAE 2305
Cdd:PTZ00121 1382 A----AKKKAEEKK----KADEAKKKAEEDKKKADELKKAAAAKKKADE------------AKKKAEEKKKADEAKKKAE 1441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2306 LLQQQKELAQ--EQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRK 2383
Cdd:PTZ00121 1442 EAKKADEAKKkaEEAKKAEEAKKK-AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKADEAKK 1517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2384 QAE-EIGEKLHRTELATQEKvtlvqtlEIQRQQSDHDAERLREAiAELEREKEKLKQEAKllqlKSEEMQTVQQEQILQE 2462
Cdd:PTZ00121 1518 AEEaKKADEAKKAEEAKKAD-------EAKKAEEKKKADELKKA-EELKKAEEKKKAEEA----KKAEEDKNMALRKAEE 1585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2463 TQALQKSFLSEKDSLLQrerfiEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMAsmEEARR----RQREAE 2538
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYE-----EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA--EEKKKaeelKKAEEE 1658
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 256418964 2539 EGVRRKQEELQHLEQQRQQQEKLLAEENQRLR-ERLQRLEEEHRAA 2583
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaEALKKEAEEAKKA 1704
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
137-236 |
4.42e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 88.31 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 256418964 217 ED-VDVPQPDEKSIITYVSSL 236
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
137-237 |
1.43e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 86.63 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 256418964 217 EDVDV--PQPDEKSIITYVSSLY 237
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1501-2441 |
1.55e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 97.43 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1501 EAAREKQRALQALDELRLQAEEAERRL----RQAE-AERARQVQVALETAQRSAEV-ELQSKRASFAEKTAQLERTLQEE 1574
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLksleRQAEkAERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1575 HVTVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgka 1654
Cdd:TIGR02168 256 EELTAELQELEEK------------------LEELRLEVSELEEEIEELQKELYALANEISRLEQQK------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1655 EEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK 1734
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEE-LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1735 VRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAErvLTEKL 1814
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE--LERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1815 AAISEATRLKTEAEIALKEKEAENERLR-RLAEDEAFQRRRLEEQAALHKAdieerlaqlrKASESELERQKGLVEDTLR 1893
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQaRLDSLERLQENLEGFSEGVKAL----------LKNQSGLSGILGVLSELIS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1894 qrrqVEEEimalkvsFEKAaagkaeLELELGRIRSNAedTMRSKEQAELEAARQRQlaaeeeqrrreaeervqrslaaee 1973
Cdd:TIGR02168 531 ----VDEG-------YEAA------IEAALGGRLQAV--VVENLNAAKKAIAFLKQ------------------------ 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1974 eaARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEK---AHAFVVQQREEELQQTLQQEQNM 2050
Cdd:TIGR02168 568 --NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNALELAKKLRPGY 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2051 ldRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQA 2130
Cdd:TIGR02168 646 --RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2131 ALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRv 2210
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR- 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2211 qmEELGKLKARIEAENRAL--ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2288
Cdd:TIGR02168 803 --EALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2289 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRtLEAERQRQLEMSAEAERLKLRMAEms 2368
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAE-- 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2369 RAQARAEEDAQRFRKQAEEIGEKLHR----TELATQEKVTLVQTLE-IQRQQSDHDA--ERLREAIAELEREKEKLKQEA 2441
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYDfLTAQKEDLTEakETLEEAIEEIDREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1413-2229 |
2.41e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 97.05 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1413 QQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1481
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1482 SQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEveLQSKRASFA 1561
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE--LESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1562 EKTAQLERTLQEEHVTVAQLREEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQK 1641
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAE---------------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1642 EEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1721
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1722 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA---- 1795
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvve 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1796 EEDAARQRAEAERVLTEKLAAISEATRLKteaeialkEKEAENERLRRLAEDEAFQR--RRLEEQAALHKADIEERLAQL 1873
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGRVTFLPLDSIK--------GTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLGGV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1874 RKASEselerqkglVEDTLRQRRQVEEEIM-------------ALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQA 1940
Cdd:TIGR02168 626 LVVDD---------LDNALELAKKLRPGYRivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1941 ELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQK 2020
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2021 RLQAEEKAHAfvVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKqsaeeqa 2100
Cdd:TIGR02168 777 LAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI------- 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2101 QAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIL 2180
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 256418964 2181 DEELQRLKAEVteaARQRSQVEEElfsVRVQMEELGKLKARIEAENRAL 2229
Cdd:TIGR02168 928 ELRLEGLEVRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1448-2342 |
3.06e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 96.58 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1448 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERR 1526
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1527 LRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvtvaqlreeaeRRAQQQAEAERAREEAEREL 1606
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL-----------AKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1607 ERWQLKANEALRLRLQAEEVAQQKSLAQAdaEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1686
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1687 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA 1766
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1767 EagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAE 1846
Cdd:pfam02463 470 S---EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1847 DEAFQRRRLEEQAALHKADIEERLAQLRKASESeLERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRI 1926
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1927 RSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQE 2006
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2007 SARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQV 2086
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2087 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2166
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2167 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAE 2246
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2247 KMKQVAEEAarlsvaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2326
Cdd:pfam02463 946 DEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
890
....*....|....*.
gi 256418964 2327 QMAQQLVEETQGFQRT 2342
Cdd:pfam02463 1014 ETCQRLKEFLELFVSI 1029
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
133-238 |
3.33e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 85.77 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 133 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 212
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 256418964 213 LLDPEDV-DVPQPDEKSIITYVSSLYD 238
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
140-236 |
3.74e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.45 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 140 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 215
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 256418964 216 PEDVDVPQPDEKSIITYVSSL 236
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1289-1873 |
4.76e-19 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 95.75 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1289 QEYVDLRTRYSELTTLTSQY-IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEL 1363
Cdd:COG4913 262 ERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1364 EAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1443
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1444 GGAEGELQALRARA---EEAEAQKRQAQEEAERLRR----------QVQDESQRKRQAeAELALR-------VKAEAEAA 1503
Cdd:COG4913 422 RELEAEIASLERRKsniPARLLALRDALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLGgfaltllVPPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1504 rekqrALQALDEL----RLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEVELQsKRASFA--EKTAQLERTl 1571
Cdd:COG4913 501 -----ALRWVNRLhlrgRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELG-RRFDYVcvDSPEELRRH- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1572 qEEHVTVAQLREEAERRAQQQAEAERAreeaerelERWQL-KANEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearr 1650
Cdd:COG4913 574 -PRAITRAGQVKGNGTRHEKDDRRRIR--------SRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL-------- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1651 rgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEATAATQKRQE 1727
Cdd:COG4913 637 --EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1728 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1807
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1808 RVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED------EAFQRRRLEE--------QAALHKA--DIEERLA 1871
Cdd:COG4913 791 RAMRA---FNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeERFKELLNENsiefvadlLSKLRRAirEIKERID 867
|
..
gi 256418964 1872 QL 1873
Cdd:COG4913 868 PL 869
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
22-122 |
1.57e-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: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 22 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 97
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 256418964 98 IRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1307-1903 |
1.62e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.95 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1307 QYIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAELEAQELQRRMQEEV 1376
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1377 ARREEaavdaqqqkrsIQEELQHLRQSSE---AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAL 1453
Cdd:PRK02224 286 ERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1454 RARAEEaeaqkrqAQEEAERLrrqvqdesqrkrqaEAELalrvkAEAEAAREKQRAlqALDELRLQAEEAERRLRQAEae 1533
Cdd:PRK02224 355 EERAEE-------LREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAP-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1534 rarqvqVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELE--RWQL 1611
Cdd:PRK02224 405 ------VDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEedRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1612 KANEALRLRLQAEEVAQQKSLAQADAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQ 1688
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1689 ELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEA 1768
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1769 GRFRELAEEAARLRALAEEAKRQRqLAEEDAARQRAEaervltEKLAAISEATRLKTEAEIALKEK----EAENERLRRL 1844
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEAR-IEEAREDKERAE------EYLEQVEEKLDELREERDDLQAEigavENELEELEEL 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1845 aedeafqRRRLEEQAALHkadieERLAQLRKASEsELERQKGLVEDTLRQRRQVEEEIM 1903
Cdd:PRK02224 697 -------RERREALENRV-----EALEALYDEAE-ELESMYGDLRAELRQRNVETLERM 742
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1665-2585 |
1.95e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 94.12 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1665 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQHEA-TAATQKRQELEAELAKVRAEMEV 1741
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1742 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLtekLAAISE 1819
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1820 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR----LEEQAALHKADIEERLAQLRKASESELE-------RQKGLV 1888
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRqaaeLSRAAEQRMQEAEEALREARAEAEKVVAeakeaaaKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1889 EDTLRQR-RQVEEEIMALKVSFEK-AAAGKAELELELG-------RIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRR 1959
Cdd:NF041483 300 ESANEQRtRTAKEEIARLVGEATKeAEALKAEAEQALAdaraeaeKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1960 EAEERVQRSLAAEEEAARQRKVALEEVERLKAKV--------------------------EEARRLRERAEQ-------- 2005
Cdd:NF041483 380 ASEDAKATTRAAAEEAERIRREAEAEADRLRGEAadqaeqlkgaakddtkeyraktvelqEEARRLRGEAEQlraeavae 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2006 ------ESARQ-LQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRL----RSEAEAARRAAEEAEEAREQ 2074
Cdd:NF041483 460 gerirgEARREaVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERAttlrRQAEETLERTRAEAERLRAE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2075 AEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlkqkqAADAEMEK-HKKFAEQTL 2153
Cdd:NF041483 540 AEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA-----DARAEAERiRREAAEETE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2154 RQKAQVEQELTTLRLQLEetdhqksildEELQRLKaevTEAARQRSQVEEELFSVRVqmeelgKLKARIEAENRALILRD 2233
Cdd:NF041483 615 RLRTEAAERIRTLQAQAE----------QEAERLR---TEAAADASAARAEGENVAV------RLRSEAAAEAERLKSEA 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2234 KDNTQRFLEEEAEKMKQVAEEAAR-LSVAAQEAARLRQLAEEDLAQQRALAEkmlKEKMQAVQEATRLKAEAellQQQKE 2312
Cdd:NF041483 676 QESADRVRAEAAAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA---RKRVE 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2313 LAQEQARRLQEDKEQMAQQLV---EETQGFQRTLEAERQRQlemsAEAERLKLRMAemsraqarAEEDAQRFRKQAEEIG 2389
Cdd:NF041483 750 EAQAEAQRLVEEADRRATELVsaaEQTAQQVRDSVAGLQEQ----AEEEIAGLRSA--------AEHAAERTRTEAQEEA 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2390 EKLHRTELATQEKVTLVQTLEIQRQQSDHDAER------LREAIAELEREKEKLKQEAKLLQLK-SEEMQTVQQEQILQE 2462
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAKalaertVSEAIAEAERLRSDASEYAQRVRTEaSDTLASAEQDAARTR 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2463 TQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASM-----EEARRRQREA 2537
Cdd:NF041483 898 ADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLiaeatGEAERLRAEA 977
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 256418964 2538 EEGVRRKQEELQHLEQQRQQQEKLLAEENQRL----RERLQRLEEEHRAALA 2585
Cdd:NF041483 978 AETVGSAQQHAERIRTEAERVKAEAAAEAERLrteaREEADRTLDEARKDAN 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1968-2580 |
4.63e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1968 SLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQE 2047
Cdd:COG1196 204 PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2048 QNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2127
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2128 EQAALKQKQAADAEMEKhkkfAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFS 2207
Cdd:COG1196 364 EEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2208 VRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2287
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2288 KEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2365
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2366 EMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2445
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2446 LKSEEMQTVQQEQILQETQALQKSFLSEKDS-LLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELM 2524
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAeAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2525 ASMEEARRRQREAEEGVRRkqeelqhleqqrqqqekllAEENQRLRERLQRLEEEH 2580
Cdd:COG1196 760 PDLEELERELERLEREIEAlgpv-----------nllaIEEYEELEERYDFLSEQR 804
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
23-120 |
6.06e-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: 82.00 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 23 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 98
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 256418964 99 RNDDI-ADGNPKLTLGLIWTIIL 120
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
137-236 |
8.80e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 81.82 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 256418964 217 ED-VDVPQPDEKSIITYVSSL 236
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 ... |
1306-2237 |
1.00e-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: 91.57 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1306 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD 1385
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1386 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELqalraraEEAEAQKR 1465
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE-------EELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1466 QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarEKQRALQALDELRLQAEEAERRLRQAEAERARQVQValeta 1545
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL----- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1546 qrsAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEaerelerwqLKANEALRLRLQAEE 1625
Cdd:pfam02463 377 ---AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL---------EILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1626 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1705
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1706 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL--EAEAGRFRELAEEAARLRA 1783
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLipKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1784 LAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaLHK 1863
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ--ELQ 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1864 ADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1943
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1944 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQ 2023
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2024 AEEKahaFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQ 2103
Cdd:pfam02463 840 LELK---EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2104 AQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEE 2183
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2184 LQRLKAEVTEAARQRSQVEEELF------SVRVQMEELGKLKARIEAENRALILRDKDNT 2237
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQRLkeflelFVSINKGWNKVFFYLELGGSAELRLEDPDDP 1056
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1312-1943 |
2.28e-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: 90.51 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1312 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAELEAQELQRRMqEEVARREEAAVDAQQQKR 1391
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1392 SIQEELQHLRQSSEAEIQAKAQQVEAaersrmrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1465
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1466 --------QAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQA-LDELRLQAEEAERRLRQAEAER-- 1534
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1535 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEE-----------------HVTVAQLREEAerraqqqaeaer 1597
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggraveevlkasiqgvHGTVAQLGSVG------------ 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1598 areeaerelERWQLKANEALRLRLQA-----EEVAQQ--KSLAQADAE----------KQKEEAEREARRRG-------- 1652
Cdd:TIGR02169 535 ---------ERYATAIEVAAGNRLNNvvvedDAVAKEaiELLKRRKAGratflplnkmRDERRDLSILSEDGvigfavdl 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 ----KAEEQAVR---QRELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQ 1699
Cdd:TIGR02169 606 vefdPKYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEG 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1700 GEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQRLEAEAgrfrELA 1775
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEIENVKS----ELK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1776 EEAARLRALaEEAKRQRQLAEEDAARQRAEAE--------RVLTEKLAAISEATRlktEAEIALKEKEAENERLRRLAED 1847
Cdd:TIGR02169 762 ELEARIEEL-EEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1848 EAFQRRRLEEQAALHKADIEERLAQLRKAsESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIR 1927
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
730
....*....|....*.
gi 256418964 1928 SNAEDTMRSKEQAELE 1943
Cdd:TIGR02169 917 KRLSELKAKLEALEEE 932
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1302-2026 |
2.96e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 90.03 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1302 TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREE 1381
Cdd:TIGR00618 134 DLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1382 AAVDAQQQKRSIQEELQHLR--QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaEGELQALRARAEE 1459
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ----EAVLEETQERINR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1460 AEAQKRQA--QEEAERLRRQVQDESQRKRQAEAELA-LRVKAEAEAAREKQRALQALDELRLQAEEAERRlRQAEAERAR 1536
Cdd:TIGR00618 289 ARKAAPLAahIKAVTQIEQQAQRIHTELQSKMRSRAkLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR-DAHEVATSI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1537 QVQVALETAQRSAEVELQSKRASFAEK---TAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1613
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKlqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1614 NEALRLrLQAEEVAQQKSLAQADAEKQ---------KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-------- 1676
Cdd:TIGR00618 448 TCTAQC-EKLEKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQdidnpgpl 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1677 ----EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1752
Cdd:TIGR00618 527 trrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1753 SRSTSEKS------------KQRLEAEAGRF-RELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLTEKLAAISE 1819
Cdd:TIGR00618 607 EDMLACEQhallrklqpeqdLQDVRLHLQQCsQELALKLTALHALQLTLTQERV--REHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1820 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASES--ELERQK--GLVEDTLRQR 1895
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSlkELMHQArtVLKARTEAHF 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1896 RQVEEEIMALKVSFEKAAAgKAELElelgrirsnaedtmrskEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 1975
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHL-AAEIQ-----------------FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1976 ARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2026
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
141-238 |
5.52e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.54 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 141 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 219
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 256418964 220 DVPQPDEKSIITYVSSLYD 238
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
939-1573 |
1.36e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.80 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 939 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkdpaRECAQRIAEQQK----AQAEVEGLGK 1013
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1014 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKE--- 1089
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqle 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1090 --AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQ-QRHGERDVEVERWRERVTQLLERWQAV 1166
Cdd:TIGR02168 383 tlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1167 LAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvPIANCQAAREQLRQEKALLEEIERHGEKVEEC--- 1243
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAiea 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1244 -------------QKFAKQYINAIKDYELQLITYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTL 1304
Cdd:TIGR02168 542 alggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1305 TSQYikFISETL-------RRMEEEERL--------------------AEQQRAEERERLAEVEAALEK-QRQLAEAHAQ 1356
Cdd:TIGR02168 622 LGGV--LVVDDLdnalelaKKLRPGYRIvtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEElEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1357 ----AKAQAELEAQELQRRMQEEVARREEAAVDAQQQK-RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRV 1431
Cdd:TIGR02168 700 laelRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1432 VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQ 1511
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1512 ALDELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEVELQSKRASFAEKTAQLERTLQE 1573
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1321-1798 |
1.64e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 86.75 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1321 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ-AELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1399
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1400 LRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1478
Cdd:COG4717 151 LEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1479 QDESQRKRQAEAELALRvkaeaeAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALetaqrSAEVELQSKRA 1558
Cdd:COG4717 230 EQLENELEAAALEERLK------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA-----LLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1559 SFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAE 1638
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1639 KQkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEA 1718
Cdd:COG4717 379 AG-----------VEDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1719 TAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1798
Cdd:COG4717 442 EELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1796-2582 |
3.81e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.56 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1796 EEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAlhkadIEERLAQLRK 1875
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAK-----KALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1876 ASESELERQKGLVEDTLRQRRQVEEEimalkvsfEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEE 1955
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQ--------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1956 QRRREAEERVQRSLAAEeeaaRQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvVQQ 2035
Cdd:pfam02463 290 LLAKEEEELKSELLKLE----RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE-----EEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2036 REEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERlKQSAEEQAQAQAQAQAAAEKLRK 2115
Cdd:pfam02463 361 LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ-LEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2116 EAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELqrlkaEVTEAA 2195
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG-----LKVLLA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2196 RQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAE------EAARLSVAAQEAARLR 2269
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElplgarKLRLLIPKLKLPLKSI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2270 QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2349
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2350 QLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE 2429
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2430 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA-KQLREE 2508
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEeKIKEEE 834
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 2509 QQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRA 2582
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2241-2662 |
4.81e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2241 LEEEAEKmkqvAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2319
Cdd:COG1196 205 LERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2320 RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAT 2399
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2400 QEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQ 2479
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2480 RERFIEQEKAKLEQLFQDEVA----KAKQLREEQQRQQQQMEQEKQELMA-----SMEEARRRQREAEEGVRRKQEELQH 2550
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEAllelLAELLEEAALLEAALAELLEELAEAaarllLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2551 LEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALPNGRDAPDGPSVEAEPEytfegLRQKVPAQ 2630
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA-----ALAAALAR 594
|
410 420 430
....*....|....*....|....*....|..
gi 256418964 2631 QLQEAGILSQEELQRLAQGHTTVAELTQREDV 2662
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
139-237 |
6.98e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 76.57 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 139 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 256418964 219 -VDVPQPDEKSIITYVSSLY 237
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1764-2580 |
7.26e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1764 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLTEKLAAISEATRlKTEAE 1828
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1829 IALKEKEAENERLRRLAED-EAFQRRRLEEQAALHKAdiEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMA 1904
Cdd:TIGR02168 229 LLVLRLEELREELEELQEElKEAEEELEELTAELQEL--EEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1905 LKVSFEKAAAGKAELELELgrirsnaEDTMRSKEQAELEAARQRQlaaeeeqrRREAEERVQRSLAAEEEAARqrkvalE 1984
Cdd:TIGR02168 307 LRERLANLERQLEELEAQL-------EELESKLDELAEELAELEE--------KLEELKEELESLEAELEELE------A 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1985 EVERLKAKVEEARRLRERAEQESArQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARR 2063
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVA-QLELQIASLNNEIErLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2064 AAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADaeme 2143
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG---- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2144 khkkfAEQTLRQKAQVEQElttLRLQLEETdhqksiLDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIE 2223
Cdd:TIGR02168 521 -----ILGVLSELISVDEG---YEAAIEAA------LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2224 AENRALILRDKDNTQRF---LEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEED------------------LAQQRA 2281
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVakdLVKFDPKLRKALSYLlGGVLVVDDLDNALELAKKLRpgyrivtldgdlvrpggvITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2282 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLK 2361
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2362 LRMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA 2441
Cdd:TIGR02168 747 ERIAQLSKELTELEA-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2442 KLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQ 2521
Cdd:TIGR02168 820 ANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELE 897
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 2522 ELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2580
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1207-1912 |
7.78e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.41 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1207 QIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSES 1286
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1287 VIQEYVDLRTRYSELttltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ 1366
Cdd:TIGR00618 302 VTQIEQQAQRIHTEL------------------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1367 ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVR----LQLETTERQ 1442
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkqqeLQQRYAELC 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1443 RGGAEGELQALRARAEEAE--AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQA 1520
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQesAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1521 EEAERRLRQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQlreeaerraqqqaeaerare 1600
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQ-----LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------------------- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1601 eaerelerWQLKANEALRLRLQAEEVaqQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA 1680
Cdd:TIGR00618 579 --------DNRSKEDIPNLQNITVRL--QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1681 QQ---RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLAS-KARAEEESRST 1756
Cdd:TIGR00618 649 HAlqlTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASS 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1757 SEKSK--QRLEAEA---GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeiaL 1831
Cdd:TIGR00618 729 SLGSDlaAREDALNqslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------L 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1832 KEKEAENERLRRLAEDEafqrrrLEEQAALHKADIEERLAQLRKASES--ELERQKGLVEDTLRQRRQVEEEIMALKVSF 1909
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDI------LNLQCETLVQEEEQFLSRLEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
...
gi 256418964 1910 EKA 1912
Cdd:TIGR00618 876 DKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1388-2331 |
1.10e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1388 QQKRSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEA----- 1462
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1463 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR------EKQRALQALDELRLQAEEAE-----RRLRQAE 1531
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1532 AERARQVQVALETaqrsaEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQaeaerareeaerelerwql 1611
Cdd:TIGR02169 311 AEKERELEDAEER-----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1612 kanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQEL 1690
Cdd:TIGR02169 367 ---EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1691 IRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAE 1767
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1768 AGRFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLTEKLAAiseatrlktEAEIALKEKEAENER---LRRL 1844
Cdd:TIGR02169 524 HGTVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKM 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1845 AEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQVEEEIMalkVS-----FEKAAAgkael 1919
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRM---VTlegelFEKSGA----- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1920 eLELGRIRSNAEDTMRSKEQAELEAARQRqlaaeeeqrrreaeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRL 1999
Cdd:TIGR02169 655 -MTGGSRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQE 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2000 RERAEQE----SARQLQLAQEAAQKRLQAEEkahafvVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQA 2075
Cdd:TIGR02169 711 LSDASRKigeiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2076 EREAAQSRKQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQ 2155
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2156 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENraliLRDKD 2235
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSE 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2236 NTQRfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2315
Cdd:TIGR02169 922 LKAK-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
|
970
....*....|....*.
gi 256418964 2316 EQARRLQEDKEQMAQQ 2331
Cdd:TIGR02169 1000 EERKAILERIEEYEKK 1015
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3438-3476 |
1.36e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 73.13 E-value: 1.36e-15
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3438 LLEAQVATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 3476
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
142-237 |
1.88e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.09 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 142 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 220
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 256418964 221 VPQPDEKSIITYVSSLY 237
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2307-2728 |
1.96e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2307 LQQQKELAqEQARRLQEDKEQM-AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQA 2385
Cdd:COG1196 205 LERQAEKA-ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2386 EEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2465
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2466 LQKSFLSEKDSLLQRERFIEQEKAKLEQLfqdevaKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQ 2545
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2546 EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgpsveaepeytFEGLRQ 2625
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-------------------LLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2626 KVPAQQLQEAGILSQEELQRLAQGHTTVAELTQREDVYRYLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALILLE 2705
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420
....*....|....*....|...
gi 256418964 2706 AQAASGFLLDPVRNRRLTVNEAV 2728
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAV 601
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1610-2470 |
1.99e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1610 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1685
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1686 --AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1763
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1764 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLTEKLAAISEatrlKTEAEIALKEKEAENERLRR 1843
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINELEEE----KEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1844 LAEDEAFQRRRLEEQAalhkADIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEImalkvsfEKAAAGKAELELEL 1923
Cdd:TIGR02169 463 DLSKYEQELYDLKEEY----DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1924 GRIrsnaedtmRSKEQAELEAARQRQLaaeeeqrrreaeervqRSLAAEEEAarqrkVALEEVERLKA------------ 1991
Cdd:TIGR02169 531 GSV--------GERYATAIEVAAGNRL----------------NNVVVEDDA-----VAKEAIELLKRrkagratflpln 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1992 KVEEARRLRERAEQESARQLQLAQEAAQKRLqaeEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEA 2071
Cdd:TIGR02169 582 KMRDERRDLSILSEDGVIGFAVDLVEFDPKY---EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2072 REQAEREAAQSRKQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2148
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2149 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSVRVQMEELGKLKARIEAENRA 2228
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2229 L--ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAEL 2306
Cdd:TIGR02169 817 IeqKLNRLTLEKEYLEKEIQELQEQRIDL-----KEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGD 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2307 LQQQKELAQEQARRLQEDKEQMAQQlVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2386
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2387 EIgeklhrtelatqEKVTLVQTLEIQrqqsdhDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2466
Cdd:TIGR02169 966 EI------------RALEPVNMLAIQ------EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
....
gi 256418964 2467 QKSF 2470
Cdd:TIGR02169 1028 NENF 1031
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
139-238 |
2.11e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.00 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 139 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 256418964 219 VDV--PQPDEKSIITYVSSLYD 238
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
139-242 |
3.17e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 74.70 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 139 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 256418964 219 VDV--PQPDEKSIITYVSSLYDAMPR 242
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4016-4054 |
3.27e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.27e-15
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 4016 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4054
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
19-118 |
3.67e-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: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 19 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 93
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 256418964 94 KLVNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2779-2817 |
5.07e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 5.07e-15
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 2779 LLEAQIATGGIIDPVHSHRVPVDVAYKRGYFDEEMNRIL 2817
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
16-121 |
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 256418964 16 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 85
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 256418964 86 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 121
Cdd:cd21219 72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3697-3735 |
1.28e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.28e-14
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3697 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3735
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1040-1905 |
1.75e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1040 SELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATK--ASLKKLRAQAEAQ 1117
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1118 QPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLaqtdvrQRELEQLGRQLRYYRESADPLSAW 1197
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV------KEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1198 LQDAKRRQEQIQAvpiancqaareqlrQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKK 1277
Cdd:TIGR02169 317 LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1278 PKvqsgsesviQEYVDLRTRYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqa 1357
Cdd:TIGR02169 383 TR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1358 kAQAELEAQElqRRMQEEVARREeaavDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLE 1437
Cdd:TIGR02169 446 -KALEIKKQE--WKLEQLAADLS----KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1438 TTERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDESQRKRQAEaeLALRVKA------EAEAAREKQR 1508
Cdd:TIGR02169 515 VLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIE--LLKRRKAgratflPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1509 ALQALDE-----LRLQAEEAERRLRQAEAERARQVQV--ALETAQR--------SAEVELQSKRA-----SFAEKTAQLE 1568
Cdd:TIGR02169 589 DLSILSEdgvigFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGILF 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1569 RTLQEEhvtvaqlreeaerraqqqaeaerareeaerelerwqlkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREA 1648
Cdd:TIGR02169 669 SRSEPA----------------------------------------ELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1649 RRRGKAEEQAV---RQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqhEA 1718
Cdd:TIGR02169 709 QELSDASRKIGeieKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EA 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1719 TAATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1797
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1798 DAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIE---ERLAQLR 1874
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIE 937
|
890 900 910
....*....|....*....|....*....|...
gi 256418964 1875 KASESELERQKGL--VEDTLRQRRQVEEEIMAL 1905
Cdd:TIGR02169 938 DPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1076-1574 |
1.89e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1076 AEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDvEVERWRER 1155
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAA 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1156 VTQLLErwqavLAQTDVRQRELEQLGRQLRYYREsADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIER 1235
Cdd:PTZ00121 1417 KKKADE-----AKKKAEEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1236 hgeKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESViqeyvdlrtRYSELTTLTSQYIKfiSET 1315
Cdd:PTZ00121 1491 ---KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---------KKAEEKKKADELKK--AEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1316 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1395
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQHLRQ--SSEAEIQAKAQQVEAAERsrmriEEEIRVVRLQLETTERQRGGAEgelqalrarAEEAEAQKRQAQEEAER 1473
Cdd:PTZ00121 1631 EKKKVEQlkKKEAEEKKKAEELKKAEE-----ENKIKAAEEAKKAEEDKKKAEE---------AKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1474 LRRQVQDESQRKRQAEAELAlrvKAEAEAAREKQRALQAlDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVEL 1553
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKK---KAEELKKAEEENKIKA-EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
490 500
....*....|....*....|.
gi 256418964 1554 QSKrasfaEKTAQLERTLQEE 1574
Cdd:PTZ00121 1773 IRK-----EKEAVIEEELDEE 1788
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1701-2571 |
1.92e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.79 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1701 EQQRQLLEEELARLQHEAtaatQKRQELEaELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1780
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKR----KKKEALK-KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1781 L--RALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKtEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1858
Cdd:pfam02463 227 LylDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK-ENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1859 AALHKADIEERlaqlrKASESE---LERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDT-- 1933
Cdd:pfam02463 306 ERRKVDDEEKL-----KESEKEkkkAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkk 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1934 ----MRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR 2009
Cdd:pfam02463 381 leseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2010 QLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEA 2089
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2090 ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLR---QKAQVEQELTTL 2166
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaqlDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2167 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAE 2246
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2247 KMKQVAEEAARLSVAAQEA----ARLRQLAEEDLAQQRALAEKMLKEKMQaVQEATRLKAEAELLQQQKELAQEQARRLQ 2322
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKIDEEEE-EEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2323 EDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhrtELATQEK 2402
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL----EKLAEEE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2403 VTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRER 2482
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2483 FIEQEK-AKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREaeegVRRKQEELQHLEQQRQQQEKL 2561
Cdd:pfam02463 936 EPEELLlEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY----NKDELEKERLEEEKKKLIRAI 1011
|
890
....*....|
gi 256418964 2562 LAEENQRLRE 2571
Cdd:pfam02463 1012 IEETCQRLKE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
941-1850 |
2.04e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 941 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKDPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1018
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1019 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEEVLKTHEEQLKE 1089
Cdd:TIGR02169 250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1090 AQAVPATLQ-ELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1168
Cdd:TIGR02169 320 AEERLAKLEaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1169 qtdvRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvpiancqaareqlrqekalleEIERHGEKVEECQKFAK 1248
Cdd:TIGR02169 390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1249 QYINAIKDYELQLITYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQ 1328
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1329 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQElqrRMQEEVARREEAAVDAQQQKRS-------------IQE 1395
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQHLRQSSEAEIQAKA-------QQVEAAER-------------SRMRIEEEIRVVRLQLETTERQ---RGGA-EGELQ 1451
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAvdlvefdPKYEPAFKyvfgdtlvvedieAARRLMGKYRMVTLEGELFEKSgamTGGSrAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1452 ALRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeAEAAREKQRALQALDELRLQAEEAERRlRQAE 1531
Cdd:TIGR02169 666 ILFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1532 AERARQVQVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERraqqqaeaerareeaerelERWQL 1611
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIE-NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------SRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1612 KANEALRLRlqAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAvRQRELAEQELEKQRQLAEGTAQQRlAAEQELI 1691
Cdd:TIGR02169 796 IQAELSKLE--EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEIENLNGKKE-ELEEELE 871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1692 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE--AEAG 1769
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEEL 951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1770 RFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLTEKLAaiseatRLKTEAEiALKEKEAENERLRRLA 1845
Cdd:TIGR02169 952 SLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILERIEEYEKKKREV 1019
|
....*
gi 256418964 1846 EDEAF 1850
Cdd:TIGR02169 1020 FMEAF 1024
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1076-1574 |
2.19e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1076 AEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAqaeaqqpvfnTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1155
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERERE----------ELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1156 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQ---AVPIANCQAAREQLRQEKALLEE 1232
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1233 IERHGEKVEECQKFAkqyinaikdyelqlitykaqlepvasPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfI 1312
Cdd:PRK02224 389 LEEEIEELRERFGDA--------------------------PVDLGNAEDFLEELREERDELREREAELEAT-------L 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1313 SETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAKAQAELEAQ----- 1366
Cdd:PRK02224 436 RTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEDLVEAEDRierle 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1367 ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvRLQLETTERQRGGA 1446
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESLER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1447 EGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDESQRKRQAEAELAlrvKAEAEAARE-KQRALQALdelrlqaE 1521
Cdd:PRK02224 594 IRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL-------E 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 1522 EAERRLRQAEAERARqVQVALETAQRSAE--VELQSKRASFAEKTAQLErTLQEE 1574
Cdd:PRK02224 664 QVEEKLDELREERDD-LQAEIGAVENELEelEELRERREALENRVEALE-ALYDE 716
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1080-1556 |
2.51e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.81 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1080 LKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRH---GERDVEVERWrERV 1156
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1157 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAW-LQDAKRRQEQIQavpiANCQAAREQLRQEKALLEEIER 1235
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ----QRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1236 HGEKVEEcQKFAKQYINAIKDYELQLITYKAQLEPVAspakkpkVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET 1315
Cdd:COG4717 228 ELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLG-------LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1316 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmqeevARREEAAVDAQQQKRSIQE 1395
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE-----AEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQHLRQSSEAEIQAKAQQVEAAErsrmRIEEEIRVVRLQLE--TTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1473
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQ----ELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1474 LRRQVQDESQRKRQAEAElalrvkaeaeaarekqralQALDELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEV 1551
Cdd:COG4717 451 LREELAELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYRE 511
|
....*
gi 256418964 1552 ELQSK 1556
Cdd:COG4717 512 ERLPP 516
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
22-122 |
2.85e-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: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 22 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 93
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 256418964 94 KLVNIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
593-771 |
2.87e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 74.79 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 593 LHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQ 672
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 673 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLQKLQETLRRKYSCDrtiTVTRLEDLLQDAQDEKEQLNEY 752
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 256418964 753 KGHLSGLAKRAKAIVQLKP 771
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1117-2027 |
3.16e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 80.22 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1117 QQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1186
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1187 YRESADPLSAWLQ-DAKRRQEQIQAVP--IANCQAAREQLRQEKALLE-EIERHGEKVEECQKFAKQYINAIKDYELQLI 1262
Cdd:pfam01576 83 RLEEEEERSQQLQnEKKKMQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1263 TYKAQLEPVASPAKK-PKVQSGSESVIQEyVDLRTRYSElttltsqyikfisETLRRMEEEERLAEQQRAEERERLAEVE 1341
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1342 AalekqrQLAEAHAQAkAQAELEAQELQRRMQEEVARREEaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQqveaAERS 1421
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1422 RMRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeA 1500
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1501 EAAREKQRALQALDELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEktAQLERTLQEEHVTVAQ 1580
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1581 LREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAqadaekqkeeaereaRRRGKAEEQAVR 1660
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLS---------------TRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1661 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK------ 1734
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1735 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1793
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1794 LAEEDAARQRAEAERVLTEKLAA---ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERL 1870
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1871 AQLRKASEselERQKGLVedtlRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQL 1950
Cdd:pfam01576 734 QARDEQGE---EKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1951 AAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEK 2027
Cdd:pfam01576 807 MKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEK 884
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1968-2661 |
4.75e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1968 SLAAEEEAARQRKVALEEVERLKAKVEEARRlRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQE 2047
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2048 QNMLDRLRSEaeaarraaeeaeeareqaereaaqsrKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2127
Cdd:PTZ00121 1154 VEIARKAEDA--------------------------RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2128 EQAALKQKQAADAEMEKHK---KFAEQTlRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2204
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAeavKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2205 lfSVRVQMEELGKLKARIEAENraliLRDKDNTQRFLEE---EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA 2281
Cdd:PTZ00121 1287 --EEKKKADEAKKAEEKKKADE----AKKKAEEAKKADEakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2282 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLveetqgfqRTLEAERQRQLEMSAEAErlK 2361
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADEL--------KKAAAAKKKADEAKKKAE--E 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2362 LRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvqtleiQRQQSDHDAERLREAiAELEREKEKLKQEA 2441
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------KADEAKKKAEEAKKA-DEAKKKAEEAKKKA 1499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2442 KLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQ 2521
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2522 ELMAsmEEARRRQREAEEGVRRKQEElqhlEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAlahSEIATTQAASTKALP 2601
Cdd:PTZ00121 1580 LRKA--EEAKKAEEARIEEVMKLYEE----EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV---EQLKKKEAEEKKKAE 1650
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 2602 NGRDAPDGPSVEAEPEY--TFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTVAELTQRED 2661
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1349-1719 |
5.43e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.01 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1349 QLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQsseAEIQAKAQQVeaAERSRMRIEEE 1428
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ---AEMDRQAAIY--AEQERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1429 IRVVRLQLEttERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEAELALRVK-AEAEAAREKQ 1507
Cdd:pfam17380 348 RELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1508 RALQALDELRLQAEEA-ERRLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvtvaqlreeae 1586
Cdd:pfam17380 417 QQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE------------ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1587 rraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQavrQRELA 1665
Cdd:pfam17380 470 --------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE---RRREA 538
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1666 EQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAT 1719
Cdd:pfam17380 539 EEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
139-240 |
5.68e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 71.27 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 139 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 256418964 219 -VDVPQPDEKSIITYVSSLYDAM 240
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
137-234 |
7.42e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.49 E-value: 7.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 212
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 256418964 213 LLDPEDVDVPQPDEKSIITYVS 234
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
137-237 |
7.77e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 70.87 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 216
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 256418964 217 ED-VDVPQPDEKSIITYVSSLY 237
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
963-1563 |
2.54e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 963 ELKDIRLQLEAcETRTVHRLRlpldkdPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1042
Cdd:COG4913 236 DLERAHEALED-AREQIELLE------PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1043 ELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEvlktheEQLKeaqavpatlQELEATKASLKKLRAQAEAQQPVFN 1122
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLE---------REIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1123 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLSAWLQDAK 1202
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1203 RRQEQ-----IQAVPIAnC---QAAREQLRQEKAlleeIER--HGEKV-----EECQKFAKQYINAIKDyELQLITYKAQ 1267
Cdd:COG4913 447 DALAEalgldEAELPFV-GeliEVRPEEERWRGA----IERvlGGFALtllvpPEHYAAALRWVNRLHL-RGRLVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1268 LEPVASPAKKPKVQSGSEsviqeyvdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-EV 1340
Cdd:COG4913 521 TGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1341 EAALEK--QRQLAEAH------AQAKAQAELEAQELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEIqaka 1412
Cdd:COG4913 587 GTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEI---- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1413 qQVEAAERSRMRIEEEIRvvrlQLETterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1492
Cdd:COG4913 662 -DVASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1493 -ALRVKAEAEAAREKQRALQALDELRlqAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEK 1563
Cdd:COG4913 730 dELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3031-3069 |
3.18e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 3.18e-13
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3031 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPELHEKL 3069
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1370-1894 |
4.28e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1370 RRMQEEVA---RREEAAVDAQQQKRSiqeeLQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggA 1446
Cdd:COG4913 228 DALVEHFDdleRAHEALEDAREQIEL----LEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--L 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1447 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAER 1525
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1526 RLrQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTlqeehvtvaqlreeaerraqqqaeaerareeaERE 1605
Cdd:COG4913 381 EF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--------------------------------EAE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1606 LERwqLKAN--------EALRLRLQAE---------------EVAQ-----------------------QKSLAQA---- 1635
Cdd:COG4913 428 IAS--LERRksniparlLALRDALAEAlgldeaelpfvgeliEVRPeeerwrgaiervlggfaltllvpPEHYAAAlrwv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1636 DAEKQKEEAEREARRRGKAEEQAVR--QRELAEqELEKQRQLAEGTAQQRLAA---------EQELIRL-RAETEQG--- 1700
Cdd:COG4913 506 NRLHLRGRLVYERVRTGLPDPERPRldPDSLAG-KLDFKPHPFRAWLEAELGRrfdyvcvdsPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1701 ------------------------EQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1756
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1757 S--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEklaaiseatrlkteaE 1828
Cdd:COG4913 665 SaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---------------L 729
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1829 IALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQ 1894
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1123-1948 |
4.30e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.53 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1123 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQRelEQLGRqlryYRESADPLSAw 1197
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQ--EKIER----YQADLEELEE- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1198 lqdakRRQEQIQAVPIANCQAAREQLRQEKAlLEEIER-------HGEKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1269
Cdd:PRK04863 363 -----RLEEQNEVVEEADEQQEENEARAEAA-EEEVDElksqladYQQALDVQQTRAIQYQQAVQALErAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1270 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERlaeveaALEKQRQ 1349
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR------RLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1350 LAEAHAQAKAQaeleAQELQRRMQEE--VARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEE 1427
Cdd:PRK04863 511 LAEQLQQLRMR----LSELEQRLRQQqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1428 EIRvvrlqletterqrggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDE---SQRKRQAEAELALRVKAEAEAAR 1504
Cdd:PRK04863 587 QLE------------------QLQARIQRLAARAPAWLAAQDALARLREQSGEEfedSQDVTEYMQQLLERERELTVERD 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1505 EKQRALQALDE--LRLQAEEAER--RLRQAeAERARQV-------QVALETA---------QRSAEVELQSKRAsfAEKT 1564
Cdd:PRK04863 649 ELAARKQALDEeiERLSQPGGSEdpRLNAL-AERFGGVllseiydDVSLEDApyfsalygpARHAIVVPDLSDA--AEQL 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1565 AQLERTLQE------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEAL--RLRLQAEEVAQQk 1630
Cdd:PRK04863 726 AGLEDCPEDlyliegdpdsfdDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLFGR---AAREKRieQLRAEREELAER- 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1631 sLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1710
Cdd:PRK04863 802 -YATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLN-------RRRVELERALADHESQEQQQRSQLEQAKEG 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1711 LARL-QHEATAATQKRQELEAELAKVRAEMEvllaskaRAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEE 1787
Cdd:PRK04863 874 LSALnRLLPRLNLLADETLADRVEEIREQLD-------EAEEAKRFVQQHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQ 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1788 AKRQRQlaeedAARQRAEAervLTEklaAISEATRLKTEAEIALKEKEAE-NERLR-RLAEDEAfQRRRLEEQAALHKA- 1864
Cdd:PRK04863 947 AQQTQR-----DAKQQAFA---LTE---VVQRRAHFSYEDAAEMLAKNSDlNEKLRqRLEQAEQ-ERTRAREQLRQAQAq 1014
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1865 --DIEERLAQLRKASeselerqkglveDTLRQRRQ-VEEEIMALKVSF-----EKAAAGKAELELEL--GRIRSNAEDTM 1934
Cdd:PRK04863 1015 laQYNQVLASLKSSY------------DAKRQMLQeLKQELQDLGVPAdsgaeERARARRDELHARLsaNRSRRNQLEKQ 1082
|
890
....*....|....
gi 256418964 1935 RSKEQAELEAARQR 1948
Cdd:PRK04863 1083 LTFCEAEMDNLTKK 1096
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
40-119 |
5.74e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 40 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 111
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 256418964 112 LGLIWTII 119
Cdd:cd21223 105 LALLWRII 112
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
137-237 |
7.06e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 67.75 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 216
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 256418964 217 ED-VDVPQPDEKSIITYVSSLY 237
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1061-1911 |
7.09e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.78 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1061 EKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQ--PVFNTLRDELRGAQEVGERL 1138
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEEriDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1139 QQRHGERDVEVERWR---ERVTQLLERWQAVLAqtdvrqRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIAN 1215
Cdd:pfam02463 260 IEKEEEKLAQVLKENkeeEKEKKLQEEELKLLA------KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1216 CQAAREQLRQEKALLEEIERHGEKVEEC-QKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDL 1294
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELeKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1295 RTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqakaqAELEAQELQRRMQE 1374
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED-------LLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1375 EVARREEAAVDAQQQKRSIQEELQHLRqsseaeiqakAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALR 1454
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLL----------ALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1455 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAER 1534
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1535 ARQVQVALETaQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1614
Cdd:pfam02463 637 LKESAKAKES-GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1615 EALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1694
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1695 ----AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR 1770
Cdd:pfam02463 796 lkaqEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1771 FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE--AENERLRRLAEDE 1848
Cdd:pfam02463 876 EEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELllEEADEKEKEENNK 955
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1849 AFQRRRlEEQAALHKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEEEIMALKVSFEK 1911
Cdd:pfam02463 956 EEEEER-NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE---KERLEEEKKKLIRAIIEE 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1320-2027 |
1.15e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1320 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEAQELQRRMQE----EVARREEAAVdaqQQKRSIQE 1395
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyegyELLKEKEALE---RQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQHLRQS---SEAEIQAKAQQVEAAERSRMRIEEEIRVVrlqletterqrggAEGELQALRARAEEAEAqkrqaqeEAE 1472
Cdd:TIGR02169 245 QLASLEEElekLTEEISELEKRLEEIEQLLEELNKKIKDL-------------GEEEQLRVKEKIGELEA-------EIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1473 RLRRQVQDESQRKRQAEAELAlrvKAEAEaarekqralqaLDELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEVE 1552
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLA---KLEAE-----------IDKLLAEIEELEREIEEERKRRD-----KLTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1553 LQSKRASFAEKTAQLERTLQEehvtvaqlreeaerraqqqaeaeraREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1632
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDE-------------------------LKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1633 AQADAEKQkeeaeREARRRGKAEEQAVRqrELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1712
Cdd:TIGR02169 421 ELADLNAA-----IAGIEAKINELEEEK--EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1713 RLQHEATAATQ-----KRQELE------------AELAKVRAEMEVLLASKA----------------------RAEEES 1753
Cdd:TIGR02169 494 EAEAQARASEErvrggRAVEEVlkasiqgvhgtvAQLGSVGERYATAIEVAAgnrlnnvvveddavakeaiellKRRKAG 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1754 RST-----------SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE-DAARQRAEAERVLT------EKLA 1815
Cdd:TIGR02169 574 RATflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDiEAARRLMGKYRMVTlegelfEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1816 AI-----------SEATRLKTEA-EIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLR-KASESELE 1882
Cdd:TIGR02169 654 AMtggsraprggiLFSRSEPAELqRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEiEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1883 RQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELeaaRQRQLAAEEEQRRREAE 1962
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI---PEIQAELSKLEEEVSRI 810
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1963 ERVQRSLAAEEEAARQRKVALE-EVERLKAKVE--EARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2027
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEkEIQELQEQRIdlKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1075-1571 |
1.28e-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: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1075 GAEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELrgAQEVGERLQQRHGERDVEVERWRE 1154
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1155 RVTQLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEI 1233
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1234 ErhgEKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIS 1313
Cdd:COG4913 397 E---EELEALEEALAEAEAALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAELEAQELQRRM- 1372
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1373 ----------QEEVARREEAA-VDAQQQ----KRSIQEELQ--------------HLR------QSSEAEIQAKAQQVEA 1417
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRsryvlgFDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1418 AERSRMRIEEEIRVVRLQLETTERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDESQRK 1485
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1486 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSKRASFAEK 1563
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 256418964 1564 TAQLERTL 1571
Cdd:COG4913 782 LNRAEEEL 789
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4285-4323 |
1.51e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 1.51e-12
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 4285 LLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMVDRI 4323
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
24-125 |
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 256418964 24 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
139-238 |
2.11e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 66.21 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 139 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 214
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 256418964 215 DPEDVdVPQPDEKSIITYVSSLYD 238
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1334-1859 |
3.30e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 73.35 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1334 RERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQ 1413
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1414 QVEAAERSRMRIEEEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEA 1490
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1491 ELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1570
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1571 LQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR 1650
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1651 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA 1730
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1731 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1810
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 256418964 1811 TEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1859
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1448-2026 |
3.41e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 73.35 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1448 GELQALRARAEEA--EAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAeAEAARekqralqaldeLRLQAEEAER 1525
Cdd:COG3899 699 GERDRAARLLLRAarRALARGAYAEALRYLERALELLPPDPEEEYRLALLLEL-AEALY-----------LAGRFEEAEA 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1526 RLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQlreeaerrAQQQAEAERAREEAERE 1605
Cdd:COG3899 767 LLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAE--------RLGDRRLEARALFNLGF 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1606 LERWQLKANEALRLRLQAEEVAQQKSLAQADAekqkeeaEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1685
Cdd:COG3899 839 ILHWLGPLREALELLREALEAGLETGDAALAL-------LALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAA 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1686 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskQRLE 1765
Cdd:COG3899 912 ALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAA---------AAAA 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1766 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1845
Cdd:COG3899 983 AAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAAL 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1846 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGR 1925
Cdd:COG3899 1063 AAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAAL 1142
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1926 IRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQ 2005
Cdd:COG3899 1143 ALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAAL 1222
|
570 580
....*....|....*....|.
gi 256418964 2006 ESARQLQLAQEAAQKRLQAEE 2026
Cdd:COG3899 1223 LLLLLLAALALAAALLALRLL 1243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3107-3145 |
3.58e-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: 3.58e-12
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3107 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETNRAL 3145
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
139-234 |
3.76e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.49 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 139 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 217
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 256418964 218 DVDVPQPDEKSIITYVS 234
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3362-3400 |
3.79e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 3.79e-12
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3362 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3400
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1085-1807 |
4.42e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.06 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1085 EQLKEAQAvpATLQELEATKASLKKLRAQAEAQQPV------FNTLRDELRGAQEVGERLQQRHGERDVEVERWRERV-- 1156
Cdd:COG3096 316 EELSARES--DLEQDYQAASDHLNLVQTALRQQEKIeryqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVds 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1157 --TQLLERWQAVlaqtDVRQRE----------LEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQ------A 1218
Cdd:COG3096 394 lkSQLADYQQAL----DVQQTRaiqyqqavqaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsvadA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1219 AREQLRQEKALLEEIERHGEKVEECQKfAKQYINAIKDYELQLitykAQLEPVAspakkpkvqsgsesviQEYVDLRTRY 1298
Cdd:COG3096 470 ARRQFEKAYELVCKIAGEVERSQAWQT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1299 S---ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAE---------LEAQ 1366
Cdd:COG3096 529 RqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaarapawLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1367 ELQRRMQEEVArreEAAVDAQQQKRSIQEELQHLRQsseaeiqAKAQQVEAAERsRMRIEEEIRvvRLQletterQRGGA 1446
Cdd:COG3096 609 DALERLREQSG---EALADSQEVTAAMQQLLERERE-------ATVERDELAAR-KQALESQIE--RLS------QPGGA 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1447 E-GELQALRAR-----------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQR 1484
Cdd:COG3096 670 EdPRLLALAERlggvllseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVF 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1485 KRQaEAELALRVKAE---------------AEAAREKQralqaLDELRLQAEE-----AERRLRQAEAER---------A 1535
Cdd:COG3096 750 DAE-ELEDAVVVKLSdrqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1536 RQVQVALETaqrSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRA-------QQQAEAERAREEAERELER 1608
Cdd:COG3096 824 GHLAVAFAP---DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1609 WQLKANEALR-LRLQAEEVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLA 1685
Cdd:COG3096 901 ELDAAQEAQAfIQQHGKALAQLEPLVAVlQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLG 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1686 AEQELI-RLRAETEQGEQQRQLLEEELARLQHEATAATQKR--------------QELEAELakvrAEMEVLLAskARAE 1750
Cdd:COG3096 981 ENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAE 1054
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1751 EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1807
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1318-2441 |
6.60e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 72.52 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1318 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHA----QAKAQAEL--EAQELQRRMQ------EEVARREE 1381
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalqeQLQAETELcaEAEEMRARLAarkqelEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1382 AAVDaQQQKRSIQeeLQHLRQSSEAEIQAKAQQVEAAERSRMrieeeirvvRLQLETTErqrggAEGELQALRARAEEAE 1461
Cdd:pfam01576 82 SRLE-EEEERSQQ--LQNEKKKMQQHIQDLEEQLDEEEAARQ---------KLQLEKVT-----TEAKIKKLEEDILLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1462 AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKaeaeaAREKQRALQALDELRLQAEEAERRlrqaEAERARQVQVA 1541
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSK-----LKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1542 LETAQRSAEVELQskrASFAEKTAQLERtlQEEHVTVAQLreeaerraqqqaeaerareeaerELERWQLKANEALRlrl 1621
Cdd:pfam01576 216 ESTDLQEQIAELQ---AQIAELRAQLAK--KEEELQAALA-----------------------RLEEETAQKNNALK--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1622 QAEEVAQQKSLAQADAEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTaQQRLAAEQELiRLRAETEQGE 1701
Cdd:pfam01576 265 KIRELEAQISELQEDLESERA-----------ARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQEL-RSKREQEVTE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1702 QQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfREL 1774
Cdd:pfam01576 332 LKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlQQAKQDSEHKR-KKL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1775 AEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-------------LTEKLAAIS-----------EATRLKTEAEIA 1830
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegknikLSKDVSSLEsqlqdtqellqEETRQKLNLSTR 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1831 LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEIMALKVSFE 1910
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLE 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1911 KAAAGKAELELELGRIRSNAEDTMrskeqaeLEAARQRQLAAEEEQRRREAEErvqrsLAAEEEAARQRKVALEEVERLK 1990
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAE 630
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1991 AKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqnmLDRLRSEAEAARRAAEEAEE 2070
Cdd:pfam01576 631 AREKETRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELER 685
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2071 AREQAEREAAQSRKQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalKQKQAADAEMEKHKKfae 2150
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR--- 745
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2151 QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2230
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2231 LRDKDNTQRFLEEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2310
Cdd:pfam01576 826 AQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSN 904
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2311 KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQrqleMSAEAERLKLRMAEMSRAQ---------------ARAE 2375
Cdd:pfam01576 905 TELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ----LERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLE 980
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2376 EDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA 2441
Cdd:pfam01576 981 EQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2703-2741 |
6.95e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 6.95e-12
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 2703 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2741
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
139-239 |
7.49e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 64.68 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 139 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 256418964 219 VdVPQPDEKSIITYVSSLYDA 239
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3940-3978 |
9.05e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 9.05e-12
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3940 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3978
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3773-3811 |
9.23e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 9.23e-12
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3773 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3811
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1401-2027 |
1.80e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.02 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1401 RQSSEAEIQAKAQQVEA--AERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1474
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1475 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1554
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1555 SKRASFAEKTAQLERTLQEEHVT-VAQLREEAERRAQQQAEAERAREEAERELE---RWQLKAN------EALRLRLQAE 1624
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALEselREQLEAGklefneEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1625 EVAQQKSLAQADAEK--QKEEAEREARRRGKAEEQAVRQRELAEQELekqrqlaegtAQQRLAAEQELIRLRAETEQGEQ 1702
Cdd:pfam12128 448 ELKLRLNQATATPELllQLENFDERIERAREEQEAANAEVERLQSEL----------RQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1703 QRQLLEEelARLQHEATAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAE 1776
Cdd:pfam12128 518 RQSALDE--LELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1777 EAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE 1856
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1857 EQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEkaaagkAELELELGRIRSN--AEDTM 1934
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSG 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1935 RSKEQAELEAARQRQLAAE-EEQRRREAEERVQRSLAAEEEAARQRKVA------------LEEVERLKAKVEEARRLRE 2001
Cdd:pfam12128 745 AKAELKALETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAIS 824
|
650 660
....*....|....*....|....*.
gi 256418964 2002 RAEQESARQlqlaQEAAQKRLQAEEK 2027
Cdd:pfam12128 825 ELQQQLARL----IADTKLRRAKLEM 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1653-1869 |
1.95e-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: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1732
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1733 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1808
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1809 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEER 1869
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
937-1573 |
3.16e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 937 SRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACEtrtvhrLRLPLDKDPARECAQRIAEQQKAQA-EVEGLGKGV 1015
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLT------LRSQLLTLCTPCMPDTYHERKQVLEkELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1016 ARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVlKTHEEQLKEAQAVPA 1095
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1096 TLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE-------------RWRERVTQLLER 1162
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREiscqqhtltqhihTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1163 WQAVLAQTDVRQRELEQLGRQLRYYR-------------ESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKAL 1229
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1230 LEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTRYSELTTL 1304
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1305 TSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAV 1384
Cdd:TIGR00618 555 RKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1385 DAQQQKRsIQEELQHLRQssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALraraEEAEAQK 1464
Cdd:TIGR00618 634 LQQCSQE-LALKLTALHA--LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML----AQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1465 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAeaarekqralQALDELRLQAEEAERRLRQAEAERARQVQVALET 1544
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALN----------QSLKELMHQARTVLKARTEAHFNNNEEVTAALQT 776
|
650 660 670
....*....|....*....|....*....|.
gi 256418964 1545 AQRSAEV--ELQSKRASFAEKTAQLERTLQE 1573
Cdd:TIGR00618 777 GAELSHLaaEIQFFNRLREEDTHLLKTLEAE 807
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1288-1786 |
4.10e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.99 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1288 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaqakaqaeleaqE 1367
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1368 LQRRMQEEVARREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrgg 1445
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1446 aegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQR----------KRQAEAELAlRVKA-------EAEAAREKQR 1508
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALE-RAKQlcglpdlTADNAEDWLE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1509 ALQA-LDELRLQAEEAERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVTVAQLreeae 1586
Cdd:PRK04863 446 EFQAkEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL----- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1587 rraqqqaeaerareeaerelerwqlkanEALRLRLQAeevAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE 1666
Cdd:PRK04863 516 ----------------------------QQLRMRLSE---LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1667 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEATAATQKRQELEAELAKvraemevlL 1743
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------L 636
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 256418964 1744 ASKARAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1786
Cdd:PRK04863 637 LERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1628-1837 |
4.70e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.29 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1628 QQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAegtaQQRLAAeQELIRLRAETEQGEQQRQLL 1707
Cdd:PRK09510 68 QQQQKSAKRAEEQRKK---------KEQQQAEELQQKQAAEQERLKQLE----KERLAA-QEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1708 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1787
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAE---AKKKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1788 AKRQRQLAEEDAARQ-RAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1837
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1294-1950 |
6.34e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 69.01 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1294 LRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQ---AELEAQELQR 1370
Cdd:pfam07111 53 LELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEglrAALAGAEMVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1371 RMQEEVARREeaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSrmrieeeirvvrlqLETTERQRGGAEGEL 1450
Cdd:pfam07111 132 KNLEEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1451 QalraraeeaeaqkrQAQEEAERLRRQVqdeSQRKRQAEAELALrvkaeAEAAReKQRALQALDELRLQAEEAERRLRQA 1530
Cdd:pfam07111 193 A--------------EAQKEAELLRKQL---SKTQEELEAQVTL-----VESLR-KYVGEQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1531 EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLreeaerraqqqaeaeraREEAERELERWQ 1610
Cdd:pfam07111 250 TMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEF-----------------PKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1611 LKANeALRLRLQAEEVAQQKSLAQADAEkqkeEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLAEGTAQQRLAAEQ 1688
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQ----VAELQEQVTSQSQEQAILQRALQDKaaEVEVERMSAKGLQMELSRAQE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1689 ELIRLRAETEQGEQQRQL-----------LEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASK---ARAEEESR 1754
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKvalAQLRQESC 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1755 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1834
Cdd:pfam07111 467 PPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1835 EAENER--LRRLAEDEAFQRRRLEEQAALHKADIEERLAQLrkasESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKA 1912
Cdd:pfam07111 546 QLEVARqgQQESTEEAASLRQELTQQQEIYGQALQEKVAEV----ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
650 660 670
....*....|....*....|....*....|....*...
gi 256418964 1913 AAGKAELELELGRIRSNAEdtmrsKEQAELEAARQRQL 1950
Cdd:pfam07111 622 ATQEKERNQELRRLQDEAR-----KEEGQRLARRVQEL 654
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
17-116 |
7.83e-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: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 88
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 256418964 89 RHRQVKLVNIRNDDIADGNPKLTLGLIW 116
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1331-1847 |
1.10e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1331 AEERERLaeVEAALEKQRQLAEAHAQAKAQaeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqssEAEIQA 1410
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAE-----QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ---TALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1411 KA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRkrqa 1488
Cdd:PRK04863 348 EKieRYQADLEELEERLEEQNEVVEEADE------------------QQEENEARAEAAEEEVDELKSQLADYQQA---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1489 eaelalrVKAEAEAAREKQRALQALDELR-------LQAEEAERRLRQAEAERARQVQVALETAQRsaeVELQSKRASFA 1561
Cdd:PRK04863 406 -------LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1562 EKTAQLERTLQEEHVtvaqlreeaerraqqqaeaerareeaerelerwqlkanealrlRLQAEEVAQQkslaqadaekqk 1641
Cdd:PRK04863 476 EQAYQLVRKIAGEVS-------------------------------------------RSEAWDVARE------------ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1642 eeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1721
Cdd:PRK04863 501 ------------LLRRLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1722 tqkRQELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdAAR 1801
Cdd:PRK04863 567 ---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE-YMQ 634
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 256418964 1802 QRAEAERVLTEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAED 1847
Cdd:PRK04863 635 QLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1517-1856 |
1.44e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.84 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1517 RLQAEEAER----RLRQAEAERARQVQV--ALETAQRSAEVELQSKRASFAEKtaqlERTLQEEHvtvaqlreeaerraq 1590
Cdd:pfam17380 287 RQQQEKFEKmeqeRLRQEKEEKAREVERrrKLEEAEKARQAEMDRQAAIYAEQ----ERMAMERE--------------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1591 qqaeaerareeaeRELERWQL----KANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGkAEEQAVRQRELAE 1666
Cdd:pfam17380 348 -------------RELERIRQeerkRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA-ARKVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1667 QELEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQHeataaTQKRQELEAELAKVRAEMEVLLASK 1746
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1747 ARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLTEKLAAISEATRL 1823
Cdd:pfam17380 487 KRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEMEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|...
gi 256418964 1824 KTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1856
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2133-2335 |
1.48e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2212
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2213 EEL----------GKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAL 2282
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2283 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2335
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1300-1517 |
1.66e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 66.82 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1300 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAELEA 1365
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1366 QELQRRMQEEVARRE-EAAVDAQQQKRSIQEELQhlrqsseAEIQAKAQQVEAAERSRMRIEEEirvvrlqLETTERQRg 1444
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANAEREVQRQ-------LEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1445 gAEGELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELR 1517
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1628-1823 |
2.19e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1628 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1707
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1708 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1787
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 256418964 1788 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRL 1823
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4361-4399 |
2.23e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.23e-10
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 4361 FLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTAQKL 4399
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1618-2030 |
2.41e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1618 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRA 1695
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1696 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1775
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1776 EEAARLRALAEEAKRQRQLAEED---------------AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENER 1840
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1841 LRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEIMALKVSFEKAAAGKAEl 1919
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1920 elelgRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAE-EEAARQRKVALEEVERLKAKVEEAR- 1997
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEa 460
|
410 420 430
....*....|....*....|....*....|...
gi 256418964 1998 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2030
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1331-1819 |
2.68e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.28 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1331 AEERERLaeVEAALEKQRQLAEAHAQAkaqaeLEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELqhlrqsseAEIQA 1410
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQL-----AEEQYRLVEMARELEELSARESDLEQDYQAASDHL--------NLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1411 KAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQAEA 1490
Cdd:COG3096 342 ALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1491 ELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqSKRASFAEKTAQLERT 1570
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD--AARRQFEKAYELVCKI 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1571 LQEehVTVAQlreeaerraqqqaeaerareeaereleRWQlKANEALR----LRLQAEEVAQ-QKSLAQAdaekqkeeae 1645
Cdd:COG3096 485 AGE--VERSQ---------------------------AWQ-TARELLRryrsQQALAQRLQQlRAQLAEL---------- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1646 rearrrgkaeEQAVRQRELAEQELEkqrQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1725
Cdd:COG3096 525 ----------EQRLRQQQNAERLLE---EFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1726 QELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1795
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPG 667
|
490 500
....*....|....*....|....
gi 256418964 1796 EEDAARQRAEAERVLTEKLAAISE 1819
Cdd:COG3096 668 GAEDPRLLALAERLGGVLLSEIYD 691
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
23-119 |
3.71e-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: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 23 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 88
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 256418964 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1692-2246 |
4.26e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1692 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1771
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1772 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE---AENERLRRLA 1845
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1846 EDEAFQRRRLEEQA---ALHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAEL 1919
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1920 ELELGRIRSNAEDTmRSKE---QAELEAARQR------------------QLAAEEEQRRREAEERVQRSLAAEEEAARQ 1978
Cdd:PRK02224 411 EDFLEELREERDEL-REREaelEATLRTARERveeaealleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1979 RKVALEE-VERLKAKVEEARRLRERAEQESArqlqLAQEAAQKRLQAEEKAHAfvvqqreeelqqtlqqeqnmLDRLRSE 2057
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRER--------------------AEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2058 AEAARRAAEEAEEAREQAereaaqsRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA 2137
Cdd:PRK02224 546 AAELEAEAEEKREAAAEA-------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2138 ADAEMEKHKKFAEQTLRqKAQVEQELTTLRlqLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGK 2217
Cdd:PRK02224 619 AELNDERRERLAEKRER-KRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
570 580 590
....*....|....*....|....*....|
gi 256418964 2218 LKARIEA-ENRALILRDkdntqrfLEEEAE 2246
Cdd:PRK02224 696 LRERREAlENRVEALEA-------LYDEAE 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1350-1574 |
4.55e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1350 LAEAHAQAKAQAELEAQelQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEI 1429
Cdd:COG4942 12 ALAAAAQADAAAEAEAE--LEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1430 RVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR-------QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1502
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1503 AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1574
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1434-1875 |
5.41e-10 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 65.76 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1434 LQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAL 1513
Cdd:COG4995 17 LALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1514 DELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQA 1593
Cdd:COG4995 97 ALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1594 EAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR 1673
Cdd:COG4995 177 LALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1674 QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1753
Cdd:COG4995 257 LLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1754 RSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKE 1833
Cdd:COG4995 337 LLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAAL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1834 KEAENERLRRLAEDEAFQR-------RRLEEQAALHK---ADIEERLAQLRK 1875
Cdd:COG4995 417 ALLLALAAYAAARLALLALieyiilpDRLYAFVQLYQlliAPIEAELPGIKR 468
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
14-122 |
6.56e-10 |
|
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: 59.52 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 14 LKDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDY 87
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALEL 86
|
90 100 110
....*....|....*....|....*....|....*
gi 256418964 88 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21222 87 MEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
497-686 |
7.61e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.08 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 497 LRYLQDLLAWVEENQRRIDSAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQLSPATRGAY---RDCLGRLD 573
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 574 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEI 650
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 256418964 651 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 686
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1328-1894 |
7.66e-10 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 65.59 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1328 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQeevarreeAAVDAQQQKRSIQEELQHLRQSSEAE 1407
Cdd:PRK10246 219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ--------ALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1408 I-----QAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRggAEGELQALRARAEEAEAQKRQAQ--EEAERLR----- 1475
Cdd:PRK10246 291 QlrphwERIQEQSAALAHTRQQIEE----VNTRLQSTMALR--ARIRHHAAKQSAELQAQQQSLNTwlAEHDRFRqwnne 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1476 ---------RQVQDESQRKRQAEAELALRVK----------------AEAEAAREKQRAL-QALDELRLQAEEAERRLRQ 1529
Cdd:PRK10246 365 lagwraqfsQQTSDREQLRQWQQQLTHAEQKlnalpaitltltadevAAALAQHAEQRPLrQRLVALHGQIVPQQKRLAQ 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1530 AEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLE--RTLQEEHVTVAQLREEAERRAQQQAEAE--RAREEAERE 1605
Cdd:PRK10246 445 LQVAIQN-----VTQEQTQRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEA 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1606 LERWQLKANEALRLRLQaEEVAQQKS-----LAQADAEKQKEEaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTA 1680
Cdd:PRK10246 520 YQALEPGVNQSRLDALE-KEVKKLGEegaalRGQLDALTKQLQ---------RDESEAQSLRQ-EEQALTQQWQAVCASL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1681 QQRLAAEQELIRLRAETEQGEQQRQLLEEELArLQHEATAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESR 1754
Cdd:PRK10246 589 NITLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1755 STSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLTEKLAAISEATrLKTEAEIALKEK 1834
Cdd:PRK10246 668 ATRQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQ 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1835 EAENERlRRLAE-----DEAFQRRRLEEQAALHKADIEE----RLAQLRKASESELERQKGLVEDTLRQ 1894
Cdd:PRK10246 739 QDVLEA-QRLQKaqaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVTQTAQA 806
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2233-2579 |
9.46e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.14 E-value: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2233 DKDNTQRFLEEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaEAELLQQQKE 2312
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------QAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2313 LAQEQARRLQEDKEQmaqqlveetqgfQRTLEAERQRQLEMSAEAERlklrMAEMSRAQARAEEDAQRFRKQAEEIGE-K 2391
Cdd:pfam17380 342 MAMERERELERIRQE------------ERKRELERIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKvK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2392 LHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEakllqlkseEMQTVQQEQILQETQALQKSFL 2471
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE---------EQERQQQVERLRQQEEERKRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2472 SEKDSLLQRERFIEQEKAKLEQLFQDEVAKAkqlreeqqrqqqQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHL 2551
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKELEERKQA------------MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK 544
|
330 340
....*....|....*....|....*...
gi 256418964 2552 EQQRqqqekllaEENQRLRERLQRLEEE 2579
Cdd:pfam17380 545 QQEM--------EERRRIQEQMRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1623-2026 |
1.02e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1623 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQ 1702
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1703 QRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1782
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1783 ALAEEAKRQRQLAEE----DAARQRAEAERV--LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1856
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLE 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1857 EQAalhkADIEERLAQLRKASESELERQkglveDTLRQRRQVEEEIMALKvsfeKAAAGKAELELELGRIRSNAEDtmrs 1936
Cdd:PRK02224 516 ERR----EDLEELIAERRETIEEKRERA-----EELRERAAELEAEAEEK----REAAAEAEEEAEEAREEVAELN---- 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1937 KEQAELEAARQRqlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLA-- 2014
Cdd:PRK02224 579 SKLAELKERIES--------------LERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfd 644
|
410
....*....|....*.
gi 256418964 2015 ----QEAAQKRLQAEE 2026
Cdd:PRK02224 645 eariEEAREDKERAEE 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2134-2440 |
1.07e-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: 65.09 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2134 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEEL------FS 2207
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-------LTEEISELEKRLEEIEQLLEELNKKIkdlgeeEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2208 VRVQmEELGKLKARIEaenralilrdkdNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRalaekml 2287
Cdd:TIGR02169 290 LRVK-EKIGELEAEIA------------SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2288 KEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAqQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEM 2367
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2368 SRAQARAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQsdhdAERLREAIAELEREKEKLKQE 2440
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEI---KKQEWKLEQLAADLSKYEQE----LYDLKEEYDRVEKELSKLQRE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1287-1852 |
1.08e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1287 VIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQAELEAQ 1366
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE-KLEKEVKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1367 ELQRRMQEEvarrEEAAVDAQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRG 1444
Cdd:PRK03918 249 SLEGSKRKL----EEKIRELEERIEELKKEIEELEEKVKelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1445 GAEGELQAL---RARAEEAEAQKRQAQEEAERLRRQVQdESQRKRQAEAELAlRVKAEaEAAREKQRALQALDELRLQAE 1521
Cdd:PRK03918 325 GIEERIKELeekEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELE-RLKKR-LTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1522 EAERRLRQAEAERARQVQ---------VALETAQRSAEV----------------------ELQSKRASFAEKTAQLERT 1570
Cdd:PRK03918 402 EIEEEISKITARIGELKKeikelkkaiEELKKAKGKCPVcgrelteehrkelleeytaelkRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1571 LQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR 1650
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1651 RGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA 1730
Cdd:PRK03918 562 EKKLDELEEELAEL-LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1731 ELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAarqraeaeRVL 1810
Cdd:PRK03918 641 RLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAELEELEKRREEIKKTL--------EKL 699
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 256418964 1811 TEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 1852
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1316-1532 |
1.13e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1316 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1395
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ---ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1472
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1473 RLRRQVqdesQRKRQAEAELALRVKAEAEAAREKQRALQALDEL--RLQAEEAERRLRQAEA 1532
Cdd:COG4942 189 ALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2132-2648 |
1.21e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2132 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQ 2211
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2212 MEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2291
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2292 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVE-ETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRA 2370
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2371 QARAEEDAQRFRKQAEEIGEKLHRTE-----------------------------LATQEKVT----------------- 2404
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVDegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2405 -LVQTLEIQRQ--QSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEE-----------------------MQTVQQEQ 2458
Cdd:TIGR02168 550 vVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2459 ILQETQALQKS------------------------FLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQ 2514
Cdd:TIGR02168 630 DLDNALELAKKlrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2515 QMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQA 2594
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 2595 ASTKALPNGRDAPDGPSVEAEPEYT---FEGLRQKVPAQQLQEAGILSQEELQRLAQ 2648
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTllnEEAANLRERLESLERRIAATERRLEDLEE 845
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4283-4320 |
1.51e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 55.95 E-value: 1.51e-09
10 20 30
....*....|....*....|....*....|....*...
gi 256418964 4283 QRLLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMV 4320
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
895-1515 |
1.53e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 895 EEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLV----AEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQ 970
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 971 LEacetrtvhrlrlpldkdparecaQRIAEQqkaqaeveglgkGVARLSAeaekvlalpepspaaptLRSELELTLGKLE 1050
Cdd:COG4913 328 LE-----------------------AQIRGN------------GGDRLEQ-----------------LEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1051 QVRSLSAIYLEKLKTISLVIRSTqgaeevlkthEEQLKEAQA-VPATLQELEATKASLKKLRAQAEAQqpvFNTLRDELR 1129
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPAS----------AEEFAALRAeAAALLEALEEELEALEEALAEAEAA---LRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1130 GAQEVGERLQQRHGERDVEVERWRERVTQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----R 1185
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1186 YYREsadpLSAWLQDAKRRQE-QIQAVPIANCQAAREQLrQEKALLEEIErhgEKVEECQKFAKQYINAIKDYELqlity 1264
Cdd:COG4913 497 HYAA----ALRWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLD---FKPHPFRAWLEAELGRRFDYVC----- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1265 kaqlepVASPAkkpkvqsgsesviqeyvDLRtRYSELTTLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERE 1335
Cdd:COG4913 564 ------VDSPE-----------------ELR-RHPRAITRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1336 RLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmqEEVARREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKAQQV 1415
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQL 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1416 EAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDESQRKRQAEAELAL 1494
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELRENLEER 774
|
650 660
....*....|....*....|.
gi 256418964 1495 RVKAEAEAAREKQRALQALDE 1515
Cdd:COG4913 775 IDALRARLNRAEEELERAMRA 795
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1129-1554 |
1.60e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.59 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1129 RGAQEvgERLQQRHGERDVEVERWR---------ERVTQLLERW-------------QAVLAQTDVRQRELEqlgRQLRY 1186
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELE---RELAQ 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1187 YRESADPLSAWLQDAKRRQEQIQA-VPIANCQAArEQLRQekaLLEEIERHGEKVEECQKFAKQYINAIkdyelqlityk 1265
Cdd:COG3096 855 HRAQEQQLRQQLDQLKEQLQLLNKlLPQANLLAD-ETLAD---RLEELREELDAAQEAQAFIQQHGKAL----------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1266 AQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltSQYIKFISETLRRM------EEEERLAEQQRAEE--RERL 1337
Cdd:COG3096 920 AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRL----KQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEklRARL 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1338 AEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHLrqsseaEIQAKAQQVEA 1417
Cdd:COG3096 994 EQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL------GVQADAEAEER 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1418 AERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEA 1490
Cdd:COG3096 1057 ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERRLHRR 1136
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1491 ELalrvkaeaeaarekqrALQALDELRLQAEEAERRLRQAEAERArQVQVALETAQ--RSAEVELQ 1554
Cdd:COG3096 1137 EL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEdpRRPERKVQ 1185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1356-2502 |
1.61e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.43 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1356 QAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQhlrqsSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlq 1435
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1436 letterqrggaegeLQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEAELALRVKAEAEAAREKQRALQALDE 1515
Cdd:pfam01576 77 --------------LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAARQKLQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1516 LRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT-AQLERTLQEEHVTVAQLREEAERRAQQQAE 1594
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1595 AERAREEAERELE--RWQL--KANEALRLRLQAEEVAQQKSLAQA---DAEKQKEEAEREARRRGKAEEQAVRQRELAEQ 1667
Cdd:pfam01576 220 LQEQIAELQAQIAelRAQLakKEEELQAALARLEEETAQKNNALKkirELEAQISELQEDLESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1668 ELEKQRQLAEGTaQQRLAAEQELiRLRAETEQGEQQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1744
Cdd:pfam01576 300 ELEALKTELEDT-LDTTAAQQEL-RSKREQEVTELKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1745 SKARAEEESRSTSEK----SKQRLEAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV----------- 1809
Cdd:pfam01576 378 AKQALESENAELQAElrtlQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegkn 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1810 --LTEKLAAIS-----------EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdieeRLAQLRKA 1876
Cdd:pfam01576 457 ikLSKDVSSLEsqlqdtqellqEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKK 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1877 SESELERQKGLVEDtlrqRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMrskeqaeLEAARQRQLAAEEEQ 1956
Cdd:pfam01576 533 LEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEK 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1957 RRREAEErvqrsLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqr 2036
Cdd:pfam01576 602 KQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAE----------- 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2037 eeelqqtlqqeqnmLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQaqaqaqaqaaaeKLRKE 2116
Cdd:pfam01576 666 --------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA------------KLRLE 719
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2117 AEQeaarraqaeqaalkqkQAAdaemekhkkfaeqtlrqKAQVEQELTTLRLQLEEtdhQKSILDEELQRLKAEVTEAAR 2196
Cdd:pfam01576 720 VNM----------------QAL-----------------KAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERK 763
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2197 QRSQveeeLFSVRVQME-ELGKLKARIEAENRAlilRDkdntqrfleeeaEKMKQVAEEAARLSVAAQEAARLRQLAEED 2275
Cdd:pfam01576 764 QRAQ----AVAAKKKLElDLKELEAQIDAANKG---RE------------EAVKQLKKLQAQMKDLQRELEEARASRDEI 824
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2276 LAQQRAlAEKMLKekmqavqeatrlKAEAELLQQQKELA-QEQARR-LQEDKEQMAQQLVEETQGfqRTLEAERQRQLEm 2353
Cdd:pfam01576 825 LAQSKE-SEKKLK------------NLEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE- 888
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2354 saeaERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDHDAERLREAIAELERE 2433
Cdd:pfam01576 889 ----ARIAQLEEELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKELKAKLQEMEGT 960
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2434 -KEKLKQ-----EAKLLQLKSEEMQTVQQEQilQETQALQKSFLSEKDSLLQRErfieqekakleqlfqDEVAKA 2502
Cdd:pfam01576 961 vKSKFKSsiaalEAKIAQLEEQLEQESRERQ--AANKLVRRTEKKLKEVLLQVE---------------DERRHA 1018
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1342-1574 |
1.70e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 64.20 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1342 AALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLR--QSSEAEIQAKAQQVEAA 1418
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEArAAKDKDAVAAALARVKakKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1419 ERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1498
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1499 EAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1574
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1326-1537 |
1.74e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1326 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMqeevARREEAAVDAQQQKRSIQEEL-------Q 1398
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELaelekeiA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1399 HLRQSSEAEIQAKAQQVEAAERSRMR-----------IEEEIRVVRLQLETTERQRggaeGELQALRARAEEAEAQKRQA 1467
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARR----EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1468 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1537
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1140-1948 |
2.12e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.20 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1140 QRHGERDVEVER-WRERVTQLLERwQAVLAQTdvrQRELEQLGRQLRYYRESADPLSAWL---QDAKRRQEQIQAVpIAN 1215
Cdd:COG3096 281 RELSERALELRReLFGARRQLAEE-QYRLVEM---ARELEELSARESDLEQDYQAASDHLnlvQTALRQQEKIERY-QED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1216 CQAAREQLRQEKALLEEIErhgEKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpkVQSGSESVIQEYVDLR 1295
Cdd:COG3096 356 LEELTERLEEQEEVVEEAA---EQLAEAEARLEAAEEEVDSLKSQLADYQQALD----------VQQTRAIQYQQAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1296 TRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAA---LEKQRQLAEAHAQA--KAQAELEAQELQR 1370
Cdd:COG3096 423 EKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAArrqFEKAYELVCKIAGEveRSQAWQTARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1371 RMQEEVARreeaAVDAQQQKRSIQEELQHLRQSSEAEIQAK------AQQVEAA---ERSRMRIEEEIRVVRLQLETTER 1441
Cdd:COG3096 503 RYRSQQAL----AQRLQQLRAQLAELEQRLRQQQNAERLLEefcqriGQQLDAAeelEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1442 QRGGAEGELQALRARAEEAEAQK---RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRL 1518
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1519 QAeeaeRRLRQAE-AERARQVQ----------------VALETA---------QRSAEVELQSKRAsfAEKTAQLERTLQ 1572
Cdd:COG3096 659 QI----ERLSQPGgAEDPRLLAlaerlggvllseiyddVTLEDApyfsalygpARHAIVVPDLSAV--KEQLAGLEDCPE 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1573 E------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANE--ALRLRLQAEEVAQQksLAQADAE 1638
Cdd:COG3096 733 DlyliegdpdsfdDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGR---AAREkrLEELRAERDELAEQ--YAKASFD 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1639 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegtaqQRLAAEQELIRLRAETEQGEQQRQLLEEE---LARLQ 1715
Cdd:COG3096 808 VQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQ-------RRSELERELAQHRAQEQQLRQQLDQLKEQlqlLNKLL 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1716 HEATA-----ATQKRQELEAELAKvraemevllaskarAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEEA 1788
Cdd:COG3096 881 PQANLladetLADRLEELREELDA--------------AQEAQAFIQQHGKAlaQLEPLVAVLQSDPEQFEQLQADYLQA 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1789 KRQRQlaeedAARQRAEAERVLTEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRRLEEQAALHKAD 1865
Cdd:COG3096 947 KEQQR-----RLKQQIFALSEVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQ 1016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1866 IEERLAQLRKASESELErqkglvedtlrQRRQVEEEIMALKVSF-----EKAAAGKAELELELGRIRS--NAEDTMRSKE 1938
Cdd:COG3096 1017 YNQVLASLKSSRDAKQQ-----------TLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSrrSQLEKQLTRC 1085
|
890
....*....|
gi 256418964 1939 QAELEAARQR 1948
Cdd:COG3096 1086 EAEMDSLQKR 1095
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1618-2026 |
2.12e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1618 RLRLQAEEVAQQ-KSLAQADAEKQKEEAEREARRRGKAE------EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL 1690
Cdd:COG4913 239 RAHEALEDAREQiELLEPIRELAERYAAARERLAELEYLraalrlWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1691 IRLRAETEQGEQQRQLLE-EELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1769
Cdd:COG4913 319 DALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1770 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV---LTEKLAAISEATRLKTEA------EIALKEKEAE--- 1837
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAElpfvgeLIEVRPEEERwrg 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1838 -------NERLRRLAEDEAFQ-------RRRLEEQAALHKADIEERLAQLRKAS-------------------ESELERQ 1884
Cdd:COG4913 479 aiervlgGFALTLLVPPEHYAaalrwvnRLHLRGRLVYERVRTGLPDPERPRLDpdslagkldfkphpfrawlEAELGRR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1885 KGLV----EDTLRQ-RRQVEEEIM--ALKVSFEK---------------AAAGKAELELELGRIRSNAEDTmrskeQAEL 1942
Cdd:COG4913 559 FDYVcvdsPEELRRhPRAITRAGQvkGNGTRHEKddrrrirsryvlgfdNRAKLAALEAELAELEEELAEA-----EERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1943 EAAR------QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALE----EVERLKAKVEEARRLRERAEQESARQLQ 2012
Cdd:COG4913 634 EALEaeldalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKG 713
|
490
....*....|....
gi 256418964 2013 LAQEAAQKRLQAEE 2026
Cdd:COG4913 714 EIGRLEKELEQAEE 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1409-1641 |
2.40e-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: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1409 QAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1488
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1489 EAELALRVKAEAEAAREKQR-ALQALDELRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1566
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1567 LERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQKSLAQADAEKQK 1641
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1353-1808 |
2.46e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 63.88 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1353 AHAQAKAQAELEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVV 1432
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1433 RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA 1512
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1513 LDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQ 1592
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1593 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1672
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1673 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1752
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1753 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1808
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAA 927
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1345-1566 |
3.48e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.13 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1345 EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEaavdaQQQKRSIQEELQhlRQSSEAEIQAKAQQVEAAERsrmr 1424
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-----LEKERLAAQEQK--KQAEEAAKQAALKQKQAEEA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1425 ieeeirvvrlQLETTERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEAELALRVKAEAEAA 1503
Cdd:PRK09510 138 ----------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1504 REKQRALQAldelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1566
Cdd:PRK09510 203 AEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1324-1905 |
3.49e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 63.72 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1324 RLAEQQRAEERERLAEVEAalekqRQLAEAHAQAKAQAELEA---QELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL 1400
Cdd:COG3899 674 RALEARGPEPLEERLFELA-----HHLNRAGERDRAARLLLRaarRALARGAYAEALRYLERALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1401 RQSSEAEIQAkaQQVEAAERSRmrieEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1480
Cdd:COG3899 749 LELAEALYLA--GRFEEAEALL----ERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAER 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1481 ESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAS 1559
Cdd:COG3899 823 LGDRRLEARALFNLgFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAA 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1560 FAEKTAQLERTLQEEH---VTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAD 1636
Cdd:COG3899 903 ALAAAAAAAALAAAELarlAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAA 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1637 AEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1716
Cdd:COG3899 983 AAAAAA-----------AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAA 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1717 EATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1796
Cdd:COG3899 1052 AAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARA 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1797 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA 1876
Cdd:COG3899 1132 AAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLA 1211
|
570 580
....*....|....*....|....*....
gi 256418964 1877 SESELERQKGLVEDTLRQRRQVEEEIMAL 1905
Cdd:COG3899 1212 LALLALEAAALLLLLLLAALALAAALLAL 1240
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
137-239 |
3.59e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.39 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 137 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 256418964 216 PEDVDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1307-2024 |
4.36e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1307 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDA 1386
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1387 QQQKRSIQEELQHLRQ---SSEAEIQA-KAQQVEAAERSRMRIEEEIRVVRLQLetteRQRGGA--------EGELQALR 1454
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1455 AR----AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEAELAlRVKAEAEAAREKQRALQAldelrlQAEEAERRLRQ 1529
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1530 AEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTL------------------QEEHVTVAQLREEAERRAQQ 1591
Cdd:pfam15921 311 QNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLvlanseltearterdqfsQESGNLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1592 QAEAERAREEAERELERWQLKANEALRLRLQAE----EVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAE 1666
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1667 QELEKQ--RQLAEGTAQQRL---AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAE---LAKVRAE 1738
Cdd:pfam15921 470 LESTKEmlRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1739 MEVL---LASKARAEEESRSTSEK-----------------SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1798
Cdd:pfam15921 550 CEALklqMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1799 AARQRAEAERVLTEKLAAISEatrLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLrKASE 1878
Cdd:pfam15921 630 LELEKVKLVNAGSERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL-KSAQ 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1879 SELERQKglveDTLRQRRQVEEEIMALKVSFEKA-AAGKAELELELGRIRSNAED-TMRSKEQAELEAARQRQLAAEEEQ 1956
Cdd:pfam15921 706 SELEQTR----NTLKSMEGSDGHAMKVAMGMQKQiTAKRGQIDALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTV 781
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1957 RRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVE--EARRLRERAEQESARqLQLAQEAAQKRLQA 2024
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaECQDIIQRQEQESVR-LKLQHTLDVKELQG 850
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1626-1860 |
4.48e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1626 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1705
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1706 LLEEELARLQHEAtaatqKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRAL 1784
Cdd:COG4942 94 ELRAELEAQKEEL-----AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1785 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1860
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
22-121 |
5.39e-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: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 22 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILH 121
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2149-2583 |
5.84e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2149 AEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELfSVRVQMEELGKLKARIEAENRA 2228
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2229 LI-LRDKDNTQRFLEEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2307
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2308 QQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRKQAE 2386
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2387 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqQEQILQETQAL 2466
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---IAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2467 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQElmASMEEARRRQREAEEGVRRKQE 2546
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE--EELEELEEELEELREELAELEA 460
|
410 420 430
....*....|....*....|....*....|....*..
gi 256418964 2547 ELQHLEQQRQQQEKLLAEEnqRLRERLQRLEEEHRAA 2583
Cdd:COG4717 461 ELEQLEEDGELAELLQELE--ELKAELRELAEEWAAL 495
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
132-234 |
6.33e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 132 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 210
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 256418964 211 TRLLDPEDVDVPQPDEKSIITYVS 234
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1077-1267 |
7.54e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 59.00 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1077 EEVLKTHEEQLKEAQaVPATLQELEATKASLKKLRAQAEAQQPVFNTLrdelrgaQEVGERLQQRHGERDVEVerwRERV 1156
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1157 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLSAWLQDAKRRQEQIQavPIANCQAAREQLRQEKALLEEIERH 1236
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 256418964 1237 GEKVEECQKFAKQYINAIKDYELQLITYKAQ 1267
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
141-236 |
8.39e-09 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.93 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 141 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 196
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 256418964 197 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 236
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1022-1568 |
9.57e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1022 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEaqaVPATLQELE 1101
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1102 ATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLqqrhgerdveverwrERVTQLLERWQAVLAQTDVRQRELEQLG 1181
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---------------SRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1182 RQLRYYRESADPLSAW---LQDAKRRQEQIqavpiancqaarEQLRQEKALL--EEIERHGEKVEECQKFAKQYINAIKD 1256
Cdd:PRK03918 345 KKLKELEKRLEELEERhelYEEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1257 YELQLITYKAQLEPVASPAKKPKVQS---GSESVIQEYVDLRTRYSElttltsqYIKFISETLRRMEEEERlaeqqraEE 1333
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1334 RERLAEVEAALEKQRQLAEAHAQAKAQAELEaQELQRRMQEEVARREEAAvdaqqqkRSIQEELQHLrqssEAEIQAKAQ 1413
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEY-------EKLKEKLIKL----KGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1414 QVEAAERsrmrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1493
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1494 lRVKAEAEAAREK-QRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1568
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1317-1524 |
9.74e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERErlaEVEAALEKQRQLaeahaqakAQAELEAQElQRRMQEEVARREeaavdAQQQKrsiQEE 1396
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQ---KQAAEQERLKQL--------EKERLAAQE-QKKQAEEAAKQA-----ALKQK---QAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1397 LQHLRQSSEAEIQAKAQQVEAAERSRmRIEEEIRvVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrr 1476
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK--- 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 256418964 1477 qVQDESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELRLQAEEAE 1524
Cdd:PRK09510 211 -AAAEAKKKAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1310-1552 |
1.23e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.32 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1310 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQ 1389
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1390 KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEGELQALRARAEEaEAQKRQAQE 1469
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREEAEKKARQ-RQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1470 EAERLRRQVQDESQRKRQAEAELALRVKAEAE------AAREKQRALQALDELRLQAEEAER-RLRQAEAERARQVQVAL 1542
Cdd:pfam13868 243 EQIELKERRLAEEAEREEEEFERMLRKQAEDEeieqeeAEKRRMKRLEHRRELEKQIEEREEqRAAEREEELEEGERLRE 322
|
250
....*....|
gi 256418964 1543 ETAQRSAEVE 1552
Cdd:pfam13868 323 EEAERRERIE 332
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1317-1550 |
1.27e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.32 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKrsIQEE 1396
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER--IQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1397 LQHLRQSSEAEIQAKAQQVEAAERSRMRI---------EEEIRVVRLQLETTERQRggAEGELQALRARAEEAEAQKRQA 1467
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1468 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQR 1547
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
...
gi 256418964 1548 SAE 1550
Cdd:pfam13868 272 EDE 274
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1136-1443 |
1.48e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1136 ERLQQRHGERDVEVERWR-----ERVTQL-LERWQAVLAQTD----VRQRELEQLGrqlryyresadplsawLQDAKRRQ 1205
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRkleeaEKARQAeMDRQAAIYAEQErmamERERELERIR----------------QEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1206 EQIQAVPIAncqAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVaspakKPKVQSGSE 1285
Cdd:pfam17380 363 ERIRQEEIA---MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI-----RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1286 SVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEA 1365
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEE 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1366 QELQRRMQEEVARREEAAvdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQR 1443
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKATeERSRLEAMEREREMMRQIVESEKAR 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1808-2546 |
1.56e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1808 RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaalhKADIEERLAQLRKASESELERQKGL 1887
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1888 VEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAED-TMRSKEQAELEAARQRQLAAEEEQRRREAEERVQ 1966
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1967 RSLAAEEEAARQRKVALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFVVqqre 2037
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETR---- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2038 eelqqtlqqeqnmlDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAaeklrkea 2117
Cdd:TIGR02169 385 --------------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE-------- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2118 eqeaarraqaeqaalkqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAE---VTEA 2194
Cdd:TIGR02169 443 -----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2195 ARQRSQVEEELFS----VRVQMEELGKLKAR------IEAENR--ALILRDKDNTQR---FLEEEA---------EKMKQ 2250
Cdd:TIGR02169 506 VRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2251 VAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAEA 2304
Cdd:TIGR02169 586 ERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2305 ELLQQQKElaqEQARRLQEDKEQMAQQLveetQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2384
Cdd:TIGR02169 666 ILFSRSEP---AELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2385 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELER-----------------EKEKLKQEAKLLQLK 2447
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqaelsklEEEVSRIEARLREIE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2448 SEEMQTVQQEQILQ-ETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQELMAS 2526
Cdd:TIGR02169 819 QKLNRLTLEKEYLEkEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
810 820
....*....|....*....|
gi 256418964 2527 MEEARRRQREAEEGVRRKQE 2546
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRK 917
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1395-1769 |
1.57e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 60.68 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1395 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1474
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1475 RRQVQDESQRKRQAEAELALRVKA-EAEAAREKQRALQA---LDELRLQAEEAERRLRQAEAERaRQVQVALETAQ---R 1547
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLEReteLERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1548 SAEVELQSKRASFAEKTAQLERtLQEehvTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1627
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-LQD---TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1628 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1707
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 1708 EEELARlqhEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1769
Cdd:pfam07888 345 EVELGR---EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2139-2600 |
1.73e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.14 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2139 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSVRVQMEELGKL 2218
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2219 KARIEAENRALILRDKDNTqrfLEEEAEKMKQVAEEAARLSVAAQEAARLR----------QLAEEDLAQQRALAEKMLK 2288
Cdd:TIGR00618 276 EAVLEETQERINRARKAAP---LAAHIKAVTQIEQQAQRIHTELQSKMRSRakllmkraahVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2289 EKMQAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMS 2368
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK------ELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2369 RAQARAEEDAQRFRKQAEEigekLHRTELATQEKVTLVQTLEIQrQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKS 2448
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2449 EEMQTVQqEQILQETQALQKSFLSEKDS-----LLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQEL 2523
Cdd:TIGR00618 501 EEPCPLC-GSCIHPNPARQDIDNPGPLTrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 2524 MASMEEArrrqreaeEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKAL 2600
Cdd:TIGR00618 580 NRSKEDI--------PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1331-1551 |
1.77e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 60.27 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1331 AEERERLAEVEAALEKQRQLAEAHAQ-AKAQAELEAQELQRRMQEEVARREEAAvdAQQQKRSIQEELQhlRQSSEAEIQ 1409
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIAE--AEAELAKKKAEER--REAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1410 AKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggaegelqalraRAEEAEAQKRQAQEEAERlrrqvqdesqrkrqae 1489
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREI-----------------ELQEKEAEREEAELEADV---------------- 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1490 aelalRVKAEAEAAREKQRALQALDELRLQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1551
Cdd:COG2268 311 -----RKPAEAEKQAAEAEAEAEAEAIRAKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
132-239 |
1.93e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.10 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 132 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 210
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 256418964 211 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1326-2115 |
2.07e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.96 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1326 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ-HLRQSS 1404
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTeQLEQAK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1405 EAEIQ-AKAQQVEAAERSRMriEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ 1483
Cdd:pfam01576 370 RNKANlEKAKQALESENAEL--QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1484 RKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEVELQSKRASFA 1561
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1562 EktaqLERTLQEEHVTVAQLREEaerraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKslaqadAEKQK 1641
Cdd:pfam01576 528 D----MKKKLEEDAGTLEALEEG----------------------KKRLQRELEALTQQLEEKAAAYDK------LEKTK 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1642 EEAEREARRRGKAEEQavrQRELAEQELEKQRQLAEGTAQQRLAAEQELI-RLRAETEQGEQQRQLLEeelarLQHEATA 1720
Cdd:pfam01576 576 NRLQQELDDLLVDLDH---QRQLVSNLEKKQKKFDQMLAEEKAISARYAEeRDRAEAEAREKETRALS-----LARALEE 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1721 ATQKRQELEAELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAGRFRELAEEA---------ARLR------ALA 1785
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELedelqatedAKLRlevnmqALK 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1786 EEAKRQRQLAEEDA-------ARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1858
Cdd:pfam01576 727 AQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1859 AALHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEIMALKVSFEKAAAGKAELELEL- 1923
Cdd:pfam01576 807 MKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERDELADEIASGASGKSALQDEKr 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1924 ---GRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREaeervqrsLAAEEEAARQRKVALEEVER----LKAKVEEA 1996
Cdd:pfam01576 886 rleARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTE--------LAAERSTSQKSESARQQLERqnkeLKAKLQEM 957
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1997 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQae 2076
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL-- 1035
|
810 820 830
....*....|....*....|....*....|....*....
gi 256418964 2077 reaaqsRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRK 2115
Cdd:pfam01576 1036 ------KRQLEEAEEEAS----------RANAARRKLQR 1058
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1334-1803 |
2.17e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1334 RERLAEVEAALEKQRQLAEAHAQAKAQAEleaQELQRRMQEEVARREEAAVDaqqqkrSIQEELQHLRQSSEAEIqakAQ 1413
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAA---AELRGPDQLAWLARLDAEHD------NLRAALRWALAHGDAEL---AL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1414 QVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1493
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1494 LRvkAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1573
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1574 EHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGK 1653
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1654 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1733
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1734 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1803
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
24-118 |
2.79e-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: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 24 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 95
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 256418964 96 VNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1471-1927 |
3.12e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.42 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1471 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1550
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1551 VELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1630
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1631 SLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1710
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1711 LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1790
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1791 QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERL 1870
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1871 AQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIR 1927
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1123-1915 |
3.57e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 60.35 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1123 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQREleQLGRqlryYRESADPLSAw 1197
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTE- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1198 lqdakRRQEQIQAVPIANCQAAREQLRQEKALlEEIERHG-------EKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1269
Cdd:COG3096 362 -----RLEEQEEVVEEAAEQLAEAEARLEAAE-EEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1270 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEER-ERLAEVEAALEK- 1346
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELlRRYRSQQALAQRl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1347 ---QRQLAEAHAQAKAQAELE--AQELQRRmqeevarreeaavdaQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERS 1421
Cdd:COG3096 515 qqlRAQLAELEQRLRQQQNAErlLEEFCQR---------------IGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1422 RMrieeeirvvrlqleTTERQRGGAEGELQALRARAEEAeaqkRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1501
Cdd:COG3096 580 RS--------------ELRQQLEQLRARIKELAARAPAW----LAAQDALERLREQSGEALADSQEVTAAMQQLLERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1502 AAREKQRALQALDELRLQAeeaeRRLRQAE-AERARQVQ----------------VALETA---------QRSAEVELQS 1555
Cdd:COG3096 642 ATVERDELAARKQALESQI----ERLSQPGgAEDPRLLAlaerlggvllseiyddVTLEDApyfsalygpARHAIVVPDL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1556 KRAsfAEKTAQLERTLQE------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANE--ALRLRL 1621
Cdd:COG3096 718 SAV--KEQLAGLEDCPEDlyliegdpdsfdDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGR---AAREkrLEELRA 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1622 QAEEVAQQksLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGE 1701
Cdd:COG3096 793 ERDELAEQ--YAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALR-------QRRSELERELAQHRAQEQQLR 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1702 QQRQLLEEE---LARLQHEATA-----ATQKRQELEAELAKVR-AEMEVLLASKARAE-EESRSTSEKSKQRLEAEAGRF 1771
Cdd:COG3096 864 QQLDQLKEQlqlLNKLLPQANLladetLADRLEELREELDAAQeAQAFIQQHGKALAQlEPLVAVLQSDPEQFEQLQADY 943
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1772 RELAEEAARLR----ALAEEAKRQRQLAEEDAARQRAEAeRVLTEKL-AAISEATRLKTEAEIALKEKEAE-NERLRRLA 1845
Cdd:COG3096 944 LQAKEQQRRLKqqifALSEVVQRRPHFSYEDAVGLLGEN-SDLNEKLrARLEQAEEARREAREQLRQAQAQySQYNQVLA 1022
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1846 E-DEAFQRRR--------------------LEEQAALHKADIEERLAQLRkASESELERQKGLVE---DTLRQR-RQVEE 1900
Cdd:COG3096 1023 SlKSSRDAKQqtlqeleqeleelgvqadaeAEERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSLQKRlRKAER 1101
|
890
....*....|....*
gi 256418964 1901 EIMALKVSFEKAAAG 1915
Cdd:COG3096 1102 DYKQEREQVVQAKAG 1116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1751-2034 |
3.86e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1751 EESRSTSEKSKQ----RLEAEagRFRELAEEAARlralaeEAKRQRQLAEEDAARQrAEAERvlteKLAAISEATRLKTE 1826
Cdd:pfam17380 279 QHQKAVSERQQQekfeKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1827 AE-----IALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQ----LRKASESELERQKGLVEDT--LRQR 1895
Cdd:pfam17380 346 RErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeleaARKVKILEEERQRKIQQQKveMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1896 RQVEEEIMALKV---------SFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQ 1966
Cdd:pfam17380 426 RAEQEEARQREVrrleeerarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1967 RSLAAEEeaaRQRKVALEEVE-RLKAKVEEARR------LRERAEQESARQLQLAQEAA---QKRLQAEEKAHAFVVQ 2034
Cdd:pfam17380 506 QAMIEEE---RKRKLLEKEMEeRQKAIYEEERRreaeeeRRKQQEMEERRRIQEQMRKAteeRSRLEAMEREREMMRQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2249-2469 |
3.87e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2249 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2324
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2325 KEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2404
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2405 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKS 2469
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1663-2577 |
4.03e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.19 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1663 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeME 1740
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1741 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervLTEKLAAISEA 1820
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1821 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaalhKADIEErlaqlrkasesELERQKGLVEDTLRQRRQVEE 1900
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ----RRDLGE-----------ELEALKTELEDTLDTTAAQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1901 EimalkvsfekaaagKAELELELGRIRSNAEDTMRSKEqAELEAARQRQLaaeeeqrrreaeervqrslAAEEEAARQrk 1980
Cdd:pfam01576 321 L--------------RSKREQEVTELKKALEEETRSHE-AQLQEMRQKHT-------------------QALEELTEQ-- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1981 vaLEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLDRLRSEA 2058
Cdd:pfam01576 365 --LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLqeLQARLSESERQRAELAEKLSKLQSEL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2059 EAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAA 2138
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2139 DAEMEKHKKFAEQTL-------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA----RQRSQVEeelfs 2207
Cdd:pfam01576 523 QAQLSDMKKKLEEDAgtlealeEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldHQRQLVS----- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2208 vrvQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKmkqvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2287
Cdd:pfam01576 598 ---NLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK----ETRALSLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2288 --------------KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQL-- 2351
Cdd:pfam01576 671 sskddvgknvheleRSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2352 ---EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIA 2428
Cdd:pfam01576 750 qvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQ 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2429 ELEREKEKLKQEAKLLQLKSE----EMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEvakakq 2504
Cdd:pfam01576 828 SKESEKKLKNLEAELLQLQEDlaasERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEE------ 901
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2505 lreeqqrqqqqmeqekqelMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAE---ENQRLRERLQRLE 2577
Cdd:pfam01576 902 -------------------QSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQlerQNKELKAKLQEME 958
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1314-1536 |
4.47e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQkr 1391
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1392 siqEELQHlrqssEAEIQAKAQQVEAAERSRmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEE- 1470
Cdd:TIGR02794 146 ---EEAAK-----QAEEEAKAKAAAEAKKKA-----------------------EEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1471 ---AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERAR 1536
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1658-2030 |
4.59e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.97 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1658 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEATAATQK----RQ 1726
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1727 ELEAELAKVRAEMEVLLA---SKARAEEESRSTSEKSK----------QRLEAE---AGRFR------ELAEEAARLRAL 1784
Cdd:COG3096 355 DLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEVDslksqladyqQALDVQqtrAIQYQqavqalEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1785 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERlrrlaeDEAFQR-RRLEEQAALHK 1863
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER------SQAWQTaRELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1864 AdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1943
Cdd:COG3096 509 A-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1944 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQ 2023
Cdd:COG3096 580 RSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
....*..
gi 256418964 2024 AEEKAHA 2030
Cdd:COG3096 660 IERLSQP 666
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1745-2028 |
6.67e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 59.19 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1745 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAarqRAEAERVLTEKLAAISEATRL 1823
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDA---VAAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1824 KTEAEIALKEKEAEnERLRRLAEDEAFQRRRLEEQAALHKADIEERL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1901
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1902 ImalkvsfEKAAAGKAELelelgrirsnAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV 1981
Cdd:PRK05035 586 I-------ARAKAKKAAQ----------QAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 256418964 1982 ALeEVERLKAKVEEARRLRERAEQESARQLQlAQEAAQKRLQAEEKA 2028
Cdd:PRK05035 649 AA-AIARAKARKAAQQQANAEPEEAEDPKKA-AVAAAIARAKAKKAA 693
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1317-1578 |
6.98e-08 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 58.12 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQ 1394
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1395 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrlqletterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1474
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1475 RRQVQDESQR-KRQA-EAELALRVKAEAEAARE--KQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1550
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 256418964 1551 VELQSKRASFAEKTAQLERTLQEEHVTV 1578
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1684-2579 |
7.09e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.03 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1684 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEKskqR 1763
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELES---R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1764 LEAEAGRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLTE-KLAAISEATRLKTEAEIAL-KEKEAENERL 1841
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1842 RRLA------EDEAFQRRRLEEQAALHKADIEERLAQLRK-------------ASESELERQ----KGLVEDTLRQRRQV 1898
Cdd:pfam01576 162 SEFTsnlaeeEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqelekakrkleGESTDLQEQiaelQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1899 EEEIMALKVSFEKAAAGKAELE---LELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 1975
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1976 ARQRKvalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLR 2055
Cdd:pfam01576 322 RSKRE---QEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2056 SEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeqeaarraqaeqaalKQK 2135
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS---------------KDV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2136 QAADAEMEKHKKFAEQTLRQK-------AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQrsqVEEELFSV 2208
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDAGTL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2209 RvQMEElGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQvaeEAARLSVAAQeaaRLRQLAEEDLAQQRALAEKMLK 2288
Cdd:pfam01576 541 E-ALEE-GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ---ELDDLLVDLD---HQRQLVSNLEKKQKKFDQMLAE 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2289 EKMQAVQEA-TRLKAEAELLQQQKElAQEQARRLQEdkeqmAQQLVEETQGFQRTLEAERQrqlEMSAEAERLKLRMAEM 2367
Cdd:pfam01576 613 EKAISARYAeERDRAEAEAREKETR-ALSLARALEE-----ALEAKEELERTNKQLRAEME---DLVSSKDDVGKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2368 SRAQARAEEDAQRFRKQAEEIGEKLHRTELAtqeKVTLVQTLEIQRQQSDHD---------------AERLREAIAELER 2432
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQFERDlqardeqgeekrrqlVKQVRELEAELED 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2433 EKE--------KLKQEAKLLQLKSE-EMQTVQQEQILQETQALQKSFlseKDslLQRErfIEQEKAKLEQLFqdevAKAK 2503
Cdd:pfam01576 761 ERKqraqavaaKKKLELDLKELEAQiDAANKGREEAVKQLKKLQAQM---KD--LQRE--LEEARASRDEIL----AQSK 829
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2504 QLREEQQRQQQQMEQEKQELMASmeEARRRQREAEegvrrkQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEE 2579
Cdd:pfam01576 830 ESEKKLKNLEAELLQLQEDLAAS--ERARRQAQQE------RDELADEIASGASGKSALQDEKRRLEARIAQLEEE 897
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
992-1576 |
7.28e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 992 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLE-------- 1061
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMAlrqqleql 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1062 -----KLKTISLVIRSTQGAEEVLKTH-EEQLKEAQAVPATLQELeatkasLKKLRAQAEAqqpvfntlRDELRGAQEV- 1134
Cdd:PRK04863 592 qariqRLAARAPAWLAAQDALARLREQsGEEFEDSQDVTEYMQQL------LERERELTVE--------RDELAARKQAl 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1135 ---GERLQQRHGERDveverwrERVTQLLERWQAVLAQTDVRQRELEQLGrqlrYYresadplSAWLQDAKrrqeqiQAV 1211
Cdd:PRK04863 658 deeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YF-------SALYGPAR------HAI 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1212 PIANCQAAREQLRQEKALLEEI-------ERHGEKVEECQKFAKQYINAIKDYELQLITYKAqlEPVASPAKKPK----V 1280
Cdd:PRK04863 714 VVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqL 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1281 QSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ 1360
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1361 AELEAQELQRRM------------------QEEVARREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE- 1419
Cdd:PRK04863 870 AKEGLSALNRLLprlnlladetladrveeiREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQq 949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1420 ---RSRMRIE--EEIRVVRLQLETTERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEAEL 1492
Cdd:PRK04863 950 tqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1493 alrvKAEAEAAREK-QRALQALDELRLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAE 1562
Cdd:PRK04863 1026 ----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLE 1101
|
650
....*....|....
gi 256418964 1563 KTAQLERTLQEEHV 1576
Cdd:PRK04863 1102 RDYHEMREQVVNAK 1115
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1695-2257 |
8.19e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1695 AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAGRFR 1772
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1773 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-LTEKLAAIS-EATRLKTEA---EIALKEKEAENERLRRLAE 1846
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeYLDELREIEkRLSRLEEEIngiEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1847 DEAFQRRRLEEQAALHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEImalkvsfEKAAAGKAELE 1920
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEI-------SKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1921 LELGRIRSNAEdtmrskeqaELEAARQ------RQLAAEEEQRRREAEERVQRSLAAE----EEAARQRKVALEEVERLK 1990
Cdd:PRK03918 419 KEIKELKKAIE---------ELKKAKGkcpvcgRELTEEHRKELLEEYTAELKRIEKElkeiEEKERKLRKELRELEKVL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1991 AKVEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAFvvqqreeelqqtlQQEQNMLDRLRSEAEAARRAAEEAEE 2070
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEY-------------EKLKEKLIKLKGEIKSLKKELEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2071 AREQAEREAAQSRKQVEE-AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFA 2149
Cdd:PRK03918 554 LKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2150 EQTLRQKA--QVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARI 2222
Cdd:PRK03918 634 ELAETEKRleELRKELEELEKKYSEEEYEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
570 580 590
....*....|....*....|....*....|....*
gi 256418964 2223 EAENRALilrdkdntqRFLEEEAEKMKQVAEEAAR 2257
Cdd:PRK03918 714 EKLEKAL---------ERVEELREKVKKYKALLKE 739
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1719-1872 |
8.87e-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: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1719 TAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRAlaEEAKRQRQLAEED 1798
Cdd:COG2268 212 TEIAIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1799 AARQR------AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAALHKADIEERLAQ 1872
Cdd:COG2268 286 AEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG-KRALAEAWNKLGDAAILLMLIE 364
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1528-2446 |
8.98e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.83 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1528 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREeaerelE 1607
Cdd:TIGR00618 56 RRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSET------E 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1608 RWQLKAnealrLRLQAEEVAQQKSLAQADAEKqkeeaereaRRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAE 1687
Cdd:TIGR00618 130 EVIHDL-----LKLDYKTFTRVVLLPQGEFAQ---------FLKAKSKEKKELLMNL--FPLDQYTQLALMEFAKKKSLH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1688 QELIrlrAETEQGEQQRQLLEEELARLqheataaTQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK--QRLE 1765
Cdd:TIGR00618 194 GKAE---LLTLRSQLLTLCTPCMPDTY-------HERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqQLLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1766 AEAGRFRELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1845
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1846 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQR-RQVEEEIMALKVSFEKAAAGKAELELELG 1924
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1925 RIrsNAEDTMRSKEQAELEAAR-QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERA 2003
Cdd:TIGR00618 411 TI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2004 EQESARQLQLAQEaaQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAaqsr 2083
Cdd:TIGR00618 489 KAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK---- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2084 kqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKeaEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQEL 2163
Cdd:TIGR00618 563 ---EQMQEIQQSFSILTQCDNRSKEDIPNLQN--ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2164 TTlRLQLEETdhqkSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEE 2243
Cdd:TIGR00618 638 SQ-ELALKLT----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2244 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAELLQQQKELAQE---QAR 2319
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNeEVTAALQTGAELSHLAAEiqfFNR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2320 RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAraeedaqRFRKQAEEIGEKLHRTELAT 2399
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG-------EITHQLLKYEECSKQLAQLT 865
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 256418964 2400 QEKVTLVQTLE----IQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQL 2446
Cdd:TIGR00618 866 QEQAKIIQLSDklngINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4014-4050 |
9.88e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 9.88e-08
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 4014 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4050
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1041-1489 |
1.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1041 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEatkaslkKLRAQAEAQQPV 1120
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-------ALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1121 FNTLRDELRGAQEVGERLQqrhgERDVEVERWRERVTQLLERWQAVLAQTDVR-QRELEQLGRQLRYYRESADPLSAWLQ 1199
Cdd:COG4717 148 LEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1200 DAKRRQEQIQAVPIAncQAAREQLRQEK----------ALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLE 1269
Cdd:COG4717 224 ELEEELEQLENELEA--AALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1270 PVASPAKKPKVQSGSESviQEYVDLRTRYSELTTLTSQYIkfisETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ 1349
Cdd:COG4717 302 KEAEELQALPALEELEE--EELEELLAALGLPPDLSPEEL----LELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1350 LAEAHAQAKAQAELEAQELQRRmQEEVARREEAAVDAQQQKRSIQEELQHLRQSS-EAEIQAKAQQVEAAERSRMRIEEE 1428
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREE 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1429 IRVVRLQLETTERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAE 1489
Cdd:COG4717 455 LAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
940-1576 |
1.18e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.43 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 940 YQQLLQSLEQGEQeesrcqrcISELKDirLQLEACETR-TVHRLRLPLDKDPARECAQRIAEQQKAQAEVEGLGKGVARL 1018
Cdd:COG3096 415 YQQAVQALEKARA--------LCGLPD--LTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1019 SAEAEKVLALPEpspAAPTLR--SELELTLGKLEQVRSlsaiyleKLKTISLVIRSTQGAEEVL----KTHEEQLKEAQA 1092
Cdd:COG3096 485 AGEVERSQAWQT---ARELLRryRSQQALAQRLQQLRA-------QLAELEQRLRQQQNAERLLeefcQRIGQQLDAAEE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1093 VPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRG--------------AQEVGERLQQRHGERDVEVERWRERVTQ 1158
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRArikelaarapawlaAQDALERLREQSGEALADSQEVTAAMQQ 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1159 LLERWQAVLAQTD---VRQRELEQLGRQLRYYRESADP-------------LS-----AWLQDA----KRRQEQIQAVPI 1213
Cdd:COG3096 635 LLEREREATVERDelaARKQALESQIERLSQPGGAEDPrllalaerlggvlLSeiyddVTLEDApyfsALYGPARHAIVV 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1214 ANCQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKKPKVQS 1282
Cdd:COG3096 715 PDLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRLEELRA 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1283 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAE 1362
Cdd:COG3096 793 ERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQL 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1363 LEAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEE 1428
Cdd:COG3096 870 KEQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQ 949
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1429 IRVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkRQAEAELA 1493
Cdd:COG3096 950 QRRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ--VLASLKSS 1027
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1494 LRVKAE--AEAARE-KQRALQALDELRLQAEEAERRLRQA-EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1569
Cdd:COG3096 1028 RDAKQQtlQELEQElEELGVQADAEAEERARIRRDELHEElSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
....*..
gi 256418964 1570 TLQEEHV 1576
Cdd:COG3096 1108 EQVVQAK 1114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1501-1948 |
1.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1501 EAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaq 1580
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1581 lreeaerraqqqaeaerareeaereLERW-QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRgKAEEQAV 1659
Cdd:COG4717 145 -------------------------PERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-EELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1660 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEM 1739
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1740 EVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISE 1819
Cdd:COG4717 279 LFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1820 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALH--KADIEERLAQLRKASESELERQKGLVEDTLRQR-R 1896
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQelKEELEELEEQLEELLGELEELLEALDEEELEEElE 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1897 QVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQR 1948
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1622-1805 |
1.38e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1622 QAEEVAQQKslaQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1697
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1698 EQGEQQRQLLEEELARLQHEATAatqkRQELEAElAKVRAEMEvllaSKARAEEESRSTSEK-SKQRLEAEAGRFRELAE 1776
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEA----KKKAEAE-AAAKAAAE----AKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*....
gi 256418964 1777 EAArlRALAEEAKRQRQLAEEDAARQRAE 1805
Cdd:PRK09510 232 AEA--KAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1205-1776 |
1.41e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1205 QEQIQAVPIANCQAAREQL-----RQEKALLEEIERHGEKVEECQKFAKQYINAIKdyelQLITYKAQLEPVASPAKKPK 1279
Cdd:COG4717 40 LAFIRAMLLERLEKEADELfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1280 VQSGSESVIQEYVDLRTRYSELTtltsqyikfisETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKA 1359
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALE-----------AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1360 QAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEE--EIRVV 1432
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqlENELEAAALEERLKEARLLLLIAAAllALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1433 RLQLETTERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQR 1508
Cdd:COG4717 265 GGSLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1509 ALQALDELRLQAEEAERRLRQAEAERARqvQVALETAQRSAEVELQSKRASFAEKTAQLERtlqeehvtvaqlreeaerr 1588
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEI--AALLAEAGVEDEEELRAALEQAEEYQELKEE------------------- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1589 aqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearrrgKAEEQAVRQRELAEQE 1668
Cdd:COG4717 404 -------------------------LEELEEQLEELLGELEELLEALDEEELEE----------ELEELEEELEELEEEL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1669 LEKQRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAE-LAKVRAEMEVLLASK 1746
Cdd:COG4717 449 EELREELAELEAElEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREErLPPVLERASEYFSRL 528
|
570 580 590
....*....|....*....|....*....|
gi 256418964 1747 ARAEEESRSTSEKSKQRLEAEAGRFRELAE 1776
Cdd:COG4717 529 TDGRYRLIRIDEDLSLKVDTEDGRTRPVEE 558
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1686-1886 |
1.55e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1686 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1765
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1766 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA 1827
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1828 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKG 1886
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1622-1808 |
1.67e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.78 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1622 QAEEVAQQKSlAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1701
Cdd:TIGR02794 51 QANRIQQQKK-PAAKKEQERQK---------KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1702 QQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EA 1778
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEA 200
|
170 180 190
....*....|....*....|....*....|
gi 256418964 1779 ARLRALAEEAKRQRQLAeedAARQRAEAER 1808
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
17-124 |
2.32e-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: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 89
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 256418964 90 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2182-2450 |
2.44e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2182 EELQRLKAEVTEAARQRSQVE------EELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEA 2255
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2256 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2335
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2336 TQGFQRTLEAERQRQLEMSAEAERLklrmaemSRAQARAEEDAQRFRKQAEEIgeklhRTELAtqekvtlvqtlEIQRQQ 2415
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEAL-------EEALAEAEAALRDLRRELREL-----EAEIA-----------SLERRK 435
|
250 260 270
....*....|....*....|....*....|....*...
gi 256418964 2416 SDHDAE--RLREAIAE-LEREKEKLKQEAKLLQLKSEE 2450
Cdd:COG4913 436 SNIPARllALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1986-2661 |
2.72e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1986 VERLKAKVEEARRLRERAEQESARQLQLA----QEAAQKRLQAEEKAHAfvVQQREEELQQTLQQEQNMLDRLRSEAEAA 2061
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2062 RRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE 2141
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2142 MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEE--LGKLK 2219
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaeLKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2220 ARIEAENRAlilrdkdntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEkMLKEKMQAVQEATR 2299
Cdd:TIGR02168 440 AELEELEEE------------LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2300 lkAEAELLQQQKELAQEQARrlqedkeqmAQQLVEETQGFQRTLEA---ERQRQLEMS------------AEAERLKLRM 2364
Cdd:TIGR02168 507 --GVKALLKNQSGLSGILGV---------LSELISVDEGYEAAIEAalgGRLQAVVVEnlnaakkaiaflKQNELGRVTF 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2365 AEMSRAQARAEEDAQRFRKQAEE--IGEKLHRTELATQEKVTL---------VQTLEI---QRQQSDHDA---------- 2420
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPKLRKALsyllggvlvVDDLDNaleLAKKLRPGYrivtldgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2421 ------------------------ERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDS 2476
Cdd:TIGR02168 656 rpggvitggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2477 LLQRERFIEQEKAKLEQL-------------FQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRR 2543
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLskelteleaeieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2544 KQEELQHLEQQRQQQEKLLAEENQRLRERLQRLE--EEHRAALAHS-----EIATTQAASTKALPNGRDAPDGPSVEAEP 2616
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEelSEDIESLAAEieeleELIEELESELEALLNERASLEEALALLRS 894
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 256418964 2617 EYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTVAELTQRED 2661
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1348-1560 |
2.95e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1348 RQLAEAHAQAKAQAELEAQELQRRMQEEVARR--EEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAER 1420
Cdd:COG3206 147 PELAAAVANALAEAYLEQNLELRREEARKALEflEEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1421 SRMRIEEEIRVVRLQLETTERQRGGAEGE---------LQALRARAEEAEAQKRQAQE-------EAERLRRQVQDESQR 1484
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1485 KRQAEAELALRVKAEAEAAREKQRALQA-LDELRLQAE---EAERRLR--QAEAERARQVQVALETAQRSAEVELQSKRA 1558
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAqLAQLEARLAelpELEAELRrlEREVEVARELYESLLQRLEEARLAEALTVG 386
|
..
gi 256418964 1559 SF 1560
Cdd:COG3206 387 NV 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1309-1549 |
3.06e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1309 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQ 1388
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1389 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAE----EAEAQK 1464
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1465 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALET 1544
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*
gi 256418964 1545 AQRSA 1549
Cdd:COG3883 258 AAGSA 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1327-1730 |
3.14e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1327 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRM------------------QEEVARREEAAVDAQQ 1388
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLprlnlladetladrveeiREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1389 QKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE----RSRMRIE--EEIRVVRLQLETTERQR-GGAEGELQ-ALRARAE 1458
Cdd:PRK04863 916 HGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1459 EAEAQKRQAQEEAerlrRQVQDESQRKRQAEAELalrvKAEAEAAREK-QRALQALDELRLQA-EEAERRLRQAEAE--- 1533
Cdd:PRK04863 996 QAEQERTRAREQL----RQAQAQLAQYNQVLASL----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElha 1067
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1534 ---RARQVQVALETAQRSAEVELQS--KRASFAEKTAQLERTLQEEHVT--VAQLREEAERRAQQQAEAERAREEAEREL 1606
Cdd:PRK04863 1068 rlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKDNGVERRLHRRELAYLSADEL 1147
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1607 ERWQLKANEALRLrlqaeevaqqkslAQADAEKqkEEAEREARRRGKAEEQAVRQRELAEQEL-EKQRQLAEGTAQQRLA 1685
Cdd:PRK04863 1148 RSMSDKALGALRL-------------AVADNEH--LRDVLRLSEDPKRPERKVQFYIAVYQHLrERIRQDIIRTDDPVEA 1212
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1686 AEQ---ELIRLRAETEQGEQQRQLLEEELA-----RLQHEATAATQKRQELEA 1730
Cdd:PRK04863 1213 IEQmeiELSRLTEELTSREQKLAISSESVAniirkTIQREQNRIRMLNQGLQN 1265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1727-2578 |
3.41e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1727 ELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRleaeaGRFRELAEEAARLRALAEEaKRQRQLAEEDAARQRAEA 1806
Cdd:TIGR02169 167 EFDRKKEKALEELEEV---EENIERLDLIIDEKRQQL-----ERLRREREKAERYQALLKE-KREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1807 ERVLTEKlaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHkadIEERLAQLrkasESELERQKG 1886
Cdd:TIGR02169 238 QKEAIER--QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR---VKEKIGEL----EAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1887 LVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNaedtmRSKEQAELEAARQRqlaaeeEQRRREAEERVQ 1966
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR-----RDKLTEEYAELKEE------LEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1967 RSLAAEEEAARQRKVALEEVERLKAKVE-EARRLRERAEQESARQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTL 2044
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKrELDRLQEELQRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2045 QQEQNMLDRLRSEAEAARRAAEEAEEAREqaereaaQSRKQVEEAERLKQSAEEQAQAQAqaqaaaeklrkeaeqeaarr 2124
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELS-------KLQRELAEAEAQARASEERVRGGR-------------------- 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2125 aqaeqaalkqkqAADAEMEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-EVT 2192
Cdd:TIGR02169 511 ------------AVEEVLKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgRAT 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2193 EAARQRSQVEEELFSVRVQMEELGKLKARIEAENR-----ALILRDKDNTQRfLEEEAEKMKQV---------------- 2251
Cdd:TIGR02169 577 FLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTLVVED-IEAARRLMGKYrmvtlegelfeksgam 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2252 ----AEEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2318
Cdd:TIGR02169 656 tggsRAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2319 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELA 2398
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEAR 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2399 TQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMqtvqqEQILQETQALQKSfLSEKDSLL 2478
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-----EEELEELEAALRD-LESRLGDL 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2479 QRERfiEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEqekqelmASMEEARRRQREAEEGVRRKQEElqhleQQRQQQ 2558
Cdd:TIGR02169 888 KKER--DELEAQLREL-ERKIEELEAQIEKKRKRLSELK-------AKLEALEEELSEIEDPKGEDEEI-----PEEELS 952
|
890 900
....*....|....*....|
gi 256418964 2559 EKLLAEENQRLRERLQRLEE 2578
Cdd:TIGR02169 953 LEDVQAELQRVEEEIRALEP 972
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1406-1543 |
3.54e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.44 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1406 AEIQAKAQQVEAAersrmrieeeIRVVRLQLETTERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE--SQ 1483
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGavSQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1484 RKRQaEAELALRV-KAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERArQVQVALE 1543
Cdd:COG1566 148 QELD-EARAALDAaQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1049-1495 |
3.92e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1049 LEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEaqaVPATLQE----LEATKASLKKLRAQAEAQQPVFNTL 1124
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD---LTASLQEkeraIEATNAEITKLRSRVDLKLQELQHL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1125 RDE---LRGAQEVGERLQQRHGERDVEVERWR---ERVTQLLERW----QAVLAQTDVRQRELEQLGRQLRYYRESADPL 1194
Cdd:pfam15921 537 KNEgdhLRNVQTECEALKLQMAEKDKVIEILRqqiENMTQLVGQHgrtaGAMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1195 SAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQkfaKQYINAIKDYELQLITYKAQLEPVASP 1274
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1275 AKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAH 1354
Cdd:pfam15921 694 TNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA-------------MKVAMGMQKQITAKR 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1355 AQAKAqaeleaqelqrrMQEEVARREEAAVDAQQQKRSIQEELQHLRQsseaeiqakaqqveaaersrmrieeeirvvrl 1434
Cdd:pfam15921 741 GQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ-------------------------------- 776
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1435 QLETTERQRGGAEGELQALRA---RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR 1495
Cdd:pfam15921 777 ELSTVATEKNKMAGELEVLRSqerRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1347-1475 |
4.05e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.44 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1347 QRQLAEAHAQ-AKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKaQQVEAAERSRMRI 1425
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ-QELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 256418964 1426 EEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1475
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1802-2192 |
4.40e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1802 QRAEAERVLTEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdiEERLAQLRkasESEL 1881
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1882 ERQKglVEDTLRQRRQVEEEIMALKVSFEKaaagkaELE-LELGRIRSNaedtmrSKEQAELEAARQRQLAaeeeqrrre 1960
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1961 aeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQReee 2039
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK--- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2040 lqqtlqqeqnmldRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeq 2119
Cdd:pfam17380 474 -------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA-- 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2120 eaarraqaeqaalKQKQAADAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT 2192
Cdd:pfam17380 539 -------------EEERRKQQEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1398-1686 |
4.66e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.11 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1398 QHLRQSsEAEIQAKAQQVEAAERSRMRIEEeiRVVRLQLETTERQrggaegelqalrARAEEAEAQKRQAQEEA-----E 1472
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAARE------------ARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1473 RLRRQVQDESQRKRQAEAELALRVKAEAEA-AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEV 1551
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAReARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1552 ELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAeaerareeaerelerwqlkANEALRLRLQAEEVAQQKS 1631
Cdd:PRK05035 574 EVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------------------AVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 1632 LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1686
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2291-2436 |
4.92e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 56.18 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2291 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLVEEtQGFQRTLEAERQRQLEMSAEAERLKL 2362
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2363 RMAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2436
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1077-1739 |
5.05e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.34 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1077 EEVLKTHEEQLKE-----AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVER 1151
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1152 WRERVTQ-------LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKR-RQEQIQAVpiANCQAAREQL 1223
Cdd:pfam01576 417 LQARLSEserqraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQElLQEETRQK--LNLSTRLRQL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1224 RQEKALLEEieRHGEKVEECQKFAKQyinaIKDYELQLITYKAQLEPVASPAK-----KPKVQSGSESVIQEY------- 1291
Cdd:pfam01576 495 EDERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaay 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1292 ------------------VDLRTRYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlAEVEAALEKQRQLAEA 1353
Cdd:pfam01576 569 dklektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR-AEAEAREKETRALSLA 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1354 HAQAKAQAELEAQELQRRMQE--------------------EVARR--EEAAVDAQQQKRSIQEEL-------------- 1397
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRaemedlvsskddvgknvhelERSKRalEQQVEEMKTQLEELEDELqatedaklrlevnm 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1398 QHLRQSSEAEIQAKAqqvEAAERSRMRIEEEIRVVRLQLETTERQRGGA-------EGELQALRARAEEAEAQKRQAQEE 1470
Cdd:pfam01576 723 QALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQ 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1471 AERLRRQVQDesqrkRQAEAELALRVKAEAEA-AREKQRALQALDELRLQAEE----AERRLRQAEAERAR-QVQVALET 1544
Cdd:pfam01576 800 LKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGA 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1545 AQRSAeveLQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELE-----RWQL-KANEALR 1618
Cdd:pfam01576 875 SGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQksesaRQQLeRQNKELK 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1619 LRLQAEEVA---QQKSLAQA------DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1689
Cdd:pfam01576 952 AKLQEMEGTvksKFKSSIAAleakiaQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSR 1031
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 256418964 1690 LIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEM 1739
Cdd:pfam01576 1032 MKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1652-1860 |
5.74e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 55.73 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1652 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheataATQKRQEL 1728
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1729 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEeakRQRQLAEEDAARQRAEAER 1808
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQE---LQRKKQQEEAERAEAEKQR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1809 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1860
Cdd:pfam15709 454 QKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2249-2465 |
5.85e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.85 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2249 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2328
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2329 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2408
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 2409 LEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2465
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1129-1554 |
6.98e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1129 RGAQEvgERLQQRHGERDVEVERW--RERVTQLLERWQ-----------AVLAQTDVRQrELEQLGRQLRY-YRESADpl 1194
Cdd:PRK04863 781 RAARE--KRIEQLRAEREELAERYatLSFDVQKLQRLHqafsrfigshlAVAFEADPEA-ELRQLNRRRVElERALAD-- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1195 sawlQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEiERHGEKVEECQ---KFAKQYINAIKDYELQLitykAQLEPV 1271
Cdd:PRK04863 856 ----HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD-ETLADRVEEIReqlDEAEEAKRFVQQHGNAL----AQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1272 AS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAeereRLAEVEAALE 1345
Cdd:PRK04863 927 VSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1346 KQRqlaEAHAQAKAQAeleAQELQRRMQEEVARREeaavdAQQQKRSIQEELQHL--RQSSEAEIQAKAQqveaaersRM 1423
Cdd:PRK04863 1003 RAR---EQLRQAQAQL---AQYNQVLASLKSSYDA-----KRQMLQELKQELQDLgvPADSGAEERARAR--------RD 1063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1424 RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEAELALRV 1496
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRLVKDNGVERRLHRRELAYLS 1143
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1497 KAEAEAAREKqrALQALdelrlqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1554
Cdd:PRK04863 1144 ADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3695-3730 |
7.08e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.08e-07
10 20 30
....*....|....*....|....*....|....*.
gi 256418964 3695 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3730
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1467-2002 |
8.43e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1467 AQEEAERLRRQVQDESQRKR---QAEAELALRVKaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALE 1543
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIK---EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1544 TAQRSAEVE-LQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQ 1622
Cdd:PRK03918 240 IEELEKELEsLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1623 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLR 1694
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1695 AETEQGEQQRQLLEEELAR--LQHEATAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR----------- 1754
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytael 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1755 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLTEKLAAISEA 1820
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1821 TRLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA---------SESELERQKGLV 1888
Cdd:PRK03918 542 KSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKEL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1889 EDTLRQRRQVEEEIMALKVSFEKAaagKAELElELGRIRSnaEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRS 1968
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
570 580 590
....*....|....*....|....*....|....
gi 256418964 1969 LAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2002
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1321-1516 |
8.48e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1321 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR-REEAAVDAQQQKRSIQEElqh 1399
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKKAAA--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1400 lRQSSEAEIQAKAQQVEAAErsrmrieeeirvvrlqletterQRGGAEGELQALRARAEEAEAQKRQAQEEAErlrrqvq 1479
Cdd:PRK09510 182 -EAKKKAEAEAAAKAAAEAK----------------------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA------- 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 256418964 1480 desqRKRQAEAELALRVKAEAEAAREKQRAlqALDEL 1516
Cdd:PRK09510 232 ----AEAKAAAEKAAAAKAAEKAAAAKAAA--EVDDL 262
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4117-4145 |
9.42e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.42e-07
10 20
....*....|....*....|....*....
gi 256418964 4117 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4145
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1665-1880 |
9.52e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1665 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1744
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1745 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK 1813
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1814 LAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE 1880
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1322-1699 |
1.07e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1322 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarREEAAVDAQQQKRSIQEELQHLR 1401
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE----LKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1402 QSSEAEIQAKAQQVEAAERSRMRIEE-EIRVVRLQLETTERqrggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1480
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLER-----ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1481 ESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKRA 1558
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1559 SFAEKTAQLERTLQEEH---VTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrLRLQAEEVAQQKSLAQA 1635
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRI-EKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1636 DAEKQKEEAEREARRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1699
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRREL--QELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1295-1414 |
1.11e-06 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 53.45 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1295 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELeaqelqR 1370
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 256418964 1371 RMQEEVARREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKAQQ 1414
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKE 177
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2139-2600 |
1.34e-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: 54.84 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2139 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2207
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2208 VRvqmeeLGKLKARIeaeNRALILRDKDNTQRFLEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRaLAEKM 2286
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2287 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLE 2352
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2353 MSAEAERLKLRMAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLR 2424
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2425 EAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQ---ETQALQKSFLSEKDSLLQR-----ERFIEQEKAKLEQLfQ 2496
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartEKQAYWQVVEGALDAQLALlkaaiAARRSGAKAELKAL-E 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2497 DEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRL 2576
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARL 833
|
490 500
....*....|....*....|....
gi 256418964 2577 EEEHRAALAhsEIATTQAASTKAL 2600
Cdd:pfam12128 834 IADTKLRRA--KLEMERKASEKQQ 855
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1316-1796 |
1.40e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1316 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1395
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQHLRQSSE------AEIQAKAQQVEAAERSRMRIEEEIR--VVRLQLET-------TERQRGGAEGELQALRARAEEA 1460
Cdd:pfam05557 133 ELEELQERLDllkakaSEAEQLRQNLEKQQSSLAEAEQRIKelEFEIQSQEqdseivkNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1461 EAQKRQAQEEAERLRRQVQDESQRKRQAEaelalrvKAEAEAAR---EKQRALQALDELRLQAEEAERRLRQAEAERARQ 1537
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREE-------KYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1538 VQValetaqRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQLK 1612
Cdd:pfam05557 286 EQL------QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkERDGYR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1613 AN-EALRLRLQAEEVAQQKSLAQADAE----KQKEEAEREARRRGKAEEQAVRQRELA---EQELEKQRQlAEGTAQQRL 1684
Cdd:pfam05557 360 AIlESYDKELTMSNYSPQLLERIEEAEdmtqKMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQALRQ-QESLADPSY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1685 AAE------QELIRLRAETEQGEQQRQLLEEELAR--------------LQHEATAATQKRQELEAELAKVRAEMEVLla 1744
Cdd:pfam05557 439 SKEevdslrRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERL-- 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1745 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEeaarLRALAEEA-KRQRQLAE 1796
Cdd:pfam05557 517 -KRLLKKLEDDLEQVLRLPETTSTMNFKEVLD----LRKELESAeLKNQRLKE 564
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2142-2445 |
1.41e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2142 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKAR 2221
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2222 IEAENRAL------ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2293
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2294 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaerqrqlemsaeaeRLKLRMAEMSRAQAR 2373
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 2374 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2445
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1278-1471 |
1.44e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1278 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1357
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1358 KAQAELEAQ--ELQRRMQEEVARREE---AAVDAQQQ----KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1428
Cdd:COG3206 263 PVIQQLRAQlaELEAELAELSARYTPnhpDVIALRAQiaalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 256418964 1429 IRV---VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1471
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1355-1569 |
1.57e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.70 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1355 AQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAqqveaAERSRMRIEEEIRvvrl 1434
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1435 qletterqrggaegelQALRARAEEAEAQKRQAQEEAERlrrQVQDESQRKRQAEAelalRVKAEAEAAREKQRALQALD 1514
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1515 ELRLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1569
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2078-2667 |
2.07e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2078 EAAQSRKQVEEAERLKQ-SAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEqtlRQK 2156
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYlDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE---EEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2157 AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDN 2236
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2237 TQR-------------FLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL---AQQRALAEKMLKEKMQAVQEATRL 2300
Cdd:pfam02463 369 EQLeeellakkkleseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeeKKEELEILEEEEESIELKQGKLTE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2301 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAeAERLKLRMAEMSRAQARAEED--- 2377
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE---QLELLLSRQKLEERSQ-KESKARSGLKVLLALIKDGVGgri 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2378 ---AQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQqsdhdaeRLREAIAELEREKEKLKQEAKLLQLKSEEMQTV 2454
Cdd:pfam02463 525 isaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ-------KLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2455 QQEQILQETQALQKSFLSEKDSLLQRErFIEQEKAKLEQLFQdEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQ 2534
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKV-VEGILKDTELTKLK-ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2535 REAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgPSVEA 2614
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL---------KQKID 746
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2615 EPEYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTvaELTQREDVYRYLK 2667
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLK 797
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1468-2004 |
2.19e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1468 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQR 1547
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1548 SAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAerraqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVA 1627
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELE----------------------------AELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1628 QQKSLAQAdaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1707
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1708 EEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1787
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1788 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALH--KAD 1865
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQelKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1866 IEERLAQLRKASESELERQKGLVEDTLRQR-RQVEEEImalkvsfekaaagkAELELELGRIRsnaedtmrsKEQAELEA 1944
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEEL--------------EELEEELEELR---------EELAELEA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1945 ARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEAR--RLRERAE 2004
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERlpPVLERAS 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2194-2442 |
2.34e-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: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2194 AARQRSQVEEELFSVRVQMEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAE 2273
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2274 EDLAQQRALaekmLKEKMQAVQEATRLKAEAELLQQQKELaqeQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEM 2353
Cdd:COG4942 97 AELEAQKEE----LAELLRALYRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2354 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAeeigeklhrTELATQEKVTLVQTLEIQRQqsdhdAERLREAIAELERE 2433
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLL---------ARLEKELAELAAELAELQQE-----AEELEALIARLEAE 235
|
....*....
gi 256418964 2434 KEKLKQEAK 2442
Cdd:COG4942 236 AAAAAERTP 244
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
4-129 |
2.43e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 50.04 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 4 SRAIQHEISslkdERDRVqkkTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EK 70
Cdd:cd21323 14 SEGTQHSYS----EEEKV---AFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKK 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 71 GRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 129
Cdd:cd21323 87 KLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1337-1749 |
2.46e-06 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 54.09 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1337 LAEVEAALEKQRQLAEAHAQAKaqaelEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1405
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1406 --------AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1477
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1478 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1557
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1558 ASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADA 1637
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1638 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1717
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 256418964 1718 ATAATQKRQELEAELAKVRAEMEVLLASKARA 1749
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3900-3937 |
2.48e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.48e-06
10 20 30
....*....|....*....|....*....|....*...
gi 256418964 3900 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3937
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
22-130 |
2.48e-06 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 50.06 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 22 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 88
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 256418964 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 130
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1653-2026 |
2.57e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.72 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1732
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1733 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1810
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1811 TEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRRLEEQAAlhkadieerlaqlrKASESELERQKGLVED 1890
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKS--------------QNGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1891 TLRQRRQVEEEimalkvsfEKAAAGKAELELELGRIR-SNAEdtmrsKEQAELEAARQRQLAAEEEQRRREAEERVQRSL 1969
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1970 AAEEEaaRQRKValEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2026
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1314-1547 |
2.83e-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: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARReEAAVDAQQQKRSI 1393
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQ-EAEQRKQCQEQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1394 QEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA------EAQKRQA 1467
Cdd:pfam15558 130 KEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQRS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1468 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ----RALQALDELRL-QAEEAERRLRQAEAERARQVQVAL 1542
Cdd:pfam15558 210 QENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNLER 289
|
....*
gi 256418964 1543 ETAQR 1547
Cdd:pfam15558 290 EKNHH 294
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1457-1573 |
2.91e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1457 AEEAEAQKRQAQEEAErLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALdELRLQAEEAErrlrqaeaeraR 1536
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARAEAEA-AYEIAEANAE-----------R 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 256418964 1537 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1573
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1077-1793 |
3.08e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.60 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1077 EEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAqqpvfntLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1155
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1156 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplSAWLQDAKRRQEQIQAvpiaNCQAAREQLRQEKALLEEIER 1235
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRK----QLSKTQEELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1236 H-GEKV------EECQKFAKQYINAIKDYELQLITYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTSQY 1308
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1309 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEAQeLQRRMQEEVARREEAAVDAq 1387
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDKAAEVEVERMSA- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1388 qqkRSIQEELQhlrQSSEAEIQAKaQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1467
Cdd:pfam07111 376 ---KGLQMELS---RAQEARRRQQ-QQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1468 QEEAER--LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldELRLQA----EEAERRLRQAEAERARQVQVA 1541
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA--ELQLSAhliqQEVGRAREQGEAERQQLSEVA 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1542 LETAQrsaevELQSKRASFAEKTAQLERTLQEEhvtvaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRl 1621
Cdd:pfam07111 527 QQLEQ-----ELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1622 qAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGE 1701
Cdd:pfam07111 566 -QELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK-ERNQELRRLQDEARKEE 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1702 QQR-----QLLEEE----LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRLEAE 1767
Cdd:pfam07111 644 GQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSLTVL 723
|
730 740
....*....|....*....|....*.
gi 256418964 1768 AGRFRELAEEAARLRALAEEAKRQRQ 1793
Cdd:pfam07111 724 LDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1076-1724 |
3.18e-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: 53.80 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1076 AEEVLKTHEEQLKEAQAVPATL-QELEATKASLKKLRAQAEA---QQPVFNTLRDE----LRGAQEVGERLQQR-HGERD 1146
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPAwlaAQDALERLREQsgeaLADSQEVTAAMQQLlERERE 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1147 VEVER-----WRERVTQLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLSAWLQDAKrrqeqiQAVPIA 1214
Cdd:COG3096 642 ATVERdelaaRKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPAR------HAIVVP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1215 NCQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKKPKVQSG 1283
Cdd:COG3096 716 DLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRLEELRAE 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1284 SESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEL 1363
Cdd:COG3096 794 RDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLK 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1364 EAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEEI 1429
Cdd:COG3096 871 EQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQ 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1430 RVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkrQAEAELAL 1494
Cdd:COG3096 951 RRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQV--LASLKSSR 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1495 RVKAE--AEAARE-KQRALQALDELRLQAEEAERRLRQA-EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1570
Cdd:COG3096 1029 DAKQQtlQELEQElEELGVQADAEAEERARIRRDELHEElSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1571 LQEEHVtvaqlreeaerraqqqaeaerareeaerelERW----QLKANEALRLRLQAEEVAQQkslaqaDAEKQKEEAer 1646
Cdd:COG3096 1109 QVVQAK------------------------------AGWcavlRLARDNDVERRLHRRELAYL------SADELRSMS-- 1150
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1647 earrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQR---------LAAEQEL-IRLRAETEQGEQQRQLLEE---ELAR 1713
Cdd:COG3096 1151 ---------DKALGALRLAVADNEHLRDALRLSEDPRrperkvqfyIAVYQHLrERIRQDIIRTDDPVEAIEQmeiELAR 1221
|
730
....*....|.
gi 256418964 1714 LQHEATAATQK 1724
Cdd:COG3096 1222 LTEELTSREQK 1232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1279-1493 |
3.20e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1279 KVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA 1355
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1356 QAKAQAELEAQELQRRMQEEVARREEAAVDAQQQkrsiQEELQHLRQSSEAEIQAKAQQVEAAERSRmrieeeirvVRLQ 1435
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEER---------AALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1436 LETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1493
Cdd:COG4942 192 ALKAERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1320-1485 |
3.28e-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: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1320 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1399
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1400 LRQSSEAEIQAKAQQVEA-AERSRMRIEEEI----RVVRLQLETTERQRGGAEGELQALRARAEEAEAQK------RQAQ 1468
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 256418964 1469 EEAERLRRQVQDESQRK 1485
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3105-3141 |
3.75e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.75e-06
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 3105 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3141
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2778-2813 |
4.01e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 4.01e-06
10 20 30
....*....|....*....|....*....|....*.
gi 256418964 2778 RLLEAQIATGGIIDPVHSHRVPVDVAYKRGYFDEEM 2813
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1655-1880 |
4.09e-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: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1655 EEQAVRQRELAEQELEK-QRQLAEgtAQQRL-AAEQELIRLRAETE--QGEQQRQLLEEELARLQHEATAATQKRQELEA 1730
Cdd:COG3206 163 EQNLELRREEARKALEFlEEQLPE--LRKELeEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1731 ELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1810
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1811 TEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAALHKADIEERLAQLRKASESE 1880
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1550-2384 |
4.29e-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: 53.20 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1550 EVELQSKRASFAEKTAQ-LERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELerwQLKANEALRLRLQAEEVAQ 1628
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEhIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDL---QTKLQEMQMERDAMADIRR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1629 QKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQqrlaaeqELIRLRAETEQGEQQRQLLE 1708
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKKIYEH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1709 EELARLQHEA--TAATQKRQELEAELA-------KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEA 1778
Cdd:pfam15921 208 DSMSTMHFRSlgSAISKILRELDTEISylkgrifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1779 ARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1858
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1859 AALHKADIEERLAQL-----RKASESELERQkglvedtlrQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEdT 1933
Cdd:pfam15921 368 FSQESGNLDDQLQKLladlhKREKELSLEKE---------QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLK-A 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1934 MRSKEQAELEaarqRQLAaeeeqrrreaeervqrslaaeeeAARQRKVALEEVERLKAKVEEARR-LRERAEQESARQLQ 2012
Cdd:pfam15921 438 MKSECQGQME----RQMA-----------------------AIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMT 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2013 LAQE---------AAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREaaq 2081
Cdd:pfam15921 491 LESSertvsdltaSLQEKERAIEATNAEItkLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL--- 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2082 sRKQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalkqkqaadaeMEKHKKFAEQTLRQKAQVEQ 2161
Cdd:pfam15921 568 -RQQIENMTQL-------------------------------------------------VGQHGRTAGAMQVEKAQLEK 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2162 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----EEELFSVRVQMEELGKLKARIE---------AENRA 2228
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrnelnslSEDYE 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2229 LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK----MLKEKMQAVQEA- 2297
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKmqlksaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRgqidALQSKIQFLEEAm 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2298 TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLvEETQGFQRTLeaeRQRQLEMSAEAERLKLRMAEMSRAQARAEED 2377
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
....*..
gi 256418964 2378 AQRFRKQ 2384
Cdd:pfam15921 834 SVRLKLQ 840
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2134-2319 |
4.44e-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: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2134 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQME 2213
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2214 ELGKLKARIEaenRAL-ILRDKDNT----QRFLEEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2285
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 256418964 2286 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2319
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2259-2537 |
4.52e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2259 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmaQQLVEETQG 2338
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK----QQQLAAISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2339 FQRTLEAERQRQLEMSAEAERlklrmaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2418
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2419 DAE---RLREAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSllqrerfiEQEKAKLEQ 2493
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 256418964 2494 LFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRR-QREA 2537
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1337-1431 |
4.86e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.03 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1337 LAEVEAALEKQRQLAEAHAQAKAQAeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKAQQV 1415
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQS----QALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 256418964 1416 EAAERSRMRI---EEEIRV 1431
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1314-1550 |
4.97e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 52.29 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQ 1388
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1389 QKRSIQEElqhlrqsseaeiqAKAQQVEAAERSRMRIEEeirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQ 1468
Cdd:PRK07735 93 AKAKAAAA-------------AKAKAAALAKQKREGTEE---------VTEEEKAAAKAKAAAAAKAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1469 EEAERLRRQVQDESQRKRQAEAelalrVKAEAeAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRS 1548
Cdd:PRK07735 151 EEVTEEEEETDKEKAKAKAAAA-----AKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
..
gi 256418964 1549 AE 1550
Cdd:PRK07735 225 QG 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1124-1574 |
5.30e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1124 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKR 1203
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1204 RQEQIQAVpiancQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLepvaspakkpkvqsg 1283
Cdd:COG4717 127 LLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1284 SESVIQEYVDLRTRYSELttltSQYIKFISETLRRMEEEERLAEQQraeeRERLAEVEAALEKQRQLAEAHAQAKAQAEL 1363
Cdd:COG4717 187 SLATEEELQDLAEELEEL----QQRLAELEEELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLLLLIAAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1364 EAQELQRRMQEEVARREEAAVDAQQQ------KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLE 1437
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1438 TTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESqrkrqaEAELALRVKAEAEAAREKQRALQALDELR 1517
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED------EEELRAALEQAEEYQELKEELEELEEQLE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1518 LQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1574
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1712-2442 |
5.75e-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: 52.80 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1712 ARLQHEATAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1788
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1789 KRQRQLAEEDAAR---QRAEAERVLT------EKLAAISEATRLKTE---AEIALKEKEaENERLRRLAEDEAFQRRRLE 1856
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMdlnnniEKMILAFEELRVQAEnarLEMHFKLKE-DHEKIQHLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1857 EQAALHKADIEERlaqlrkasESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRS 1936
Cdd:pfam05483 240 KQVSLLLIQITEK--------ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1937 keqaeleaarQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR---KVALEEVERLKAKVEEARRLRERAEQESARQLQL 2013
Cdd:pfam05483 312 ----------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2014 AQEAAQKRLQAEEKAHAFVVQQREEelqqtlqqeqnmLDRLRSEAEAARRAAEEaeeareqaereaaqsRKQVEE-AERL 2092
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVE------------LEELKKILAEDEKLLDE---------------KKQFEKiAEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2093 KQSAEEQAQAQAQAQAAAEKLRkeaeQEAARRAQAEQAALKQKQAADAEMEKHK-KFAEQT------LRQKAQVEQELTT 2165
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLE----IQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTahcdklLLENKELTQEASD 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2166 LRLQLEetDHQKSILDEELQ--RLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkarieaENRALILRDKDNTQRFLEE 2243
Cdd:pfam05483 511 MTLELK--KHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFIQKGD-------EVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2244 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ---EATRLKAEAELLQQQKELAQEQARR 2320
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQK 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2321 LQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSaeaERLKLRMAEMSraqARAEEDAQRFRKQAEEIGEKLHRTELATQ 2400
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAEMV---ALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 256418964 2401 EKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAK 2442
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1701-1892 |
5.75e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1701 EQQRQLLEEELAR-LQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGRFR----ELA 1775
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1776 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 1854
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 256418964 1855 LEEQAALHKADIEERLAQLRKASESELERQKGLVEDTL 1892
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2139-2594 |
6.03e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2139 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEE-TDHQKSILDE-ELQRLKAEVTEAAR-----QRSQVEEELFSVRVQ 2211
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEElEEERDDLLAEaGLDDADAEAVEARReeledRDEELRDRLEECRVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2212 MEELGK----LKARI-EAENRALILRDKDNTqrfLEEEAEKMK-QVAEEAARLSVAAQEAARLRQL---AEEDLAQQRAL 2282
Cdd:PRK02224 337 AQAHNEeaesLREDAdDLEERAEELREEAAE---LESELEEAReAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2283 AEKMLKEKMQAVQEATRLKAEaelLQQQKELAQEQARRLQEDKEQMAQQLVEETqGFQRTLEAERQRQLEMSAEAERLKL 2362
Cdd:PRK02224 414 LEELREERDELREREAELEAT---LRTARERVEEAEALLEAGKCPECGQPVEGS-PHVETIEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2363 RMAEMSRAQARAEE------DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2436
Cdd:PRK02224 490 EVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2437 LKQEAKLLQLKSEEM-QTVQQEQILQETQALQKSFLSEKDSLL-QRERFIEQEKAKLEQLFQDEVAKAKQLREEQQrqqq 2514
Cdd:PRK02224 570 AREEVAELNSKLAELkERIESLERIRTLLAAIADAEDEIERLReKREALAELNDERRERLAEKRERKRELEAEFDE---- 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2515 qmeqekqelmASMEEARRRQREAEE------GVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALA-HS 2587
Cdd:PRK02224 646 ----------ARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAlYD 715
|
....*..
gi 256418964 2588 EIATTQA 2594
Cdd:PRK02224 716 EAEELES 722
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3436-3472 |
6.81e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.55 E-value: 6.81e-06
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 3436 IRLLEAQVATGGIIDPVHSHRLPVDVAYQRGYFDEEM 3472
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1667-2055 |
6.90e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1667 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EATAATQKRQELEAELAKVRAEMEvlla 1744
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1745 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRaeaervlteklaaISEATRLK 1824
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------------LAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1825 TEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVedtlrqrrQVEEEIMA 1904
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL--------FLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1905 LKVSF---EKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV 1981
Cdd:COG4717 288 LLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1982 ALEEVERL--KAKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEK-AHAFVVQQREEELQQTLQQEQNMLDRLR 2055
Cdd:COG4717 368 LEQEIAALlaEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGeLEELLEALDEEELEEELEELEEELEELE 445
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2225-2501 |
7.02e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2225 ENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA 2304
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2305 ELLQQQKELAQEQARRLQEDKEQMAQqlvEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2384
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRAR---IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2385 AEEIGEKLHRT------ELATQEKVTLVQTLEIQ----RQQSDHDAER---------LREAIAELEREKEKLKQeakLLQ 2445
Cdd:TIGR00618 320 MRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQeihiRDAHEVATSIreiscqqhtLTQHIHTLQQQKTTLTQ---KLQ 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2446 LKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAK 2501
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
594-686 |
7.20e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 594 HGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQA 673
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 256418964 674 ALQTQWSWMLQLC 686
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
132-239 |
7.43e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 47.88 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 132 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 210
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 256418964 211 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1301-1540 |
7.87e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1301 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAELEAQELQRrMQEEVAR 1378
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1379 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggAEGELQALRAR-A 1457
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1458 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEaAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1537
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
...
gi 256418964 1538 VQV 1540
Cdd:COG3206 388 VRV 390
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2241-2603 |
7.88e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2241 LEEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2320
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2321 LQEDKEQMAQQLVEETQgfqrtLEAERQRQLEMSAEAERLKLrmaemsraqaraEEDAQRFRKQAEEIGEKLHRtELATQ 2400
Cdd:pfam02463 249 EQEEIESSKQEIEKEEE-----KLAQVLKENKEEEKEKKLQE------------EELKLLAKEEEELKSELLKL-ERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2401 EKVTLVQTLEIQRQQSDHDAERLREAIAELEREKeKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQR 2480
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2481 ERFIEQEKAKLEQLFQdevaKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVR-RKQEELQHLEQQRQQQE 2559
Cdd:pfam02463 390 AKLKEEELELKSEEEK----EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTeEKEELEKQELKLLKDEL 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 256418964 2560 KLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALPNG 2603
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1327-1509 |
8.25e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1327 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRrmqeEVARREEAAVDAQQQKRSIQEELQHLRqsSEA 1406
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1407 EIQAKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1486
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 256418964 1487 QAEAELALRVKAEAEAAREKQRA 1509
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRK 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1756-2199 |
8.39e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1756 TSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1834
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1835 EAENERLRRLAEdeafQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAA 1914
Cdd:COG4717 145 PERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1915 GKAELELELGRIRSNAEDTMRSKEQAELEAArQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-- 1992
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1993 -VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEA 2071
Cdd:COG4717 300 lGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2072 REQAEREAAQSRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQAALKQK-QAADAEMEKHKKFAE 2150
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKE----------ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 256418964 2151 QTLRQKAQVEQELTTLrlqleETDHQKSILDEELQRLKAEVTEAARQRS 2199
Cdd:COG4717 450 ELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2151-2544 |
1.02e-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: 52.04 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2151 QTLRQKAQVE------QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS----QVEEELFSVRVQMEELGKLKA 2220
Cdd:pfam15921 445 QMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaSLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2221 RIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedLAQQRALAEKMLKEKMQAVQEAT 2298
Cdd:pfam15921 525 RVDLKLQELQhLKNEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEKEIN 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2299 RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDA 2378
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2379 QRFRKQAEEIgeklhrtELATQEkvtlvqtLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQlkseEMQTVQQEQ 2458
Cdd:pfam15921 681 RNFRNKSEEM-------ETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ----KQITAKRGQ 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2459 IlqetQALQK--SFLSEKDSLLQRER-FIEQEKAKLEQLFQdEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRR-- 2533
Cdd:pfam15921 743 I----DALQSkiQFLEEAMTNANKEKhFLKEEKNKLSQELS-TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKas 817
|
410 420
....*....|....*....|.
gi 256418964 2534 ----------QREAEEGVRRK 2544
Cdd:pfam15921 818 lqfaecqdiiQRQEQESVRLK 838
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2154-2439 |
1.05e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2154 RQKAQVEQELTTLRLQLeeTDHQKSiLDEE-------------LQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkA 2220
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQQA-LDVQqtraiqyqqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2221 RIEAENRaliLRDKDNTQRFLEEEAEKMKQVAEEaarlsVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKM 2291
Cdd:PRK04863 458 LLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGE-----VSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2292 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEEtqgfqrtLEAERQRQLEMSAEAERLKLRMAE-MSRA 2370
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARA 602
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2371 QA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLREAIAELEREKEKLKQ 2439
Cdd:PRK04863 603 PAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1317-1432 |
1.09e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-ELEAQELQRRMQEEVARREEAAVD---------A 1386
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 256418964 1387 QQQKR----SIQEELQHLRQSSEAEIQAkaqQVEAAERsRMRIEEEIRVV 1432
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAEEKA---RLEAEER-RQKEEEAARLA 508
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1685-1780 |
1.10e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.88 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1685 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1764
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 256418964 1765 EAEAGRFrELAEEAAR 1780
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1326-1754 |
1.12e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.45 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1326 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1405
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1406 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1485
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1486 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1565
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1566 QLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAE 1645
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1646 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1725
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 256418964 1726 QELEAELAKVRAEMEVLLASKARAEEESR 1754
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3902-3940 |
1.13e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.13e-05
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3902 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3940
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2238-2501 |
1.22e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2238 QRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2317
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2318 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAE-RLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTE 2396
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2397 LATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQIlQETQALQKSFLSEKDS 2476
Cdd:pfam13868 194 EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA-EREEEEFERMLRKQAE 272
|
250 260
....*....|....*....|....*
gi 256418964 2477 LLQRERFIEQEKAKLEQLFQDEVAK 2501
Cdd:pfam13868 273 DEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1460-1670 |
1.29e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1460 AEAQKRQAQEEAERLRRQVQDESQRKRQAEaELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQ 1539
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1540 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEaerelerwqlKANEALRL 1619
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA----------KKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1620 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1670
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
19-118 |
1.63e-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: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 19 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 94
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 256418964 95 LVNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
925-1538 |
1.75e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 925 DRLVAEREYGSCSRhyQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETrtvhrlrlplDKDPAREcaqRIAEQQKA 1004
Cdd:PRK02224 223 ERYEEQREQARETR--DEADEVLEEHEERREELETLEAEIEDLRETIAETER----------EREELAE---EVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1005 ----QAEVEGLGKGVARLSAEAEKVLALPEpspaapTLRSELELTLGKLEQVRSlsaiyleklkTISLVIRSTQGAEEVL 1080
Cdd:PRK02224 288 leelEEERDDLLAEAGLDDADAEAVEARRE------ELEDRDEELRDRLEECRV----------AAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1081 KTHEEQLKEAQAVPATLQ-ELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTql 1159
Cdd:PRK02224 352 DDLEERAEELREEAAELEsELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1160 lerwqavlaqtdvrqrELEqlgrqlryyresadplsawlqdakrrqeqiqavpiANCQAAREQLRQEKALLEEierhgEK 1239
Cdd:PRK02224 430 ----------------ELE-----------------------------------ATLRTARERVEEAEALLEA-----GK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1240 VEECQKFAKQ--YINAIKDYELQLITYKAQLEPVASpakkpkvqsgsesviqEYVDLRTRYSELTTLTSQyikfiSETLR 1317
Cdd:PRK02224 454 CPECGQPVEGspHVETIEEDRERVEELEAELEDLEE----------------EVEEVEERLERAEDLVEA-----EDRIE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1318 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevARREEAAVDAQQQkrSIQEEL 1397
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLA--ELKERI 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1398 QHLR--QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAlrARAEEAEAQKRQAQEEAErlr 1475
Cdd:PRK02224 589 ESLEriRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLE--- 663
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1476 rQVQDESQRKRQAEAELALRVKA------EAEAAREKQRAL----QALDELRLQAEEAERRLRQAEAE-RARQV 1538
Cdd:PRK02224 664 -QVEEKLDELREERDDLQAEIGAveneleELEELRERREALenrvEALEALYDEAEELESMYGDLRAElRQRNV 736
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1626-1947 |
1.82e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.37 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1626 VAQQKSLAQADA--EKQKEEAEREARRRGKAEEQAVRQRelaeQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ 1703
Cdd:NF012221 1535 VATSESSQQADAvsKHAKQDDAAQNALADKERAEADRQR----LEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1704 RQLLEEELARLQHEATAATQKRQELEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEAGRF----R 1772
Cdd:NF012221 1608 RDAILEESRAVTKELTTLAQGLDALDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQ 1685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1773 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1852
Cdd:NF012221 1686 KVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQA 1765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1853 RRLEEQAALHKADIEERlaqlRKASESELERQKGLVEDtlrqrrqVEEEIMALKVSFEKAAAGKaelelelgrirsNAED 1932
Cdd:NF012221 1766 QADAKGAKQDESDKPNR----QGAAGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG 1822
|
330
....*....|....*
gi 256418964 1933 tMRSKEQAELEAARQ 1947
Cdd:NF012221 1823 -LTEQEQEALEGATN 1836
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3068-3104 |
1.89e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.89e-05
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 3068 KLLSAEKAVTGYRDPYSGQSVSLFQALKKGLIPREQG 3104
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1924-2589 |
1.92e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.13 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1924 GRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERA 2003
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2004 EQEsaRQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSR 2083
Cdd:pfam02463 222 EEE--YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2084 KQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQEL 2163
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2164 TTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM--EELGKLKARIEAENRALILRDKDNTQRFL 2241
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2242 EEEAEKM-KQVAEEAARLSVAA----QEAARLRQLAEEDLAQQRA--------LAEKMLKEKMQAVQEATRLKAEAELLQ 2308
Cdd:pfam02463 460 LLKDELElKKSEDLLKETQLVKlqeqLELLLSRQKLEERSQKESKarsglkvlLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2309 QQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEI 2388
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2389 GEKLHRTELATQEKVTLVQTLEIQRQQsdhdaeRLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2468
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKES------GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2469 SFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEgvRRKQEEL 2548
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE--EKSELSL 771
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 256418964 2549 QHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEI 2589
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2156-2581 |
1.99e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2156 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSVRVQMEELGKLKAriEAENRALILRDKD 2235
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2236 NTQ-RFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2310
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2311 ----KELAQEQARRLQEDKEQMaQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEmsraqaraEEDAQRFRKQAE 2386
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2387 EIGEKLHRTElatQEKVTLVQTleiqRQQSDHDAERLREAIAELE----REKEKLKQEAKLLQLKSEEMQTVQQEQILQE 2462
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQA----REKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2463 TQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQqqmeqEKQELMASMEEARRRQREAEEGVR 2542
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES-----VREEFIQKGDEVKCKLDKSEENAR 576
|
410 420 430
....*....|....*....|....*....|....*....
gi 256418964 2543 RKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2581
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2259-2464 |
2.04e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.72 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2259 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQaVQEATRLKAEAELLQQQKelaQEQARRLQEDKEQMAQQLVEETQG 2338
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMRRLE-VERKRREQEEQRRLQQEQ---LERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2339 FQRTLEAERQRQlemsAEAERLKLRMAEMsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQE------KVTLVQTLEIQ 2412
Cdd:pfam15709 392 RKQRLEEERQRQ----EEEERKQRLQLQA--AQERARQQQEEFRRKLQELQRKKQQEEAERAEaekqrqKELEMQLAEEQ 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 256418964 2413 RQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQ 2464
Cdd:pfam15709 466 KRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1132-1537 |
2.07e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1132 QEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKrrqeqiqav 1211
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK--------- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1212 piancqaarEQLRQEKALLEEIERHGEKVEECQK---FAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVI 1288
Cdd:TIGR00606 765 ---------NDIEEQETLLGTIMPEEESAKVCLTdvtIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1289 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAELEA 1365
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQLVELSTEVQsLIREIKDAKEQDSPLE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1366 Q---ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL------------------RQSSEAEIQAKAQQVEAAERSRMR 1424
Cdd:TIGR00606 916 TfleKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienkiqdgkddyLKQKETELNTVNAQLEECEKHQEK 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1425 IEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeAAR 1504
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKR 1068
|
410 420 430
....*....|....*....|....*....|...
gi 256418964 1505 EKQRALQALDELRLQAEEAERRLRQAEAERARQ 1537
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1610-1806 |
2.09e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1610 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQE 1689
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1690 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAE 1767
Cdd:COG2268 268 -----YEIAEANAEREVqRQLEIAEREREIELQEKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAE 339
|
170 180 190
....*....|....*....|....*....|....*....
gi 256418964 1768 AGRFRELAEEAARLRALAEEAKRQRQLAEedAARQRAEA 1806
Cdd:COG2268 340 AEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEAAAKP 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1467-1724 |
2.10e-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: 50.15 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1467 AQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERArqvqvALETAQ 1546
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELA-----ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1547 RSAEVELQSKRASFAEKTAQLERtlqeehvtvaQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEV 1626
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAE----------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1627 AQQKslaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQL 1706
Cdd:COG4942 156 RADL---AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR--------LEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 256418964 1707 LEEELARLQHEATAATQK 1724
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1375-1540 |
2.14e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.91 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1375 EVARR----EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggaegel 1450
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1451 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEsqrkrqaeaelalrvKAEAEAAREKQRALQALDElRLQAEEAERRLRQ 1529
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 256418964 1530 AEAERARQVQV 1540
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2143-2587 |
2.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2143 EKHKKFAEQTlRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEEL-G 2216
Cdd:COG4913 259 ELAERYAAAR-ERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2217 KLKARIEAENRAL--ILRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA 2293
Cdd:COG4913 338 DRLEQLEREIERLerELEERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2294 VQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM---------------------------AQQLVEETQG 2338
Cdd:COG4913 418 RRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervlggfALTLLVPPEH 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2339 FQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQS-- 2416
Cdd:COG4913 498 YAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA-ELGRRFDYVCVDSPEELRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2417 --------------DHDAERL-----------REAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKS 2469
Cdd:COG4913 577 itragqvkgngtrhEKDDRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2470 FLSEKDsLLQRERFIEQEKAKLEQL--FQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEE 2547
Cdd:COG4913 657 SWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 256418964 2548 LQHLEQQRQQQEKLLAEEnQRLRERLQRLEEEHRAALAHS 2587
Cdd:COG4913 736 LEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEER 774
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2185-2469 |
2.27e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2185 QRLKAEVTEAARQRSQVEEELFSVRVQmeelgKLKARIEAENRALILRDKDNTQRFLEEEAE--KMKQVAEEAARLSVAA 2262
Cdd:pfam05667 220 QEWEEEWNSQGLASRLTPEEYRKRKRT-----KLLKRIAEQLRSAALAGTEATSGASRSAQDlaELLSSFSGSSTTDTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2263 QEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATrlkaeaelLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQ 2340
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQ--------QQREEELEelQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2341 RTLEAERQRQLEMSAEAE--RLKLRMAE--------MSRAQARAEEDAQRFRKQAEEIGEklHRT--------------- 2395
Cdd:pfam05667 367 QVEEELEELKEQNEELEKqyKVKKKTLDllpdaeenIAKLQALVDASAQRLVELAGQWEK--HRVplieeyralkeaksn 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2396 -ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA-------KLLQL-KSEEMQTVQQEQILQETQAL 2466
Cdd:pfam05667 445 kEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrsaytrRILEIvKNIKKQKEEITKILSDTKSL 524
|
...
gi 256418964 2467 QKS 2469
Cdd:pfam05667 525 QKE 527
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
22-129 |
2.27e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 47.31 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 22 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 88
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 256418964 89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 129
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2181-2400 |
2.36e-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: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2181 DEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIlRDKDNTQRFLEEEAEKMKQVAEEAARLSV 2260
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2261 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM---A 2329
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaeL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 2330 QQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQ 2400
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1355-1512 |
2.37e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 49.73 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1355 AQAKAQAEL-EAQELQRRMQEEVARReEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER--SRMRIEEEIRV 1431
Cdd:pfam00529 59 ALDSAEAQLaKAQAQVARLQAELDRL-QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIdlARRRVLAPIGG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1432 V-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALrvkAEAEAAREKQRA 1509
Cdd:pfam00529 138 IsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIaEAEAELKL---AKLDLERTEIRA 214
|
...
gi 256418964 1510 LQA 1512
Cdd:pfam00529 215 PVD 217
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
17-125 |
2.45e-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: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 87
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 256418964 88 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2252-2702 |
2.47e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 50.74 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2252 AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2331
Cdd:COG4995 23 ALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALALALAAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2332 LVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2411
Cdd:COG4995 103 LAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2412 QRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKL 2491
Cdd:COG4995 183 LLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2492 EQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRE 2571
Cdd:COG4995 263 ALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2572 RLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgpsvEAEPEYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHT 2651
Cdd:COG4995 343 ALLAAALAAALALAAALALALLAALLLLL------------AALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLR 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2652 TVAELTQREDVYRYLKGRSSIAGLLLKP--TNEKLSVYTALQRQLLSPGTALI 2702
Cdd:COG4995 411 LLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2138-2379 |
2.51e-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: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2138 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGK 2217
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2218 LKARI----EAENRALILRDKDNTQRFLEEeAEKMKQVAEEAARLsVAAQEAARlrqlaeEDLAQQRALAEKMLKEKMQA 2293
Cdd:COG3883 91 RARALyrsgGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2294 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2373
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
....*.
gi 256418964 2374 AEEDAQ 2379
Cdd:COG3883 243 AASAAG 248
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1552-1947 |
2.54e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.07 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1552 ELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1631
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1632 LAQADAEKQKEEAEREARRRGKAEEQ---AVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLE 1708
Cdd:pfam19220 101 EAEAAKEELRIELRDKTAQAEALERQlaaETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1709 EELARLQH-------EATAATQKRQELEAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAAR 1780
Cdd:pfam19220 174 QENRRLQAlseeqaaELAELTRRLAELETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1781 LRALAEEAKRQRQLAEEDAARQRaeaervltEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAA 1860
Cdd:pfam19220 250 LEALTARAAATEQLLAEARNQLR--------DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1861 lhKADIEERLAQLRKA---SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAG-KAELElelgrirsnAEDTMRS 1936
Cdd:pfam19220 320 --RAELEERAEMLTKAlaaKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRlKEELQ---------RERAERA 388
|
410
....*....|.
gi 256418964 1937 KEQAELEAARQ 1947
Cdd:pfam19220 389 LAQGALEIARE 399
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2227-2423 |
2.55e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2227 RALILRDKDNTQRFLEEEAEKMKQVAEEAarLSVAAQEAARLRQLAEEDLAQQRalaekmlkEKMQAVQEatRLKAEAEL 2306
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERR--------NELQKLEK--RLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2307 LQQQKELAQEQARRLQEDKEQMAQQL--VEETQGFQRTLEAERQRQLE----MSAEAERLKLrmaeMSRAQARAEEDAQR 2380
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQqeLEKKEEELEELIEEQLQELErisgLTAEEAKEIL----LEKVEEEARHEAAV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 256418964 2381 FRKQAEEIGEklhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2423
Cdd:PRK12704 174 LIKEIEEEAK-----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1333-1847 |
2.62e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.41 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1333 ERERLAEVEAALEKQ-----RQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRsiQEELQHLRQ----- 1402
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeyKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQ--DSELAKLRVeemeq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1403 --SSEAEIQAKAQqVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQd 1480
Cdd:pfam05701 113 giADEASVAAKAQ-LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1481 esqrkrQAEAELALRVKAEAEAAREKQRALQALDELRL-------QAEEAERRLRQaEAERARQVQVALETAqrsaEVEL 1553
Cdd:pfam05701 191 ------ATKESLESAHAAHLEAEEHRIGAALAREQDKLnwekelkQAEEELQRLNQ-QLLSAKDLKSKLETA----SALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1554 QSKRASFAektAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEALRLRLQAEevaqqkSLa 1633
Cdd:pfam05701 260 LDLKAELA---AYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEK---AKDEVNCLRVAAA------SL- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1634 QADAEKQKeeaerearrrgkAEEQAVRQRELA--------EQELEKQRQLAEgTAQQRLAAEQE--------LIRLRAET 1697
Cdd:pfam05701 327 RSELEKEK------------AELASLRQREGMasiavsslEAELNRTKSEIA-LVQAKEKEAREkmvelpkqLQQAAQEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1698 EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK------ARAEEESRSTSEKSKQR-------L 1764
Cdd:pfam05701 394 EEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEklalaaIKALQESESSAESTNQEdsprgvtL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1765 EAE-----AGRFRElAEEAARLRalAEEAKRQRQLAEEDAAR---QRAEAERVLTEKLAAISEATrlkTEAEIALKEKEA 1836
Cdd:pfam05701 474 SLEeyyelSKRAHE-AEELANKR--VAEAVSQIEEAKESELRsleKLEEVNREMEERKEALKIAL---EKAEKAKEGKLA 547
|
570
....*....|.
gi 256418964 1837 ENERLRRLAED 1847
Cdd:pfam05701 548 AEQELRKWRAE 558
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1361-1520 |
2.73e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1361 AELEAQELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEeeirvvRLQlette 1440
Cdd:COG1566 74 ARLDPTDLQAALAQ--AEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQ------ALY----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1441 RQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrKRQAEAELalrvkAEAEAAREKqrALQALDELRLQA 1520
Cdd:COG1566 141 KKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQ--AELNLARTTIRA 212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2141-2590 |
2.90e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2141 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDE---ELQRLKAEVTEAARQRSQVEE---ELFSVRVQMEE 2214
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEErheLYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2215 LGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSvaaQEAARL------------------RQLAEED- 2275
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---KEIKELkkaieelkkakgkcpvcgRELTEEHr 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2276 ---LAQQRALAEKMLKEKMQAVQEATRLKAEAE----LLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAE 2346
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRelekVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2347 RQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtLEIQRQQSDHDAE-RLRE 2425
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-ERLKELEPFYNEYlELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2426 AIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKSFlSEKDSLLQRERFIEQEKakleqlfqdEVAKAK 2503
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKrlEELRKELEELEKKY-SEEEYEELREEYLELSR---------ELAGLR 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2504 qlreeqqrqqqqmeqekqelmASMEEARRRQREAEEGVR--RKQEELQHLEQQRQQQEKLLAEENQRLRERLQRL--EEE 2579
Cdd:PRK03918 680 ---------------------AELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERVEELREKVKKYkaLLK 738
|
490
....*....|.
gi 256418964 2580 HRAALAHSEIA 2590
Cdd:PRK03918 739 ERALSKVGEIA 749
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1454-1640 |
3.33e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1454 RARAEEAEAQ------KRQAQEEAerlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALDELRLQAEEAER-- 1525
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1526 -RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLreeaerraqqqaeaerare 1600
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM------------------- 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 256418964 1601 EAERELERWQLKANEALRLRLQAEEVAQQKS----LAQADAEKQ 1640
Cdd:pfam15709 472 AEEERLEYQRQKQEAEEKARLEAEERRQKEEeaarLALEEAMKQ 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2133-2457 |
3.38e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQm 2212
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2213 EELGKLKARIEAENRALILRDKDNTQRFLEEE---------------AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLa 2277
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEEL- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2278 qQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGfqrTLEAERQRQLEMSAEA 2357
Cdd:COG4717 322 -EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDEEELRAALEQAEEY 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2358 ERLKLRMAEMSR--AQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTL---------EIQRQQSDHDAERLREA 2426
Cdd:COG4717 398 QELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELreelaeleaELEQLEEDGELAELLQE 477
|
330 340 350
....*....|....*....|....*....|.
gi 256418964 2427 IAELEREKEKLKQEAKLLQLKSEEMQTVQQE 2457
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2133-2342 |
3.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSVRV 2210
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2211 QMEELGKLKARIEAENRaLILRDKDNTQRFLEEEAE---KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2287
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2288 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRT 2342
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3324-3362 |
3.73e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.47 E-value: 3.73e-05
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3324 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3362
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1691-1996 |
3.90e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1691 IRLRA-ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1763
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1764 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlteklaaiseatrlkteAEIALKEKEAENERLRR 1843
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1844 LAEDEAFQRRrleeqaalhkadieerlAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAlkvsfeKAAAGKAELELEL 1923
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA------RAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1924 grIRSNAEDTMRSKEQAELEAARQRQLaaeeeqrrreaeeRVQRSLAAEEEAARQRKVALE-EVERLKAKVEEA 1996
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKA-------------AQQQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1293-1573 |
3.93e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1293 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAELEAQELQRRM 1372
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1373 QEEVARREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGE 1449
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1450 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAARE-KQRALQALDELRLQAE- 1521
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1522 EAERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1573
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4359-4396 |
3.98e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 3.98e-05
10 20 30
....*....|....*....|....*....|....*...
gi 256418964 4359 QRFLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTA 4396
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3324-3359 |
4.10e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.10e-05
10 20 30
....*....|....*....|....*....|....*.
gi 256418964 3324 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3359
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1244-1575 |
4.15e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.01 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1244 QKFAKQYINAIKDYelqlitYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1322
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1323 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ----------ELQRRMQE-EVARREEAAVDAQQQKR 1391
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1392 SIQEELQHLRQSSEAEiQAKAQQVEAAERSRMRIEEEIR---------VVRLQLETTE------RQRGGAEGELQALRAR 1456
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEAKrradaklkeAVEKNVATSEqdkpkrRAKRGVLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1457 AEEAEAQKRQAQEEAerlrrqVQDESQR--KRQAEAElalRVKAEAEAAREKQR-------ALQALDELRLQAEEAERRL 1527
Cdd:NF033838 280 ENDAKSSDSSVGEET------LPSPSLKpeKKVAEAE---KKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKV 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1528 RQAEA----ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1575
Cdd:NF033838 351 KEAELelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2244-2403 |
4.23e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2244 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2323
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2324 DKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2403
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1173-1531 |
4.26e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1173 RQRELEQLGRQlryyRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEI----ERHGEKVEECQKFAK 1248
Cdd:pfam02029 12 RRRAREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTakreERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1249 QYINAIKDYElqlitykaqlEPVASPAKKPKVQSGSESVIQEYVDLR-TRYSELTTLTSQyikfiSETLRRMEEEERLAE 1327
Cdd:pfam02029 88 EFDPTIADEK----------ESVAERKENNEEEENSSWEKEEKRDSRlGRYKEEETEIRE-----KEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1328 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELE-AQELQRRMQEEVARREEAAVDAQqqkrsiqEELQHLRQSSEA 1406
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvKYESKVFLDQKRGHPEVKSQNGE-------EEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1407 EIQAKAQQVEAAERSRMRIEEEIRvvrlqLETTERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1485
Cdd:pfam02029 226 RQGGLSQSQEREEEAEVFLEAEQK-----LEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 256418964 1486 RQAEAElalRVKAEAEaarEKQRALQALDelRLQAEEAERRLRQAE 1531
Cdd:pfam02029 301 KQEEAE---RKLREEE---EKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1342-1522 |
4.37e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1342 AALEKQRQLAEAHAQAKAQAELEAQelQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERS 1421
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHR--LKELPAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1422 RMRIEEEIRVVRlqletTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1501
Cdd:COG1579 75 IKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|.
gi 256418964 1502 AAREKQRALQALDELRLQAEE 1522
Cdd:COG1579 150 ELAELEAELEELEAEREELAA 170
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1312-1517 |
4.37e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1312 ISETLRRMEEEERLAEQQRAEERERLAEVEAALekqrqlaeahAQAKAQAELEAQELqRRMQEEVARREEAAVDAQQQKR 1391
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1392 siqeelQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1465
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1466 -----QAQEEAERLRRQVQDESQRKrQAEAELALR--VKAEAEAAREKQRALQALDELR 1517
Cdd:COG1842 157 gidsdDATSALERMEEKIEEMEARA-EAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1378-1731 |
4.50e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1378 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1457
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1458 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1537
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1538 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1617
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1618 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1697
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 256418964 1698 EQGEQQRQLLEEELARLQHEATAATQKRQELEAE 1731
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4110-4138 |
4.53e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.53e-05
10 20
....*....|....*....|....*....
gi 256418964 4110 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4138
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1293-1572 |
4.60e-05 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 49.45 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1293 DLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-AKAQAELE-A 1365
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1366 QELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVE------AAERSRMRIEEEirVVRLQLETT 1439
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1440 ERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqaldelrl 1518
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKAREFEVEA--------- 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1519 qaeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1572
Cdd:pfam15450 453 --------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2226-2588 |
4.75e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2226 NRALILRDKDNTQRflEEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2300
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2301 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLkLRMAE 2366
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2367 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQL 2446
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2447 KSEEMQTVQQEQILQEtqalqksfLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEqqrqqqqmeqekqelmas 2526
Cdd:COG3096 505 RSQQALAQRLQQLRAQ--------LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL------------------ 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 2527 MEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSE 2588
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQ 626
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1608-1794 |
4.80e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1608 RWQLKANEALRLRLQAE----EVAQQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQR 1683
Cdd:pfam15709 335 RDRLRAERAEMRRLEVErkrrEQEEQRRLQQEQLERAEKM---------REELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1684 LAAEQELiRLRAETEQGEQQRQLLEEELARLQHE--------ATAATQKRQELEAELA---KVRAEMevllASKARAEEE 1752
Cdd:pfam15709 406 EERKQRL-QLQAAQERARQQQEEFRRKLQELQRKkqqeeaerAEAEKQRQKELEMQLAeeqKRLMEM----AEEERLEYQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 256418964 1753 SRSTSEKSKQRLEAEAGRFRElaEEAARLraLAEEAKRQRQL 1794
Cdd:pfam15709 481 RQKQEAEEKARLEAEERRQKE--EEAARL--ALEEAMKQAQE 518
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1317-1490 |
4.89e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQaeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1396
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRL-----EEERQRQEEEERKQRLQLQAAQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1397 LQHLRQsseaEIQAKAQQVE---AAERSRMRIEEEIRVVrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaer 1473
Cdd:pfam15709 428 FRRKLQ----ELQRKKQQEEaerAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE--- 496
|
170
....*....|....*..
gi 256418964 1474 lRRQVQDESQRKRQAEA 1490
Cdd:pfam15709 497 -RRQKEEEAARLALEEA 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1345-1565 |
5.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1345 EKQRQLAEAHAQ-AKAQAELEAqeLQR---RMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER 1420
Cdd:COG3883 20 AKQKELSELQAElEAAQAELDA--LQAeleELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1421 SRMR------------IEEEIRvvrlQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1488
Cdd:COG3883 98 SGGSvsyldvllgsesFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1489 EAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1565
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2141-2551 |
5.24e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2141 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSVRVQMEE 2214
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2215 LGKLKARIEAENRALI--LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2292
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2293 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRMAEM 2367
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2368 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL-KQEAKL 2443
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2444 LQLKSE----------------EMQTVQQE--------------------QILQETQALQKSFLSEKDS---LLQRERFI 2484
Cdd:PRK03918 542 KSLKKElekleelkkklaelekKLDELEEElaellkeleelgfesveeleERLKELEPFYNEYLELKDAekeLEREEKEL 621
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 2485 EQEKAKLEQLFqDEVAKAKQLREEQQRQQQQMEQEKQELmaSMEEARRRQREAEEGVRRKQEELQHL 2551
Cdd:PRK03918 622 KKLEEELDKAF-EELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEEL 685
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1451-1689 |
5.39e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1451 QALRARAEEAEAQKRQAQEEAERLRRQVqDESQRKRQA--EAELALRVKAEAEAAREKQRALQA-LDELRLQAEEAERRL 1527
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1528 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREeaerraqqqaeaerareeaerele 1607
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA------------------------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1608 rwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELA--EQELEKQRQLAEGTAQQRLA 1685
Cdd:COG3206 299 --QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEE 376
|
....
gi 256418964 1686 AEQE 1689
Cdd:COG3206 377 ARLA 380
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
21-122 |
5.67e-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: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1403-1638 |
5.83e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1403 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1480
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1481 -ESQRKRQAEAELAL------------RVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAErARQVQVALETAQR 1547
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1548 saevELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1627
Cdd:COG3883 172 ----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
250
....*....|.
gi 256418964 1628 QQKSLAQADAE 1638
Cdd:COG3883 248 GAGAAGAAGAA 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1437-1688 |
6.01e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1437 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDEL 1516
Cdd:TIGR02794 25 HSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1517 RlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaqlreEAERRAQQQAEAE 1596
Cdd:TIGR02794 105 K-QAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA---------AEAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1597 RAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaEREARRRGKAEEQAVRQRELAEQELEKQRQla 1676
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAA---AAAAEAERKADEAELGDIFGLASGSNAEKQ-- 249
|
250
....*....|..
gi 256418964 1677 EGTAQQRLAAEQ 1688
Cdd:TIGR02794 250 GGARGAAAGSEV 261
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2232-2387 |
6.10e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2232 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2308
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2309 QQKELAQEQARRLQEDKE---QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRaqaRAEEDAQRF---- 2381
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 256418964 2382 -RKQAEE 2387
Cdd:pfam15709 512 aMKQAQE 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1909-2468 |
6.10e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1909 FEKAAAGKAELELELGRIRSNAEDTMRSKEQAElEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKvalEEVER 1988
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1989 LKAKVEEARRLRERAEQEsARQLQLAQEAAQKRLqAEEKAHAFVVQQREEELQQTLQQEQNMLdRLRSEAEAARRAAEEA 2068
Cdd:PRK03918 236 LKEEIEELEKELESLEGS-KRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2069 EEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2148
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2149 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLK----------AEVTEAARQR--SQVEEELFSVRVQMEELG 2216
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKEllEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2217 KLKARIEAENRAL-ILRDKDNTQRFLEEEAEKMKQVAEE-----AARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2290
Cdd:PRK03918 473 EKERKLRKELRELeKVLKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2291 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQlEMSAEAERLKLRMAEMSRA 2370
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK-ELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2371 Q---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL------------VQTLEIQRQQSDHDAERLREAIAELEREKE 2435
Cdd:PRK03918 632 FeelAETEKRLEELRKELEELEKKYSEEEYEELREEYLelsrelaglraeLEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590
....*....|....*....|....*....|...
gi 256418964 2436 KLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2468
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1638-1995 |
6.32e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1638 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1717
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1718 ATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAE 1796
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1797 EDAARQR---AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQL 1873
Cdd:COG4372 169 LEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1874 RKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAE 1953
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 256418964 1954 EEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEE 1995
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1756-2035 |
6.37e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1756 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA-EIALKEK 1834
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1835 EAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKvsfEKAAA 1914
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE---AEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1915 GKAELELELGRIRSNAEDTMRSKEQAElEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-V 1993
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 256418964 1994 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQ 2035
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1418-1537 |
6.74e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.19 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1418 AERSRMRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvK 1497
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQER-----LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---K 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 256418964 1498 AEAEAAREKQRALQALDELRLQAEEAERRLRQaEAERARQ 1537
Cdd:pfam05672 81 AEEEAEEREQREQEEQERLQKQKEEAEAKARE-EAERQRQ 119
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1341-1841 |
7.27e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.28 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1341 EAALEKQRQLAEAhAQAKAQAELeAQELQRRMQEeVARREEAAVDAQQQKRSIQE---ELQHLRQSSEAEiqakaqqvea 1417
Cdd:PRK10929 25 EKQITQELEQAKA-AKTPAQAEI-VEALQSALNW-LEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1418 aersrmriEEEIRVVRLQLETterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRRQVQDESQ-RKRQAEAELALrv 1496
Cdd:PRK10929 92 --------RDEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAREISDSLSQlPQQQTEARRQL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1497 kAEAEaarekqRALQALDELRLQAEEAERRLRQAEAerarqvqvaletAQRSAEVElqskrasfaektaqlertlqeehv 1576
Cdd:PRK10929 154 -NEIE------RRLQTLGTPNTPLAQAQLTALQAES------------AALKALVD------------------------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1577 tvaqlreeaerraqqqaeaerareeaerELERWQLKAN---EALRLRLqaeEVAQQKSlAQADAEKQKEeaerearrrgK 1653
Cdd:PRK10929 191 ----------------------------ELELAQLSANnrqELARLRS---ELAKKRS-QQLDAYLQAL----------R 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1654 AEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQHEATAATQK-RQELEA-- 1730
Cdd:PRK10929 229 NQLNSQRQRE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlr 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1731 ----ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRA 1804
Cdd:PRK10929 307 eqsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTA 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1805 EAERVLTEKLAA---------------ISEATRLK---TEAEIALKE-KEAENERL 1841
Cdd:PRK10929 376 EQNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1513-1979 |
7.42e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 49.25 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1513 LDELRLQAEEAERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQ 1591
Cdd:COG3903 470 LETVREYAAERLAEAGERAAARRRHADYYLALAERaAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1592 QAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEkqkeeaeREARRRGKAEEQAVRQRELAEQELEK 1671
Cdd:COG3903 550 ALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAAR-------AAAAAAAAAAAAAAAAAAAAAAAAAA 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1672 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEE 1751
Cdd:COG3903 623 LLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAA 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1752 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIAL 1831
Cdd:COG3903 703 LAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1832 KEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEK 1911
Cdd:COG3903 783 AAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAA 862
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1912 AAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR 1979
Cdd:COG3903 863 AAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAA 930
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
4-119 |
7.42e-05 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.73 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 4 SRAIQHeisSLKDErdrvQKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EK 70
Cdd:cd21292 14 SEGTTH---SYSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKK 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 256418964 71 GRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21292 87 KLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2132-2350 |
8.12e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2132 LKQKQAA-DAEMEKHKKFAE-QTLRQ-KAQVEQELTTLRLQLEETDHQksildeelqrlkAEVTEAARQRSQVEEELFSV 2208
Cdd:NF012221 1551 AKQDDAAqNALADKERAEADrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2209 RVQMEELGKlkaRIEA----------------ENRALILRDK-----DNTQRFLEEEAEKMKQ--------VAEEAARLS 2259
Cdd:NF012221 1619 TKELTTLAQ---GLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSE 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2260 VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlveETQGF 2339
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAKGA 1772
|
250
....*....|.
gi 256418964 2340 QRTLEAERQRQ 2350
Cdd:NF012221 1773 KQDESDKPNRQ 1783
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1439-2041 |
8.15e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1439 TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ--VQDESQRKRQA--EAELALRVKAEAEAARE--------- 1505
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLdeLQQEASRRQQAlqQALAAEEKAQPQLAALSlaqparqlr 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1506 -----KQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTL---QEEHVT 1577
Cdd:PRK10246 294 phwerIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLAEHDRFRqwnNELAGW 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1578 VAQLREEAERRAQQQAEAERAREEaereleRWQLKANEALRLRLQAEEVAQqkslAQADAEKQKEEAEREARRRGKAEEQ 1657
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQQLTHA------EQKLNALPAITLTLTADEVAA----ALAQHAEQRPLRQRLVALHGQIVPQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1658 AVRQRELAE------QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgEQQRQLLEEELARLQ------------HEAT 1719
Cdd:PRK10246 439 QKRLAQLQVaiqnvtQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ-EARIKDLEAQRAQLQagqpcplcgstsHPAV 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1720 AATQ---------KRQELEAELAK-------VRAEMEVLLASKARAEEESRSTSEKSK------QRLEAEAGRFRELAEE 1777
Cdd:PRK10246 518 EAYQalepgvnqsRLDALEKEVKKlgeegaaLRGQLDALTKQLQRDESEAQSLRQEEQaltqqwQAVCASLNITLQPQDD 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1778 AARLRALAEEAKRQ-RQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIA-----LKEKEAENERLRRLAEDEAFQ 1851
Cdd:PRK10246 598 IQPWLDAQEEHERQlRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltLPQEDEEASWLATRQQEAQSW 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1852 RRRLEEQAALhkadiEERLAQLRKASESELERQKGLVED---TLRQRRQVEEEIMALKvsfEKAAAGKAELELELGRIrs 1928
Cdd:PRK10246 678 QQRQNELTAL-----QNRIQQLTPLLETLPQSDDLPHSEetvALDNWRQVHEQCLSLH---SQLQTLQQQDVLEAQRL-- 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1929 naedtmrSKEQAELEAARQrqlaaeeeqrrREAEERVQRSLAA-EEEAARQRKVALEEveRLKAKVEEARRLRERAEQES 2007
Cdd:PRK10246 748 -------QKAQAQFDTALQ-----------ASVFDDQQAFLAAlLDEETLTQLEQLKQ--NLENQRQQAQTLVTQTAQAL 807
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 256418964 2008 ARQLQLAQEAAQKRLQAE--EKAHAFVVQQ------REEELQ 2041
Cdd:PRK10246 808 AQHQQHRPDGLDLTVTVEqiQQELAQLAQQlrenttRQGEIR 849
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3771-3807 |
8.24e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.24e-05
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 3771 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3807
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2665-2703 |
9.02e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 42.31 E-value: 9.02e-05
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 2665 YLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALIL 2703
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1321-2039 |
9.06e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1321 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1396
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1397 LQHLR-QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQ-----LETTERQRGGAEGELQALRARAEEAEAQKRQAQEE 1470
Cdd:PRK04863 378 QEENEaRAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1471 AERLRRQVQDESQRKRQAE--AELALRVKAEAEAAREKQRALQALDELRLQAEEAER----RLRQAEAERARQVQVALET 1544
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1545 AQRSAEVELQSK--RASFAEK-TAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWqLKANEALRlRL 1621
Cdd:PRK04863 538 LLAEFCKRLGKNldDEDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA-RL 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1622 QAEEVAQQKSLAQADAEKQKEEAERearrrgKAEEQAVRQRELAEQELEKQ-RQLaegtaQQRLAAEQELIRLRAETEQG 1700
Cdd:PRK04863 616 REQSGEEFEDSQDVTEYMQQLLERE------RELTVERDELAARKQALDEEiERL-----SQPGGSEDPRLNALAERFGG 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1701 EQQRQL-----LEEE------LARLQH--------EATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK 1761
Cdd:PRK04863 685 VLLSEIyddvsLEDApyfsalYGPARHaivvpdlsDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIA 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1762 QRlEAEAGRFRE--LAEEAARlRALAEEAKRQRQLAEEDAARQRAEAERVLT-----EKLAAISEATRLKTEAEIALKEK 1834
Cdd:PRK04863 765 DR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDVQKLQRlhqafSRFIGSHLAVAFEADPEAELRQL 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1835 EAE-NERLRRLAEDEAfqrrrLEEQAALHKADIEERLAQLRK-ASESELerqkgLVEDTLRQR-RQVEEEIMALkvsfEK 1911
Cdd:PRK04863 843 NRRrVELERALADHES-----QEQQQRSQLEQAKEGLSALNRlLPRLNL-----LADETLADRvEEIREQLDEA----EE 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1912 AAA-----GKA--ELELELGRIRSNAEDTMRSKEQaeLEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAlE 1984
Cdd:PRK04863 909 AKRfvqqhGNAlaQLEPIVSVLQSDPEQFEQLKQD--YQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNS-D 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1985 EVERLKAKVEEARRLRERA-EQESARQLQLAQ-------------------EAAQKRLQ---------AEEKA------- 2028
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRArEQLRQAQAQLAQynqvlaslkssydakrqmlQELKQELQdlgvpadsgAEERArarrdel 1065
|
810
....*....|...
gi 256418964 2029 HAFVV--QQREEE 2039
Cdd:PRK04863 1066 HARLSanRSRRNQ 1078
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
159-236 |
1.08e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.22 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 159 DNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 236
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3658-3694 |
1.08e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 3658 RYLYGTGAVAGVYLPGSRQTLTIYQALKKGLLSAEVA 3694
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2154-2585 |
1.16e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2154 RQKAQVEQELTTLRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2230
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2231 LRDKDNTQRFLEEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2309
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2310 QKELAQEQARRLQEDKEQMAQQLVEE--TQGFQ----RTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRK 2383
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERmsAKGLQmelsRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2384 QAEEIG----------EKLHRTELATQEKVTLVQTleiqRQQSDHDAERLREAIAELEREKEKLKQEAKLL--------- 2444
Cdd:pfam07111 427 AVARIPslsnrlsyavRKVHTIKGLMARKVALAQL----RQESCPPPPPAPPVDADLSLELEQLREERNRLdaelqlsah 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2445 -----------QLKSEEMQTV----QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQ-LFQDEVAKAKQLREE 2508
Cdd:pfam07111 503 liqqevgrareQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2509 QQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQ----EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAL 2584
Cdd:pfam07111 583 VAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLML 662
|
.
gi 256418964 2585 A 2585
Cdd:pfam07111 663 A 663
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1769-2015 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1769 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1848
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1849 AFQRRRLEEQAALHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELE 1922
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1923 LGRIRSNAEDTMRSKEQAELEAARQRQLaaeeeQRRREAEERVQRSLAAEEEAARQRKVALEE-VERLKAKVEEARRLRE 2001
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQK-----LTTAHRKEAENEALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 256418964 2002 RAEQESAR-QLQLAQ 2015
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1652-2030 |
1.38e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.09 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1652 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQHEATAATQK 1724
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1725 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1799
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1800 ARQRAEAERvlteklaaiSEATRL---KTEAEIALKE-KEAENERLRRLAED-----EAFQRRRLEEQAALHKADIEERL 1870
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAEEEaKRRADAKLKEAVEKnvatsEQDKPKRRAKRGVLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1871 AQLRKASESELERQKgLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAE------------LELELgrirsnAEDTMRSKE 1938
Cdd:NF033838 280 ENDAKSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEI------AESDVKVKE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1939 qAELEAARQRqlaaeeeqrrreaeervqrslAAEEEAARQRKVALEEVERLKA---KVEEARRLRERAEQESARQLQLAQ 2015
Cdd:NF033838 353 -AELELVKEE---------------------AKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEED 410
|
410
....*....|....*
gi 256418964 2016 EAAQKRLQAEEKAHA 2030
Cdd:NF033838 411 KVKEKPAEQPQPAPA 425
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3940-3974 |
1.40e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|....*
gi 256418964 3940 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3974
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2154-2358 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2154 RQKAQVEQELTTLRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIl 2231
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2232 rDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQEATRLKAEAELLQQQK 2311
Cdd:COG3206 261 -QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEAELEALQAREASLQAQL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 256418964 2312 ELAQEQARRLQEdKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAE 2358
Cdd:COG3206 337 AQLEARLAELPE-LEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1454-1724 |
1.42e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1454 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaeaELALRVKAEAEAAREKQRAlqaldELRLQAE----EAERRLRQ 1529
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKA-----EERREAEtaraEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1530 AEAERARQVQVALETAQRSAEVELQSKRAsfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeaerelerw 1609
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEA--------------------------------------------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1610 qlkanealrLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTAQQRLAAeqe 1689
Cdd:COG2268 300 ---------EREEAELEADVRKPAEAEKQAAE-------------------AEAEAEAEAIRAKGLAEAEGKRALAE--- 348
|
250 260 270
....*....|....*....|....*....|....*.
gi 256418964 1690 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQK 1724
Cdd:COG2268 349 -----AWNKLGDAAILLmLIEKLPEIAEAAAKPLEK 379
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1333-1554 |
1.44e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1333 ERERLAEVEAALEKQRQLAEAHAQAKAQAE---LEAQELQRRMQEEVarreeaavdaqqqkRSIQEELQHLRQSSEAEIQ 1409
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQqlrTELQELEAQQQEEA--------------ESSREQLQELEEQLATERS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1410 AKaqqvEAAERSRMRIEEEIRVVRLQLETTERQRggaegelqalraraeeaEAQKRQAQEEAERLRRQVQDESQRKRQaE 1489
Cdd:pfam09787 108 AR----REAEAELERLQEELRYLEEELRRSKATL-----------------QSRIKDREAEIEKLRNQLTSKSQSSSS-Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1490 AELALRVKAEAEAAREKQRALQAL----DELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1554
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALstekNSLVLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLR 234
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1326-1440 |
1.44e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1326 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ---AKAQAELEAQELQRRM---------QEEVARREEAAVDAQQQKRSI 1393
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 256418964 1394 QEELQHLRQSSEAEiqakaQQVEAAERSRMRIEEEIRVVRLQLETTE 1440
Cdd:COG1566 168 QAQLAQAQAGLREE-----EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2156-2583 |
1.47e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2156 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEaENRALILRDK 2234
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2235 DNTQRFLEEEAEKMKQVAEEAARLSVAAQEAArLRQLAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQQQ 2310
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2311 KELAQEQARRLQEDkeqmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2390
Cdd:PRK02224 351 ADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2391 KLH--RTELAT-QEKVTLVQTL-----------EIQRQQSDHDAERLREAIAELEREKEKLKQ-----EAKLLQLKSEEM 2451
Cdd:PRK02224 427 REAelEATLRTaRERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEeveevEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2452 QTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQ---EKAKLEQLFQD--EVAKAKQLREEQQRQQQQMEQEKQELMAS 2526
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEElreRAAELEAEAEEkrEAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2527 MEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQR---LEEEHRAA 2583
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERkreLEAEFDEA 646
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2303-2588 |
1.60e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2303 EAELLQQQKELAQEQA----RRLQEDKEQMAQQLVEETQGfQRTLEAERQRQLEMS-----AEAERLKLRMAEMSRAQAR 2373
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2374 AEEDAQRFRKQAEEI-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDhdaERLREAIAELEREKEKLKQEAKLLQLKSEEM 2451
Cdd:pfam17380 346 RERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2452 QTVQQEQILQETQALQKsflsekdslLQRERFIEQEKAKLEQLfqdevakakqlreeqqRqqqqmEQEKQELMASMEEAR 2531
Cdd:pfam17380 423 EQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E-----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 2532 RRQREAEEGVRRKQ----EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSE 2588
Cdd:pfam17380 473 KRKKLELEKEKRDRkraeEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2132-2434 |
1.60e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.37 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2132 LKQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSVRVQ 2211
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2212 MEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2290
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2291 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRT---LEAERQRQLEMSAEAERLKLRMAEM 2367
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 2368 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLREaiaELEREK 2434
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3734-3770 |
1.67e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.67e-04
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 3734 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPAEEA 3770
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2133-2580 |
1.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETdhqKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2212
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2213 EELGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2287
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSN-----IPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2288 ------KEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQED-----------------KEQMAQQL----VEETQ 2337
Cdd:COG4913 489 ltllvpPEHYAAALRWvnrLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcVDSPE 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2338 GFQRT--------------------------------LEAERQRQ-LEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2384
Cdd:COG4913 569 ELRRHpraitragqvkgngtrhekddrrrirsryvlgFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERRE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2385 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---SDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQ 2461
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2462 ETQALQK--SFLSEKDSLLQRERFIEQekakLEQLFQDEVAKAKQLREEqqrqqqqmeqekqelmASMEEARRRQREAEE 2539
Cdd:COG4913 728 ELDELQDrlEAAEDLARLELRALLEER----FAAALGDAVERELRENLE----------------ERIDALRARLNRAEE 787
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 256418964 2540 GVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2580
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2160-2389 |
1.73e-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: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2160 EQELTTLRLQLEE----TDHQKSILDEELQRLKAEVTEAARQRS-----QVEEELFSVRVQMEELGKLKARI-EAENRal 2229
Cdd:COG3096 450 EQQATEEVLELEQklsvADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRLQQLRAQLaELEQR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2230 iLRDKDNTQRFLEEEAEKMKQVAEEAARLsvaaqeaarlrqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2309
Cdd:COG3096 528 -LRQQQNAERLLEEFCQRIGQQLDAAEEL--------------EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2310 Q-KEL---------AQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQ 2379
Cdd:COG3096 593 RiKELaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
250
....*....|
gi 256418964 2380 RFRKQAEEIG 2389
Cdd:COG3096 673 RLLALAERLG 682
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2133-2445 |
1.81e-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: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 KQKQAADAE---MEKHKKFAEQTLRQKAqVEQEL-----------TTLRLQlEETDHQKSILDEELQRLKAE---VTEAA 2195
Cdd:COG3096 297 ARRQLAEEQyrlVEMARELEELSARESD-LEQDYqaasdhlnlvqTALRQQ-EKIERYQEDLEELTERLEEQeevVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2196 RQRSQVEEELFSVRVQMEELGKLKARI-----EAENRAL----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA 2266
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYqqaldVQQTRAIqyqqAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2267 RLR-----QLAEEDLAQQR-----ALAEKMLKE--KMQAVQEATRL-------KAEAELLQQ---------QKELAQEQA 2318
Cdd:COG3096 455 EEVleleqKLSVADAARRQfekayELVCKIAGEveRSQAWQTARELlrryrsqQALAQRLQQlraqlaeleQRLRQQQNA 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2319 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE---EIGEKLHRT 2395
Cdd:COG3096 535 ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPawlAAQDALERL 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2396 ELATQEKVTLVQTLEIQRQQSdhdAERLREAIAE---LEREKEKLKQEAKLLQ 2445
Cdd:COG3096 615 REQSGEALADSQEVTAAMQQL---LEREREATVErdeLAARKQALESQIERLS 664
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4249-4282 |
1.90e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.90e-04
10 20 30
....*....|....*....|....*....|....
gi 256418964 4249 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4282
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1355-1836 |
1.99e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1355 AQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrl 1434
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1435 QLETTERQRGGAEgelqalRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALD 1514
Cdd:COG3064 78 KLAEAEKAAAEAE------KKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1515 ELRLQAEEAERRlrqAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAE 1594
Cdd:COG3064 152 AEAEAARAAAAA---AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1595 AERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1674
Cdd:COG3064 229 SREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1675 LAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1754
Cdd:COG3064 309 GAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1755 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1834
Cdd:COG3064 389 AGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKA 468
|
..
gi 256418964 1835 EA 1836
Cdd:COG3064 469 VA 470
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2136-2296 |
2.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2136 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQmEEL 2215
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2216 GKLKARIEAENRALILRDKDnTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2295
Cdd:COG1579 92 EALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
.
gi 256418964 2296 E 2296
Cdd:COG1579 171 K 171
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1365-1537 |
2.34e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.77 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1365 AQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqSSEAEIQAKAQQVeaaersrmrieeeirvvrlqlETTERQRG 1444
Cdd:COG3524 175 REDAVRFAEEEVERAEERLRDAREALLAFRNRNGIL--DPEATAEALLQLI---------------------ATLEGQLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1445 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeaarekQRALQALDELRLQAEEAE 1524
Cdd:COG3524 232 ELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSL------------ASLLAEYERLELEREFAE 299
|
170
....*....|....*
gi 256418964 1525 RRLRQAEA--ERARQ 1537
Cdd:COG3524 300 KAYTSALAalEQARI 314
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2136-2592 |
2.36e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2136 QAADAEMEKHKKFAEQTLRQKAQVEQElTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEEL 2215
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2216 GKLKARIEAEnralilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2295
Cdd:TIGR00618 427 AHAKKQQELQ------------QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2296 EATRLKAEAELLQQQkELAQEQAR----------RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2365
Cdd:TIGR00618 495 RLLELQEEPCPLCGS-CIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2366 EMSRAQARAEEDAQRFRKQAEEIgekLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2445
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2446 LKSEEMQ----------TVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQ 2515
Cdd:TIGR00618 651 LQLTLTQervrehalsiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2516 MEQEKQELMA---SMEEARRRQRE-----AEEGVRRKQE---------ELQHLEQQRQQQEKLLAEENQRLRErlqrLEE 2578
Cdd:TIGR00618 731 GSDLAAREDAlnqSLKELMHQARTvlkarTEAHFNNNEEvtaalqtgaELSHLAAEIQFFNRLREEDTHLLKT----LEA 806
|
490
....*....|....
gi 256418964 2579 EHRAALAHSEIATT 2592
Cdd:TIGR00618 807 EIGQEIPSDEDILN 820
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1447-1581 |
2.38e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 46.67 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1447 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERR 1526
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1527 LRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVTVAQL 1581
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2147-2595 |
2.52e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2147 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAEN 2226
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2227 RALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2306
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2307 LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2386
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2387 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2466
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2467 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQE 2546
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 256418964 2547 ELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAA 2595
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1348-1717 |
2.70e-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: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1348 RQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQ---QQKRSIQEELQHLRQSSEAEIQAKAQQVEA-AERSRM 1423
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMmeeERERALEEEEEKEEERKEERKRYRQELEEQiEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1424 RIEEEirvvrlqlettERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1503
Cdd:pfam13868 89 RQEEY-----------EEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1504 REKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQrsaevelqskrasfAEKTAQLERTLQEEHvtvaqlre 1583
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK--------------AERDELRAKLYQEEQ-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1584 eaerraqqQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1663
Cdd:pfam13868 216 --------ERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1664 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1717
Cdd:pfam13868 288 RLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1754-1902 |
2.84e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1754 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1832
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256418964 1833 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1902
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2152-2384 |
2.92e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2152 TLRQKAQVEQELTTLRLQleetdhQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIL 2231
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2232 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2305
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 2306 LLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2384
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1628-1774 |
3.03e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.97 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1628 QQKSLAQA--DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQR 1704
Cdd:pfam17045 101 QRKQLKEAreEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1705 QLLEEELARLQH-----EATAATQKRQELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1774
Cdd:pfam17045 181 QCLEASQSEIQRlrsklERAQDSLCAQELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1653-1876 |
3.13e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1724
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1725 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE-EAKRQRQLAEEDAARQR 1803
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARaKAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1804 AEAERVLTEKL-AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAlhKADIEERLAQLRKA 1876
Cdd:PRK05035 607 VAEVDPKKAAVaAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQ--ANAEPEEAEDPKKA 678
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1744-1943 |
3.18e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1744 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLTEKLAAISEATRL 1823
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1824 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIM 1903
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 256418964 1904 ALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1943
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1773-2008 |
3.67e-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: 46.30 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1773 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAeneRLRRLAEDEAFQR 1852
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1853 RRLEEQaalhKADIEERLAQLRKASE-------------SELERQKGLVEDTLRQRRqveEEIMALKVSFEKAAAGKAEL 1919
Cdd:COG4942 97 AELEAQ----KEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1920 ELELGRIRSNAEDtmRSKEQAELEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVAL-EEVERLKAKVEEARR 1998
Cdd:COG4942 170 EAERAELEALLAE--LEEERAALEALKAER-------------QKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
|
250
....*....|
gi 256418964 1999 LRERAEQESA 2008
Cdd:COG4942 235 EAAAAAERTP 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2133-2337 |
3.78e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 KQKQAaDAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR----------S 2199
Cdd:PRK11281 50 KQKLL-EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslrqleS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2200 QVEE-------------------------------ELFSVRVQMEELGKLKARIEAENRALI--LRDKDNT-QRFLEEEA 2245
Cdd:PRK11281 129 RLAQtldqlqnaqndlaeynsqlvslqtqperaqaALYANSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAeQALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2246 EKMKQVAEEAARLSVAAQE-----AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAElLQQQKELAQEQARR 2320
Cdd:PRK11281 209 DLQRKSLEGNTQLQDLLQKqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAAR-IQANPLVAQELEIN 287
|
250
....*....|....*..
gi 256418964 2321 LqedkeQMAQQLVEETQ 2337
Cdd:PRK11281 288 L-----QLSQRLLKATE 299
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1300-1539 |
3.99e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 46.90 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1300 ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAELeaQELQRRMQE-EVAR 1378
Cdd:pfam13779 517 ELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEM-TQQDLQRMLDRIEELARSGRRAEAQQML--SQLQQMLENlQAGQ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1379 REEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAL 1453
Cdd:pfam13779 594 PQQQQQQGQSEMQQAMDELGDLLReqqqlLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEAL 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1454 RARAEEAEAQKRQAQEEAERLRRQVQ-DESQRKRQA-----EAELALRVKAEAEAAREKQRALQALdelrlqaEEAERRL 1527
Cdd:pfam13779 674 GDLAERQQALRRRLEELQDELKELGGkEPGQALGDAgramrDAEEALGQGDLAGAVDAQGRALEAL-------RKGAQQL 746
|
250
....*....|..
gi 256418964 1528 RQAEAERARQVQ 1539
Cdd:pfam13779 747 AEAMQQQQGQGQ 758
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1386-1587 |
4.13e-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: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1386 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmRIEEEIRVVRLqletteRQRGGAEGELQALRARAEEAEAQKR 1465
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ---RAAEQARQKEL------EQRAAAEKAAKQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1466 QAQEEAErlrrqvQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERrlrQAEAERArqvqvALETA 1545
Cdd:TIGR02794 120 QAEEAKA------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK---KAEAEAK-----AKAEA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 256418964 1546 QRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAER 1587
Cdd:TIGR02794 186 EAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1677-2026 |
4.20e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1677 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1756
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1757 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEA 1836
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1837 ENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGK 1916
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1917 AELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEA 1996
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350
....*....|....*....|....*....|
gi 256418964 1997 RRLRERAEQESARQLQLAQEAAQKRLQAEE 2026
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAE 462
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1396-1544 |
4.58e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQA-------- 1467
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1468 -QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALET 1544
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
989-1482 |
4.64e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 989 DPARECAQRIAEQQKAQAE-VEGLGKGVARLSAEAEKV-LALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLK-- 1064
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIkMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNka 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1065 --TISLVIR----STQGAEEVLKTHEEQLKEAQavpatlQELEATKASLKKLRAQAEAQQPVFNTLRDELrgaqevgERL 1138
Cdd:pfam05483 344 kaAHSFVVTefeaTTCSLEELLRTEQQRLEKNE------DQLKIITMELQKKSSELEEMTKFKNNKEVEL-------EEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1139 QQRHGERDV---EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQL-------RYYRESADPLSAWLQDAKRRQEQI 1208
Cdd:pfam05483 411 KKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1209 QAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK------KPKVQS 1282
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1283 GSESVIQEYVDLRTRYSELTTLTS------QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHA 1355
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKlELELASAKQ 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1356 QAKA-----QAELEAQEL-QRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRmriEEEI 1429
Cdd:pfam05483 651 KFEEiidnyQKEIEDKKIsEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1430 RVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1482
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1660-1950 |
4.82e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1660 RQREL------AEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqheataatqkrQELEAelA 1733
Cdd:COG0497 142 AQRELldafagLEELLEEYREAY----RAWRALKKELEELRADEAERARELDLLRFQL--------------EELEA--A 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1734 KVRAEMEVLLaskaraEEEsrstseksKQRLEAeAGRFRELAEEAarLRALAEEakrqrqlaEEDAARQRAEAERVLtEK 1813
Cdd:COG0497 202 ALQPGEEEEL------EEE--------RRRLSN-AEKLREALQEA--LEALSGG--------EGGALDLLGQALRAL-ER 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1814 LAAISE-----ATRLkTEAEIALKEKEAEnerLRRLAEDEAFQRRRLEEqaalhkadIEERLAQLRKaseseLERQKGL- 1887
Cdd:COG0497 256 LAEYDPslaelAERL-ESALIELEEAASE---LRRYLDSLEFDPERLEE--------VEERLALLRR-----LARKYGVt 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 1888 VEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAED--TMRSKEQAELEAARQRQL 1950
Cdd:COG0497 319 VEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKlsAARKKAAKKLEKAVTAEL 383
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1315-1491 |
4.83e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1315 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---------LAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD 1385
Cdd:PRK12678 45 GMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRaaraaaaarQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1386 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKR 1465
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREER 196
|
170 180
....*....|....*....|....*.
gi 256418964 1466 QAQEEAERLRRQVQDESQRKRQAEAE 1491
Cdd:PRK12678 197 GRDGDDRDRRDRREQGDRREERGRRD 222
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3360-3395 |
4.88e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.88e-04
10 20 30
....*....|....*....|....*....|....*.
gi 256418964 3360 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3395
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2703-2736 |
4.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.97e-04
10 20 30
....*....|....*....|....*....|....
gi 256418964 2703 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2736
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2156-2340 |
5.21e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2156 KAQVEQELTTLRLQLEETDHQKsiLDEELQRLKAEVTEAarqrsqVEEELFSV----RVQMEELGKLKARIEAENRALIl 2231
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKR--CQALLQELSAPLEEK------ISQGSYSVpggyQLYLEDREKLVEKYRQVPRKGV- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2232 RDKDNTQRFLEEEA--------------EKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKM 2291
Cdd:cd16269 167 KAEEVLQEFLQSKEaeaeailqadqaltEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKM 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 256418964 2292 QavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLVEETQGFQ 2340
Cdd:cd16269 247 E--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1676-2172 |
5.26e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.39 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1676 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV----------RAEMEVLLAS 1745
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1746 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKT 1825
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1826 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAL 1905
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1906 KVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE 1985
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1986 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAA 2065
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2066 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2145
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 256418964 2146 KKFAEQTLRQKAQVEQELTTLRLQLEE 2172
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1041-1257 |
5.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1041 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATKASLkklraqaEAQQPV 1120
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1121 FNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLSAWLQD 1200
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1201 AKRRQEQIQAVPiancQAAREQLRQE-KALLEEIERHGEKVEEC-QKFAKQYINAIKDY 1257
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1653-1796 |
5.38e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEATAATQKRQELEAE 1731
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1732 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALAE-EAKRQRQLAE 1796
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNElEIAKAKELADiEATKFERIVE 795
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2991-3028 |
5.38e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.38e-04
10 20 30
....*....|....*....|....*....|....*...
gi 256418964 2991 RQALRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVA 3028
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
991-1683 |
5.43e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 991 ARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISLVI 1070
Cdd:PRK10246 256 QQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1071 RSTQGAEEVLKTHEEQLKEAQAVPATLQELeatkaslkklrAQAEAQQPVFNTLRDELRG-----AQEVGERLQQRhger 1145
Cdd:PRK10246 319 RLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR---- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1146 dveveRWRERVTQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLSAWLQDAKRRQEQIQAvpiANCQAAR 1220
Cdd:PRK10246 384 -----QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNVTQ 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1221 EQLRQEKALLEEIERHGEKVEE-------CQKFAKqyinaIKDYElqliTYKAQLEPvASPAkkPKVQSGSESVIQEYVD 1293
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLE----AQRAQLQA-GQPC--PLCGSTSHPAVEAYQA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1294 LRtryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQaelEAQELQRRMQ 1373
Cdd:PRK10246 523 LE----------------PGVNQSRLDALEKEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQ---EEQALTQQWQ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1374 EEVARREEAAVDAQQQKRSIQEELQHLRQ----SSEAEIQAkaqQVEAAERSRMRIEEEIRVVRLQLETTERQrggaege 1449
Cdd:PRK10246 583 AVCASLNITLQPQDDIQPWLDAQEEHERQlrllSQRHELQG---QIAAHNQQIIQYQQQIEQRQQQLLTALAG------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1450 lQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA-LRVKAEAEAAREKQRALQALDELR--------LQA 1520
Cdd:PRK10246 653 -YALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTpLLETLPQSDDLPHSEETVALDNWRqvheqclsLHS 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1521 E-EAERRLRQAEAERARQVQVALETAqrsaeveLQSKRasFAEKTAQLERTLQEEhvTVAQLREEAERRAQQQAEAERAR 1599
Cdd:PRK10246 732 QlQTLQQQDVLEAQRLQKAQAQFDTA-------LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLV 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1600 EEAERELERWQLKANEALRLRLQAEEVAQQksLAQadaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGT 1679
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQE--LAQ---------------LAQQLRENTTRQGEIRQQ----LKQDADNR 859
|
....
gi 256418964 1680 AQQR 1683
Cdd:PRK10246 860 QQQQ 863
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2664-2700 |
5.54e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.54e-04
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 2664 RYLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTA 2700
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1525-1846 |
5.61e-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: 45.68 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1525 RRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAER 1604
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1605 ELERWQLKANEALRLRLQAEevaQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegtaqqRL 1684
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREE---IDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI--------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1685 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRsTSEKSKQRL 1764
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER-RLAEEAERE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1765 EAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRL 1844
Cdd:pfam13868 260 EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
..
gi 256418964 1845 AE 1846
Cdd:pfam13868 340 KE 341
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1406-1539 |
6.03e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.05 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1406 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1485
Cdd:PRK12678 53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1486 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQ 1539
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAE 186
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2220-2588 |
6.05e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2220 ARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLS-------VAAQEAARLRQLAEEDLAQQRAL--AEKMLKEK 2290
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNeaesdleQDYQAASDHLNLVQTALRQQEKIerYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2291 MQAVQEATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLklrMAEMS 2368
Cdd:PRK04863 361 EERLEEQNEVVEEA---DEQQEENEARAEAAEEEVDELKSQLADYQQALdvQQTRAIQYQQAVQALERAKQL---CGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2369 RAQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVQTLeiqRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKS 2448
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEEL----LSLEQKLSVAQAA---HSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2449 EEMQTVQQEQILQETQALQKSFLSEKDSllqrERFIEQEKAKLEQLFQDEvakakqlreeqqRQQQQMEQEKQELMASME 2528
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDE------------DELEQLQEELEARLESLS 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2529 EARRRQREAEEGVRRKQEelqhleqqrqQQEKLLAEENQR------LRERLQRLEEEHRAALAHSE 2588
Cdd:PRK04863 572 ESVSEARERRMALRQQLE----------QLQARIQRLAARapawlaAQDALARLREQSGEEFEDSQ 627
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
938-1366 |
6.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 938 RHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEAcetrtvhrlrlpldkdpARECAQRIAEQQKAQAEVEGLGKGVAR 1017
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEK-----------------LLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1018 LSAEAEKVLALPEpspAAPTLRSELELTLGKLEQVRSLSAiyLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQavpatl 1097
Cdd:COG4717 151 LEERLEELRELEE---ELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQ------ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1098 QELEATKASLKKLRAQAEAQQPvFNTLRDELRGAQEVGERL-----QQRHGERDVEV------------------ERWRE 1154
Cdd:COG4717 220 EELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALLallglGGSLLSLILTIagvlflvlgllallflllAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1155 RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRE-SADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQE-KALLEE 1232
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1233 IerHGEKVEECQKFAKQYiNAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFI 1312
Cdd:COG4717 379 A--GVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1313 SET---LRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ 1366
Cdd:COG4717 456 AELeaeLEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1310-1569 |
6.16e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1310 KFISETLR----RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQR-RMQEEVARREEAAV 1384
Cdd:pfam05667 250 KRIAEQLRsaalAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAaTSSPPTKVETEEEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1385 DAQQQK--RSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaegelQALRARA-EEAE 1461
Cdd:pfam05667 330 QQQREEelEELQEQLEDL----ESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ--------YKVKKKTlDLLP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1462 aqkrQAQEEAERLRRQVQDESQRKrqaeAELAlrvkAEAEAAR----EKQRALQalDELRLQAEEAERRLRQAEAERaRQ 1537
Cdd:pfam05667 398 ----DAEENIAKLQALVDASAQRL----VELA----GQWEKHRvpliEEYRALK--EAKSNKEDESQRKLEEIKELR-EK 462
|
250 260 270
....*....|....*....|....*....|..
gi 256418964 1538 VQVALEtaqrsaevELQSKRASFAEKTAQLER 1569
Cdd:pfam05667 463 IKEVAE--------EAKQKEELYKQLVAEYER 486
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2419-2547 |
6.20e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2419 DAERLREAIAELEREKEKLKQEAKLLqlkseemqtvqqEQILQETQALQKSFLSEKDSLLQRErfiEQEKAKLEQLFQDE 2498
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 256418964 2499 VAKAKQLREEQQRQQQQMEQEKQELMAS--MEEARRRQREAEEGVRRKQEE 2547
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAheLIEARKRLNKANEKKEKKKKK 629
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3659-3697 |
6.31e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.00 E-value: 6.31e-04
10 20 30
....*....|....*....|....*....|....*....
gi 256418964 3659 YLYGTGAVAGVYLPGSRQTLTIYQALKKGLLSAEVARLL 3697
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1424-1569 |
6.77e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1424 RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1503
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1504 REKQRAL-----QALDELRLQAEEAERRLRQAEAERaRQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1569
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKK-DTLKARAKAAKAQEKVNEALSGIDSDDATSALER 169
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1041-1575 |
6.95e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1041 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKthEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPV 1120
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE--EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1121 FNTLRDELRgaQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ-LGRQLRYYRESADPLSAWLQ 1199
Cdd:pfam02463 472 DLLKETQLV--KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1200 DAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEecQKFAKQYINAIKDYE-LQLITYKAQLEPVASPAK-- 1276
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL--KSIAVLEIDPILNLAqLDKATLEADEDDKRAKVVeg 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1277 ------------KPKVQSGSESVIQEYVDLRTRYSELTTLTS---QYIKFISETLRRMEEEERLAE-----------QQR 1330
Cdd:pfam02463 628 ilkdteltklkeSAKAKESGLRKGVSLEEGLAEKSEVKASLSeltKELLEIQELQEKAESELAKEEilrrqleikkkEQR 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1331 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQA 1410
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1411 KAQQVEAAERS------RMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDES 1482
Cdd:pfam02463 788 VEEEKEEKLKAqeeelrALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEE 867
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1483 QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1562
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
570
....*....|...
gi 256418964 1563 KTAQLERTLQEEH 1575
Cdd:pfam02463 948 KEKEENNKEEEEE 960
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1653-2033 |
7.04e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 KAEEQAVRQRELAEQElekQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEElarlqheataATQKRQELEAEL 1732
Cdd:COG3064 9 AAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE----------AEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1733 AKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTE 1812
Cdd:COG3064 76 AKKLAE-----AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1813 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTL 1892
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1893 RQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAE 1972
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1973 EEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVV 2033
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2147-2314 |
7.40e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.23 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2147 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSVRVQMEEL----------- 2215
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALrsylspnspqv 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2216 GKLKARIEAenralilrdkdntqrfLEeeaekmKQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAV 2294
Cdd:COG3524 252 RQLRRRIAA----------------LE------KQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAAL 309
|
170 180
....*....|....*....|
gi 256418964 2295 QEAtrlKAEAEllQQQKELA 2314
Cdd:COG3524 310 EQA---RIEAA--RQQRYLA 324
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1238-1521 |
7.55e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1238 EKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLR 1317
Cdd:PRK10929 58 EERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1318 RMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAeleaqelqrrMQEEVARReEAAVDaqqqkrsiQE 1395
Cdd:PRK10929 132 AREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA----------LQAESAAL-KALVD--------EL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQHLRQSSEAEIqakaqqveaaerSRMRIeeeirvvrlqlETTERQRGGAEGELQALRAR--------AEEAEAQKRQA 1467
Cdd:PRK10929 193 ELAQLSANNRQEL------------ARLRS-----------ELAKKRSQQLDAYLQALRNQlnsqrqreAERALESTELL 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1468 QEEAERLRRQVQDESQRKRQAEAEL---ALRVKAEA----EAAREKQRALQALDELRLQAE 1521
Cdd:PRK10929 250 AEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQALNTLREQSQ 310
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1458-1537 |
7.86e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1458 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL----RVKAE--AEAAREKQRALQA-LDELRLQAEEAERRLRQA 1530
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAqqqeLVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 256418964 1531 EAERARQ 1537
Cdd:PRK11448 218 RKEITDQ 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1656-1851 |
8.33e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1656 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1732
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1733 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAE-AGRFRELAEEAARLRALAEEAKRQRQLAE 1796
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQiAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 1797 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1851
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1767-1876 |
8.33e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1767 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLTEKLAAISEATRLKTEAEIA-LKEKEAE 1837
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 256418964 1838 NERLRRLaedeafQRRRLEEQAAlHKADIEERL------AQLRKA 1876
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAA-KRLELSEEEtrilidQQLRKA 247
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1327-1430 |
8.34e-04 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 44.79 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1327 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAqelqrRMQEEVARREEAAVDAQQQKRS-IQEELQHLRQSSE 1405
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAA-----AAAEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 256418964 1406 ----------------AEIQAkaqQVEAAERSRMRIEEEIR 1430
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1486-1828 |
8.37e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1486 RQAEAELALRVKAEAEAAREKQR--ALQAldelRLQAEEAERRLRQAEAERARQVQValETAQRSAEVELQSKRASFAEK 1563
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAREARHKKAAEARAAKD--KDAVAAALARVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1564 TAQLERTLQEEHVTVAQLREEaerraqqqaeaerareeaerelerwqlkanealrlRLQAEEVAQQKSLAQADAEKQKEE 1643
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREAR-----------------------------------KAQARARQAEKQAAAAADPKKAAV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1644 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqqrlaaeqelirlRAETEQGEQQrqlleeelarlqHEATAATQ 1723
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIA-------------RAKAKKAAQQ------------AASAEPEE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1724 KRQELEAELAKVRAEMEVLLASKARAEEESRSTSEkskqrleaeagrfrelaeEAARLRALAEE---AKRQRQLAEEDAA 1800
Cdd:PRK05035 606 QVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP------------------VDPRKAAVAAAiarAKARKAAQQQANA 667
|
330 340
....*....|....*....|....*...
gi 256418964 1801 RQRAEAERVLTEKLAAISEATRLKTEAE 1828
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1682-1837 |
8.55e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1682 QRLAAEQELIRlRAETEQGEQQRQLlEEELARLQHEATAATQKRQELEAELAkvraEMEVLLASKARAEEESRSTSEKSK 1761
Cdd:PRK00409 495 KRLGLPENIIE-EAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1762 QRLEAEAgrfrelaeEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1837
Cdd:PRK00409 569 EEAEKEA--------QQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2270-2500 |
8.68e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 45.32 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2270 QLAEEDLAQQRALAEKMLKEKmqavqeatrlkaEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2349
Cdd:COG4487 18 SLYADIVKQRRAEFEKELAER------------LADAAKREAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2350 QLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtLVQTLEIQRQQsdhdaerlreaiaE 2429
Cdd:COG4487 86 ALAVAEEKEK---ELAALQEALAEKDAKLAELQAKELELLKKERELEDAKRE---AELTVEKERDE-------------E 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 2430 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQetqalqksflsekdsllQRERFIEQEKAKLEQLFQDEVA 2500
Cdd:COG4487 147 LDELKEKLKKEEEEKQLAEKSLKVAEYEKQLK-----------------DMQEQIEELKRKKEQGSTQLQG 200
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1368-2001 |
9.04e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1368 LQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAE 1447
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1448 gELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElaLRVKAEaeaarekqralQALDELRLQAEEAERRL 1527
Cdd:pfam05483 159 -LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1528 RQAEAERARQV-----QVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVTVAQLREEAERRAQQQAEAERAREEA 1602
Cdd:pfam05483 225 QHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1603 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegTAQQ 1682
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR----TEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1683 RLaaeqelirlraetEQGEQQRQLLEEELARLQHEATAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESRSTSE 1758
Cdd:pfam05483 371 RL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1759 KSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeialkekeaEN 1838
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------EN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1839 ERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEIMALKVS 1908
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1909 FEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE--------AARQRQLAAEEEQRRREAEERVQRSLAAEE------E 1974
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEiidnyqK 661
|
650 660 670
....*....|....*....|....*....|.
gi 256418964 1975 AARQRKVA----LEEVERLKAKVEEARRLRE 2001
Cdd:pfam05483 662 EIEDKKISeeklLEEVEKAKAIADEAVKLQK 692
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1327-1428 |
9.34e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.49 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1327 EQQRAEERERLAEVEAALEKQRQLAEAHAQAkaqaelEAQELQRRMQEEVARREEaaVDAQQQKRSIQEELQHLRQSSEA 1406
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 256418964 1407 EIQAKAQQVEAAERSRMRIEEE 1428
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1468-1792 |
9.40e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1468 QEEAERLRRQVQDESQRKRQAEAELALRV---------KAEAEAAREKQRALQALDEL-----RLQAEEAERRLRQAEAE 1533
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVtesvepnehNSYEEDSELKPSGQGGLDEEeafldRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1534 RaRQVQVALETAQRSAEVELQSKRASFAE-KTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1612
Cdd:pfam02029 84 E-RQKEFDPTIADEKESVAERKENNEEEEnSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1613 ANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL-I 1691
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAeV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1692 RLRAETEQGEQQRQLLEEElarlQHEATAATQKRQELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEAGRf 1771
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKE----SEEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLREEEEK- 315
|
330 340
....*....|....*....|.
gi 256418964 1772 RELAEEAARLRALAEEaKRQR 1792
Cdd:pfam02029 316 RRMKEEIERRRAEAAE-KRQK 335
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1387-1556 |
9.47e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.39 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1387 QQQKRSIQEELQHLRQSSEAEIQAKAQQVE-----AAERSRM--RIE-EEIRVVRLQLETTerqrgGAEGELQAlRARAE 1458
Cdd:PTZ00491 647 DSLQKSVQLAIEITTKSQEAAARHQAELLEqeargRLERQKMhdKAKaEEQRTKLLELQAE-----SAAVESSG-QSRAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1459 -EAEAQKRQAQEEAErlrrqVQDESQRKRqaeaelALRVKAEAEAAREKQRALQALDELRLQAE---EAERRLRQAEAER 1534
Cdd:PTZ00491 721 aLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATK 789
|
170 180
....*....|....*....|....*.
gi 256418964 1535 ARQVQVAL--ET--AQRSAEVELQSK 1556
Cdd:PTZ00491 790 FERIVEALgrETliAIARAGPELQAK 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2320-2599 |
1.02e-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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2320 RLQEDKEQMAQQLVEETQGFQRT--LEAERQRQLE-MSAEAERlklrmAEMSRAQARAEEDAQR--FRKQAEEIGEKLHR 2394
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLedILNELERQLKsLERQAEK-----AERYKELKAELRELELalLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2395 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ-----LKSEEMQTVQQEQILQETQALQKS 2469
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAneisrLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2470 FLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQ 2549
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 256418964 2550 HLEQQRQQQEKLLAEENQRLRERLQRLeEEHRAALAHSEIATTQAASTKA 2599
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKL-EEAELKELQAELEELEEELEEL 452
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2254-2479 |
1.02e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2254 EAARLsvAAQEAARLRQLAEE--DLAQQRALAEKMLKE---KMQAVQEATRLKAEAELLQQQKELA-------------- 2314
Cdd:PRK10929 120 EKSRQ--AQQEQDRAREISDSlsQLPQQQTEARRQLNEierRLQTLGTPNTPLAQAQLTALQAESAalkalvdelelaql 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2315 -----QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARA----EEDAQRFRKQ 2384
Cdd:PRK10929 198 sannrQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2385 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ------SDHDAERLREAIA---------ELERE-----------KEKLK 2438
Cdd:PRK10929 278 AQRMDLIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVArlpempkpqQLDTEmaqlrvqrlryEDLLN 357
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 256418964 2439 QEAKLLQLKSEEMQ--TVQQEQILQETQALQKSFLSekdSLLQ 2479
Cdd:PRK10929 358 KQPQLRQIRQADGQplTAEQNRILDAQLRTQRELLN---SLLS 397
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3031-3064 |
1.03e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....
gi 256418964 3031 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPE 3064
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1317-1573 |
1.10e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAELEaqelqrrmqeevarREEAAVDAQQQKRSIQE 1395
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1396 ELQhLRQSSEAEIQAKAQQVEAAERSR----MRI--------------EEEIRVVRLQLETTERQ---RGGAEGEL-QAL 1453
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARvdleAKIeslkeelaflkknhEEEVRELQAQVSDTQVNvemDAARKLDLtSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1454 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA-LDELRLQAEEAERRLRQAEA 1532
Cdd:pfam00038 173 AEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIeLQSLKKQKASLERQLAETEE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 256418964 1533 ERARQvqvaLETAQRSaeveLQSKRASFAEKTAQLERTLQE 1573
Cdd:pfam00038 253 RYELQ----LADYQEL----ISELEAELQETRQEMARQLRE 285
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1070-1755 |
1.16e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1070 IRSTQGAEEVLKTHEEQLKEAQAVPATLQE-LEATKASLKKLRAQAEAQqpvFNTLRDELRGAQEVG-ERLQQRHGERDV 1147
Cdd:pfam12128 250 FNTLESAELRLSHLHFGYKSDETLIASRQEeRQETSAELNQLLRTLDDQ---WKEKRDELNGELSAAdAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1148 EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEK 1227
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1228 AL-LEEIERHGEKVE-ECQKFAKQYINAIKDYELQLITYKAQL-----EPVASPAKKPKVQSGSESVIQEYVDLRTRYSE 1300
Cdd:pfam12128 407 DRqLAVAEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELklrlnQATATPELLLQLENFDERIERAREEQEAANAE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1301 LTTLTSQYIKFIS---ETLRRMEEEERLAEQQRaeerERLAEVEAALEKQRqlAEAHAQAKAQAELEAQELQRRMQEEVA 1377
Cdd:pfam12128 487 VERLQSELRQARKrrdQASEALRQASRRLEERQ----SALDELELQLFPQA--GTLLHFLRKEAPDWEQSIGKVISPELL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1378 RREEaaVDAQQQKRSIQEELQ------HLRQ-------SSEAEIQAKAQQVE----AAERSRMRIEEEIRVVRLQLETTE 1440
Cdd:pfam12128 561 HRTD--LDPEVWDGSVGGELNlygvklDLKRidvpewaASEEELRERLDKAEealqSAREKQAAAEEQLVQANGELEKAS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1441 RQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRalQALDELRLQA 1520
Cdd:pfam12128 639 REETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK--EQKREARTEK 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1521 EEAERRLRQAEAERARQVQVALETAQRSAEVELQS----------KRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQ 1590
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAletwykrdlaSLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1591 QQAEAErareeaerelERWQLkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1670
Cdd:pfam12128 797 YFDWYQ----------ETWLQ---RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1671 KQRQLAEGTAQQRLAAEQElirlRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAE 1750
Cdd:pfam12128 864 GLRCEMSKLATLKEDANSE----QAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREE 938
|
....*
gi 256418964 1751 EESRS 1755
Cdd:pfam12128 939 DHYQN 943
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1320-1503 |
1.21e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1320 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1399
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1400 LRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAErlrrqv 1478
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*
gi 256418964 1479 QDESQRKRQAEAELAlRVKAEAEAA 1503
Cdd:PRK05035 671 EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1595-2024 |
1.29e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1595 AERAREEAERELERWQLKANEALRLRLQAEevaqqkSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1674
Cdd:COG3903 487 RAAARRRHADYYLALAERAAAELRGPDQLA------WLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1675 LAEGT--AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1752
Cdd:COG3903 561 LREGRrwLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1753 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1832
Cdd:COG3903 641 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAA 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1833 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKA 1912
Cdd:COG3903 721 AAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1913 AAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 1992
Cdd:COG3903 801 AAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAA 880
|
410 420 430
....*....|....*....|....*....|..
gi 256418964 1993 VEEARRLRERAEQESARQLQLAQEAAQKRLQA 2024
Cdd:COG3903 881 AAALLAAAAAAAAAAAAAAAAAAALAAAAAAA 912
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1318-1505 |
1.33e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1318 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEEL 1397
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1398 QHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRqaQEEAERLRRQ 1477
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEALKAKD-------------------------HKAFDLKQESKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 256418964 1478 VQDESQR-KRQAEAElalrVKAEAEAARE 1505
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2133-2440 |
1.40e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2133 KQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2212
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2213 EELGKLKArieaenralILRDKdntqrFLEEEAEKmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2292
Cdd:pfam15905 132 LELTRVNE---------LLKAK-----FSEDGTQK---------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2293 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQA 2372
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 2373 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQE 2440
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2087-2408 |
1.44e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2087 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQ-TLRQKAQVEQELTT 2165
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETgIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2166 LRLQLEETDHQKSILDEElqrlkaevteaaRQRSQVEEELFSVRVQMEElgkLKARIEAENRALilrdKDNTQRFLEEEA 2245
Cdd:COG5185 352 LTENLEAIKEEIENIVGE------------VELSKSSEELDSFKDTIES---TKESLDEIPQNQ----RGYAQEILATLE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2246 EKMKQVAEEAARLSVAaqeaarLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqARRLQE 2323
Cdd:COG5185 413 DTLKAADRQIEELQRQ------IEQATSSNEEVSKLLneLISELNKVMREADEESQSRLEEAYDEINRSVRSK-KEDLNE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2324 DKEQMAQQLVEETQGFQrTLEAERQRQLE-----MSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2398
Cdd:COG5185 486 ELTQIESRVSTLKATLE-KLRAKLERQLEgvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAAN 564
|
330
....*....|
gi 256418964 2399 TQEKVTLVQT 2408
Cdd:COG5185 565 LRTAVIDELT 574
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1696-1828 |
1.46e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1696 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1775
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1776 EEAARLRA-------------LAEEAKRQRQLAEEDAARQRAEAERVlTEKLAAISEATRLKTEAE 1828
Cdd:pfam05262 287 QIEIKKNDeealkakdhkafdLKQESKASEKEAEDKELEAQKKREPV-AEDLQKTKPQVEAQPTSL 351
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1307-1485 |
1.51e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1307 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR---REEAA 1383
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKarqRQELQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1384 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLeTTERQRGGAEGELQALRARAEEAEAQ 1463
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH-RRELEKQIEEREEQRAAEREEELEEG 317
|
170 180
....*....|....*....|..
gi 256418964 1464 KRQAQEEAERLRRqVQDESQRK 1485
Cdd:pfam13868 318 ERLREEEAERRER-IEEERQKK 338
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
16-119 |
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 256418964 16 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 73
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 256418964 74 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1657-2568 |
1.59e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1657 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVR 1736
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1737 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1808
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1809 VLTEKLAAISEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---ALHKADIEERLAQLRKASESELERQK 1885
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1886 GLVEDTLRQRRQVEEEIMALKVSFEK----AAAGKAELELELGRIRSNAeDTMRSKEQAELEAARQRQLAAEEEQRRREA 1961
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKElqqlEGSSDRILELDQELRKAER-ELSKAEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1962 EERvqrSLAAEEEAARQRKVALEEVERL-KAKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAF-----VVQQ 2035
Cdd:TIGR00606 516 KLR---KLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKskeinQTRD 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2036 REEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRK 2115
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2116 EAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA 2195
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK-STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2196 RQRSQVEEELFSVRVQMEELGKLKARIEAENRA--LILRDKDNTQRFLEEEAEKMKQVAEEAARL-----SVAAQEAARL 2268
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2269 RQLAEEDL---AQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQedkeQMAQQLVEETQGFQRTLEA 2345
Cdd:TIGR00606 831 KQEKQHELdtvVSKIELNRKLIQDQQEQIQH---LKSKTNELKSEKLQIGTNLQRRQ----QFEEQLVELSTEVQSLIRE 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2346 ERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQT-LEIQRQQSDHDAERLR 2424
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVN 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2425 EAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQETQALQKsfLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAKQ 2504
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRK--RENELKEVEEEL-----KQHLKEMGQMQVLQMKQ 1054
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 2505 LReeqqrqqqqmeqekQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQR 2568
Cdd:TIGR00606 1055 EH--------------QKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1670-1945 |
1.61e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 44.08 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1670 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK 1746
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1747 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1806
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1807 ErvLTEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLEE-QAALHK-ADIEERLAQLRKASES 1879
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIERaEKERAAsAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1880 ELERQKGLVEDTLRQRrqVEEEIMAlkvsfekaaagKAELELELGRIRSNAEDTmrSKEQAELEAA 1945
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEETEDA-----------KNKLEWQLKKTLQEIAEL--EKNIEALEKA 287
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1450-1539 |
1.64e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1450 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEaarekQRALQALDELRLQAEEAERRLRQ 1529
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 256418964 1530 AEAERARQVQ 1539
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1695-1822 |
1.66e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1695 AETEQGEQQRQLLEEELARLQHEATAATQKR-QELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQRLEAEAGRFRE 1773
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1774 LAEEAARLRALAEEAKRQRQLA--EEDAAR-------------QRAEAERVLT-------------EKLAAISEATR 1822
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEvtEEDIAEvvsrwtgipvgklLEGEREKLLNleeelhervigqdEAVEAVADAIR 566
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1652-1833 |
1.67e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1652 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEATAATQKRQELEA 1730
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1731 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDaarqrAEAERV 1809
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 256418964 1810 LTEKLAAISEATRLKTEAEIALKE 1833
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1765-1889 |
1.70e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1765 EAEAGRFRELA-EEAARLRALAEEAKRQ----RQLAEEDAA--------RQRAEAERVLTEKLAAISEAtrlKTEAEIAL 1831
Cdd:COG2268 205 EAEAERETEIAiAQANREAEEAELEQEReietARIAEAEAElakkkaeeRREAETARAEAEAAYEIAEA---NAEREVQR 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1832 KEKEAENERLRRLAEDEAfQRRRLEEQAALHK-ADIEERLAQLRKASESELERQKGLVE 1889
Cdd:COG2268 282 QLEIAEREREIELQEKEA-EREEAELEADVRKpAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1614-1836 |
1.72e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.46 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1614 NEALRLRLQ-AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--LAEGTAQQRLAAEQEl 1690
Cdd:COG5283 9 DKPFKSALEsAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQalDQAGIDTRQLSAAQR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1691 iRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVRAEME-----VLLASKARAEEESRSTSEKSKQRLE 1765
Cdd:COG5283 88 -RLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQR-LAGAGAAAAaigaaLAASVKPAIDFEDAMADVAATVDLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1766 AEAGRFRELAEEA----ARLRALAEE-AKRQRQLAEEDAARQRAEAervLTEKLAAISEATRLKTE--AEIALKEKEA 1836
Cdd:COG5283 166 KSSEQFKALGKQArelsAQTPQSADDiAAGQAALAQAGVSAEDILA---FTPTAAKLATAFDTDAEeaAEIAAKILNA 240
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2300-2593 |
1.74e-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: 44.78 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2300 LKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRTLEAERqrqlEMSAEAERLKLRMAEmsraqaraeedaq 2379
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAA------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2380 rfRKQaeEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqqEQI 2459
Cdd:pfam01576 69 --RKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLE----EDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2460 LqetqalqksFLSEKDSLLQRER-FIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQmeqekqelMASMEEARRRQ---R 2535
Cdd:pfam01576 141 L---------LLEDQNSKLSKERkLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM--------ISDLEERLKKEekgR 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 2536 EAEEGVRRKQEELQHLEQQRQQQEKLLAEEnqrLRERLQRLEEEHRAALAHSEIATTQ 2593
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAE---LRAQLAKKEEELQAALARLEEETAQ 258
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1307-1501 |
1.79e-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: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1307 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarreeaavda 1386
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKE------------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1387 QQQKRSIQEELQHLRQSSEAEIQAKAQQvEAAERSRMRIEEEiRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1466
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 256418964 1467 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1501
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2156-2533 |
1.80e-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: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2156 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2235
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2236 NTQRFLEEE---AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmQAVQEATRLKAEAELLQQQKE 2312
Cdd:pfam07888 127 HEARIRELEediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ----QTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2313 LAQEQARRLQEDKEQMAQQLveeTQGFQRTLEAER--------QRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRK 2383
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKL---TTAHRKEAENEAlleelrslQERLNASERkVEGLGEELSSMAAQRDRTQAELHQARL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2384 QAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAkllqlkseemqtvqqeqilQE 2462
Cdd:pfam07888 280 QAAQLTLQLADASLALREgRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER-------------------ME 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2463 TQALQKSFLSEKDS----LLQRERFIEQEKAKLeQLFQDEvakakqlreeqqrqQQQMEQEKQELMASMEEARRR 2533
Cdd:pfam07888 341 REKLEVELGREKDCnrvqLSESRRELQELKASL-RVAQKE--------------KEQLQAEKQELLEYIRQLEQR 400
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2182-2390 |
1.83e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2182 EELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKM-----KQVAEEAA 2256
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2257 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLV 2333
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 2334 EETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2390
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1374-1858 |
1.83e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.62 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1374 EEVARREEAAVDAQQQK--RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG-EL 1450
Cdd:NF033838 53 NESQKEHAKEVESHLEKilSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQfKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1451 QALRARAEEAEAQK------RQAQEEAERLRRQVQDESQRKRQAE-AELALRVKaEAEAAREKQRALQALDELRLQAEEA 1523
Cdd:NF033838 133 DTLEPGKKVAEATKkveeaeKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1524 ERRLRQAEAERARQVQVALETAQRSAEvelqskrasfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeae 1603
Cdd:NF033838 212 KVESKKAEATRLEKIKTDREKAEEEAK----------------------------------------------------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1604 relERWQLKANEALRLRLQAEEVAQQKSLAQADAeKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1683
Cdd:NF033838 239 ---RRADAKLKEAVEKNVATSEQDKPKRRAKRGV-LGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE--AEKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1684 LAAEQElirlRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQR 1763
Cdd:NF033838 313 VEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAK-------EPRNEEKIKQAKAKVESK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1764 LeAEAGRFrelaeeaarlralaEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 1843
Cdd:NF033838 382 K-AEATRL--------------EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEK 446
|
490
....*....|....*..
gi 256418964 1844 LAEDEAFQ--RRRLEEQ 1858
Cdd:NF033838 447 PADQQAEEdyARRSEEE 463
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1620-1790 |
1.88e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1620 RLQAEEVAQQKSLA-QADAE-KQKEEAEREARRRGkaEEQAVRQRELA---------EQELEKQRQLAEGTAQQRLAAEQ 1688
Cdd:PRK11637 114 KLEQQQAAQERLLAaQLDAAfRQGEHTGLQLILSG--EESQRGERILAyfgylnqarQETIAELKQTREELAAQKAELEE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1689 ELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEkskqrleaea 1768
Cdd:PRK11637 192 KQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAE---------- 261
|
170 180
....*....|....*....|..
gi 256418964 1769 grfRElAEEAARLRALAEEAKR 1790
Cdd:PRK11637 262 ---RE-AREAARVRDKQKQAKR 279
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1327-1434 |
1.91e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1327 EQQRAEERERLAEVEAAL-----------EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVA------RREEAAVDAQQQ 1389
Cdd:PRK00409 526 EELERELEQKAEEAEALLkeaeklkeeleEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 256418964 1390 KRSIQEELQHLRQSSeaEIQAKAQQVEAAERSRMRIEEEIRVVRL 1434
Cdd:PRK00409 606 AHELIEARKRLNKAN--EKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2184-2397 |
1.99e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2184 LQRLKAEVTEAARQRSQVEEElfsvrvQMEELGKLKARIEAENRALilrdkdNTQRFLEEEAEKMkqvAEEAARLSVAAQ 2263
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL------EKERLAAQEQKKQ---AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2264 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLVEETQGFQRT 2342
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2343 LEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2397
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2149-2397 |
2.00e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2149 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSVRVQMEELGK 2217
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2218 LKARIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedlaQQRALAEKMlkEKMQAVQ 2295
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPL------QYDCWWEKV--ENLQDLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2296 EATRLKAE--AELLQQQKELaqeqarrlqEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2373
Cdd:PLN02939 310 DRATNQVEkaALVLDQNQDL---------RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQL 380
|
250 260
....*....|....*....|....
gi 256418964 2374 AEEDAQRFRKQAEEIGEKLHRTEL 2397
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESKKRSL 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2149-2327 |
2.01e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2149 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAarQRSQVEEELFSVRVQME-ELGKLKARIEAENR 2227
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2228 ALilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2307
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|
gi 256418964 2308 QQQKELAQEQARRLQEDKEQ 2327
Cdd:COG3206 364 RELYESLLQRLEEARLAEAL 383
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1317-1398 |
2.05e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.53 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAELEAQELQRR-----MQEEVARREEAAVDAQ 1387
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEalaeaQAEAQASKEKARREIE 111
|
90
....*....|.
gi 256418964 1388 QQKRSIQEELQ 1398
Cdd:PRK07353 112 QQKQAALAQLE 122
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2211-2509 |
2.09e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2211 QMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2290
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2291 MQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMS 2368
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2369 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQlks 2448
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--- 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 2449 EEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQ 2509
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1653-1793 |
2.15e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 43.43 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA-- 1730
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 1731 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1793
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2740-2776 |
2.15e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.15e-03
10 20 30
....*....|....*....|....*....|....*..
gi 256418964 2740 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2776
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1317-1487 |
2.20e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.12 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1317 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1396
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPE-AAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1397 LQHLRQSSEAEIQAKAQQVEAAERSRMRieeeiRVVRLQLETTERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRR 1476
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 256418964 1477 QVQDESQRKRQ 1487
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2153-2450 |
2.27e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2153 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIeaenralil 2231
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2232 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2311
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2312 ELAQEQARRLQEDKEQMAQQLVEET--QGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIG 2389
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2390 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2437
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 256418964 2438 KQEAKllQLKSEE 2450
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1799-2021 |
2.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1799 AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEErLAQLRKASE 1878
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1879 SELERQKGLVEDTLRQR-RQVEEEIMALKVSFEKAAAGKAELEL--ELGRIRSNAEDTMRsKEQAELEAARQRQLAAEEE 1955
Cdd:COG4942 97 AELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELR-ADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1956 QRRREAEERVQRSLAAEEEAARQRKVALEEvERLKAKVEEARRLRERAEQESARQLQLAQEAAQKR 2021
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLE-KELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2248-2447 |
2.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2248 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE- 2326
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2327 ----QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2402
Cdd:COG4717 128 lplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 256418964 2403 vtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLK 2447
Cdd:COG4717 208 ---LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1656-1799 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1656 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1735
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256418964 1736 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1799
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1862-2279 |
2.40e-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: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1862 HKADIEERLAQlRKASESELERQKGLVEDTLRQ---RRQVEEEIMALKVSFEKAAAGKAELElelgrirsnaedTMRSKE 1938
Cdd:pfam17380 280 HQKAVSERQQQ-EKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRQAAIYAEQE------------RMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1939 QAELEAARQRQLAAeeeqrrreaeervqrslaaEEEAARQRKVALE-----EVERLKAKvEEARRLRERAEQESARQLQL 2013
Cdd:pfam17380 347 ERELERIRQEERKR-------------------ELERIRQEEIAMEisrmrELERLQME-RQQKNERVRQELEAARKVKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2014 AQEAAQKRLQAEEKAHAFVvqqreeelqqtlqqeqnmldrlrseaeaarraaeeaeeareqaereaaqsRKQVEEAERlk 2093
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQI--------------------------------------------------RAEQEEARQ-- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2094 qsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQaadaEMEKHKKFAEQTLRQKAQVEQElttLRLQLEET 2173
Cdd:pfam17380 435 -----------------REVRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEERKRKKLELEKE---KRDRKRAE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2174 DHQKSILDEELQRLKAEVTEAARQRSQVEEElfsvrvqMEELGKlkaRIEAENRALILRDKDNTQRFLEEE---AEKMKQ 2250
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKE-------MEERQK---AIYEEERRREAEEERRKQQEMEERrriQEQMRK 560
|
410 420
....*....|....*....|....*....
gi 256418964 2251 VAEEAARLSVAAQEAARLRQLAEEDLAQQ 2279
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2141-2549 |
2.42e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2141 EMEKHKKFAEQTLRQKAQVEQELttlRLQLEETDHQ----KSILDEELQRLKAEVTEAAR---QRSQVEEELFSVRVQME 2213
Cdd:pfam15921 121 EMQMERDAMADIRRRESQSQEDL---RNQLQNTVHEleaaKCLKEDMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2214 E-----------LGKLKARIEAENRALILRDKDNTQRFL-------EEEAEKMKQVAEEAARLsVAAQEAARLRQLAEED 2275
Cdd:pfam15921 198 EasgkkiyehdsMSTMHFRSLGSAISKILRELDTEISYLkgrifpvEDQLEALKSESQNKIEL-LLQQHQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2276 LAQQRALAEKmlkekmqavqeATRLKAEAELLQQQKELAQEQAR-------RLQEDKEQMAQQLVEETQGFQRTLEaERQ 2348
Cdd:pfam15921 277 EVEITGLTEK-----------ASSARSQANSIQSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYE-DKI 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2349 RQLEMsaeaerlKLRMAEMSRAQARAEEDaqRFRKQAEEIGEKLHR--TELATQEKvtlvqTLEIQRQQSDHDAERLRE- 2425
Cdd:pfam15921 345 EELEK-------QLVLANSELTEARTERD--QFSQESGNLDDQLQKllADLHKREK-----ELSLEKEQNKRLWDRDTGn 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2426 --AIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQ-KSFLSEKDSLLQRErfIEQEKAKLEQLFQDEVAKa 2502
Cdd:pfam15921 411 siTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgKNESLEKVSSLTAQ--LESTKEMLRKVVEELTAK- 487
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 256418964 2503 KQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQ 2549
Cdd:pfam15921 488 KMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1450-1549 |
2.49e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1450 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEsQRKRQAEAElALRVKAEAEAAREKQRALQALDelrlqaEEAERR 1526
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 256418964 1527 LRQAEAERARQVQVALETAQRSA 1549
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2138-2595 |
2.52e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2138 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSildEELQRLKAEVTEAARQR-SQVEEELFSVRVQMEELg 2216
Cdd:NF041483 209 AEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAES---DQARRQAAELSRAAEQRmQEAEEALREARAEAEKV- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2217 kLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEeaarlsvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQE 2296
Cdd:NF041483 285 -VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGE-------ATKEAEALKAEAEQALADARAEAEKLVAEAAEKART 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2297 ATRLKAEAELLQQQKElAQEQARRLQEDKEQMAQQLVEEtqgfqrtleAERQRQlEMSAEAERLKLRMAEMS-RAQARAE 2375
Cdd:NF041483 357 VAAEDTAAQLAKAART-AEEVLTKASEDAKATTRAAAEE---------AERIRR-EAEAEADRLRGEAADQAeQLKGAAK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2376 EDAQRFRKQAEEIGEKLHRTElatqekvtlvqtleiqrqqsdHDAERLR-EAIAELEREKEKLKQEAkllqLKSEEMQTV 2454
Cdd:NF041483 426 DDTKEYRAKTVELQEEARRLR---------------------GEAEQLRaEAVAEGERIRGEARREA----VQQIEEAAR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2455 QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQ 2534
Cdd:NF041483 481 TAEELLTKAKADADELRSTATAESERVRTEAIERATTLRR-QAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELR 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2535 REAEEGVRRKQEELqhleqqrqqqekllAEENQRLR----ERLQRLEEEHRAALAHSEIATTQAA 2595
Cdd:NF041483 560 EETERAIAARQAEA--------------AEELTRLHteaeERLTAAEEALADARAEAERIRREAA 610
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2241-2379 |
2.52e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2241 LEEEA------EKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQ 2310
Cdd:PTZ00491 675 LEQEArgrlerQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAE 751
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 2311 KELAQEQARRLQEDKEQmaQQLVEetqgfqrtLEAERQRQLeMSAEAERLKLRMAEMSR----AQARAEEDAQ 2379
Cdd:PTZ00491 752 AELEKLRKRQELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1393-1728 |
2.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1393 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1472
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1473 RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVE 1552
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1553 LQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1632
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1633 AQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1712
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*.
gi 256418964 1713 RLQHEATAATQKRQEL 1728
Cdd:COG4372 324 LAKKLELALAILLAEL 339
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
17-125 |
2.69e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 40.74 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 87
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 256418964 88 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
28-118 |
2.71e-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: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 28 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 100
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 256418964 101 DDIADGNPKLTLGLIWTI 118
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2374-2498 |
2.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2374 AEEDAQRFRKQAEEigeklhRTELATQEKVTLVQTlEIQRQQSDHDAErLREAIAELEREKEKLKQEAKLLQLKSEEMQt 2453
Cdd:PRK12704 36 AEEEAKRILEEAKK------EAEAIKKEALLEAKE-EIHKLRNEFEKE-LRERRNELQKLEKRLLQKEENLDRKLELLE- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 256418964 2454 vQQEQILQEtqalqksflsEKDSLLQRERFIEQEKAKLEQLFQDE 2498
Cdd:PRK12704 107 -KREEELEK----------KEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
497-591 |
3.04e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 497 LRYLQDLLAWVEENQRRIDSAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQL---SPATRGAYRDCLGRLD 573
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 256418964 574 LQYAKLLNSSKARLRSLE 591
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1663-1859 |
3.36e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1663 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEV 1741
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1742 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAER----VLTEK 1813
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKlrnqLTSKS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 256418964 1814 LAAISEA---TRLKTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQA 1859
Cdd:pfam09787 160 QSSSSQSeleNRLHQLTE-TLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1606-1873 |
3.43e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1606 LERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR-----RGKAEEQAVRQRELAEQELEKQRQLAEGTA 1680
Cdd:pfam13868 65 EERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERiqeedQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1681 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsEKS 1760
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE-----RKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1761 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLT------EKLAAISEATRLKTEAEIALKEK 1834
Cdd:pfam13868 220 RQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRkqaedeEIEQEEAEKRRMKRLEHRRELEK 297
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 256418964 1835 EAENERLRRLAEDEAF--QRRRLEEQAALHKADIEERLAQL 1873
Cdd:pfam13868 298 QIEEREEQRAAEREEEleEGERLREEEAERRERIEEERQKK 338
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1345-1476 |
3.48e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1345 EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKAQQVEAAERSR 1422
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1423 MRIEEEIRVVRLQLETTERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1476
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1435-1898 |
3.76e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1435 QLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR--VKAEAEAAREKQRALQA 1512
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1513 LDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehVTVAQLREEAERRAQQQ 1592
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA--RAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1593 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1672
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1673 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1752
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1753 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1832
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1833 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 1898
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2213-2330 |
3.90e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2213 EELGKLKARIEAENRALILRDKDNTQrfLEEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2292
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 256418964 2293 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2330
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1312-1413 |
3.97e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.67 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1312 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAKA-----QAELEAQELQRRMQE-----EV 1376
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEVakiqmQQKIMEKEAEKKISEiedemHL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 256418964 1377 ArREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAQ 1413
Cdd:cd03406 237 A-REKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2268-2442 |
4.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2268 LRQLAEEDLAQQRALAEKMLKEkmqavqeatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAER 2347
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2348 QRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAI 2427
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEA 171
|
170
....*....|....*.
gi 256418964 2428 AELEREKEKL-KQEAK 2442
Cdd:PRK12704 172 AVLIKEIEEEaKEEAD 187
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2231-2404 |
4.09e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2231 LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2310
Cdd:pfam05262 177 ISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2311 KELAQEQAR--------RLQEDKEQMAQQLVEETQgfQRTLEAERQRQlemsAEAERLKLRMAEMSRAQARAEEDAQRFR 2382
Cdd:pfam05262 257 AKNLPKPADtsspkedkQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|..
gi 256418964 2383 kqaEEIGEKLHRTELATQEKVT 2404
Cdd:pfam05262 331 ---EPVAEDLQKTKPQVEAQPT 349
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1403-1537 |
4.13e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1403 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDES 1482
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 1483 QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1537
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2994-3031 |
4.13e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.69 E-value: 4.13e-03
10 20 30
....*....|....*....|....*....|....*...
gi 256418964 2994 LRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVAVAL 3031
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1364-1502 |
4.40e-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: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1364 EAQELQRRMqEEVARREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1443
Cdd:COG0542 412 ELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1444 GGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEAELALRVKAEAEA 1502
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1351-1539 |
4.45e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1351 AEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIR 1430
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1431 vvRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAE-AELALRVKAEAEAAREKQRA 1509
Cdd:PRK12678 147 --EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG--RREERGRDGDdRDRRDRREQGDRREERGRRD 222
|
170 180 190
....*....|....*....|....*....|
gi 256418964 1510 LQALDELRLQAEEAERRLRQAEAERARQVQ 1539
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1359-1696 |
4.76e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1359 AQAELEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQl 1436
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1437 ETTERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA--REKQRALQALD 1514
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKwsTEVRQAEEEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1515 ELRLQAEEAERRLRQAEAERarqvQVALETAQRSAEVELQSKrASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAE 1594
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKE----EVKDEKIKKEKKVKYESK-VFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1595 AERAREEAERELERWQlkANEALRLRLQA--EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQElekq 1672
Cdd:pfam02029 233 SQEREEEAEVFLEAEQ--KLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE---- 306
|
330 340
....*....|....*....|....
gi 256418964 1673 RQLAEGTAQQRLaaEQELIRLRAE 1696
Cdd:pfam02029 307 RKLREEEEKRRM--KEEIERRRAE 328
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1124-1492 |
4.88e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1124 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLgrqLRYYRESADPLSAWLQDAKR 1203
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1204 RQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKV-------EECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK 1276
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1277 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSqyiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAH 1354
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQ---KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1355 AQAKAQAELEAQELQrrMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEiRVVRL 1434
Cdd:pfam07888 266 QRDRTQAELHQARLQ--AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 256418964 1435 QLETT-ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1492
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1314-1441 |
4.99e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQEL-QRRMQEEVARREEAAVDAQQQKR 1391
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 256418964 1392 SIQEELQHLRQSSEAeiqAKAQQVEAAErsRMRIEEEIRVVRLQLETTER 1441
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAE--RQRQEREKIMQQEEQERLER 135
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2134-2407 |
5.07e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2134 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVR 2209
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2210 VQMEELGKL-----KARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRAL 2282
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2283 AEKMLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDK--EQMAQQLVEETQGFQRTLEAERQRQLEMSAEAER 2359
Cdd:pfam13868 213 EEQERKERQKEREEAeKKARQRQELQQAREEQIELKERRLAEEAerEEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 256418964 2360 LKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2407
Cdd:pfam13868 293 RELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3399-3430 |
5.17e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.17e-03
10 20 30
....*....|....*....|....*....|..
gi 256418964 3399 KLLSAEKAVTGYKDPYSGNTISLFQAMKKGLV 3430
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1314-1498 |
5.21e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEEER---LAEQQRAEererLAEVEAALEKQRQlaEAHAQAKAQAELE-----AQELQRRMQEEVARREEAAVD 1385
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE----LDASRALAEKQKH--ELDTEKRCAEELKeamqmAMEGHARMLEQYADLEEKHIQ 1125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1386 AQQQKRSIQEELQHLRQSSE------AE---IQAKAQQVEA----AERSRMRIEEEIRVVRLQLETTER--QRGG----- 1445
Cdd:PLN03188 1126 LLARHRRIQEGIDDVKKAAAragvrgAEskfINALAAEISAlkveREKERRYLRDENKSLQAQLRDTAEavQAAGellvr 1205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1446 ---AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1498
Cdd:PLN03188 1206 lkeAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1658-2015 |
5.25e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1658 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--HEATAATQKRQELEA 1730
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1731 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLR--------ALAEEAKRQRQLAEEDAARQ 1802
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKsqladyqqALDVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1803 RAE------------AERVLTEKLAAISEATRLKTEAEIALKEKEAENER-------LRRLAED----EAFQR-----RR 1854
Cdd:PRK04863 425 RAKqlcglpdltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlVRKIAGEvsrsEAWDVarellRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1855 LEEQAALhkadiEERLAQLRkASESELERQkglvedtLRQRRQVEEeimaLKVSFEKAAAGKAELELELGRIRSNAEDTM 1934
Cdd:PRK04863 505 LREQRHL-----AEQLQQLR-MRLSELEQR-------LRQQQRAER----LLAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1935 RSKEQaELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE-------------------VERLKAKVEE 1995
Cdd:PRK04863 568 ESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeefedsqdvteymqqlLERERELTVE 646
|
410 420
....*....|....*....|
gi 256418964 1996 ARRLRERAEQESARQLQLAQ 2015
Cdd:PRK04863 647 RDELAARKQALDEEIERLSQ 666
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2266-2441 |
5.34e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2266 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLVEETQG 2338
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2339 FQRTLEAERQRQLemsaeAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2418
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 256418964 2419 DAERLREAIAELEREKEKLKQEA 2441
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1653-1810 |
5.34e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1653 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEATAATQKRQELEA 1730
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1731 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1806
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....
gi 256418964 1807 ERVL 1810
Cdd:COG1842 207 EDEL 210
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2207-2387 |
5.35e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2207 SVRVQMEE----LGKLKARIEAENRA-LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEED 2275
Cdd:PRK11637 62 SVRQQQQQraslLAQLKKQEEAISQAsRKLRETQNTLNQLNKQIDELNasiaklEQQQAAQERLLAAQLDAAFRQGEHTG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2276 LAQQRALAEKMLKEKMQA----VQEAtRLKAEAELLQQQKELAQEqaRRLQEDKEQMAQQLVEETQGFQRTLE---AERQ 2348
Cdd:PRK11637 142 LQLILSGEESQRGERILAyfgyLNQA-RQETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEqarNERK 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256418964 2349 RQL---------------EMSAEAERLKLRMAEMSR-AQARAEE---DAQRFRKQAEE 2387
Cdd:PRK11637 219 KTLtglesslqkdqqqlsELRANESRLRDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2238-2450 |
5.44e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2238 QRFleeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQ 2317
Cdd:PRK05035 453 ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAARE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2318 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQR-------QLEMSAEAE-----RLKLRMAEMSRAQAR-AEEDAQRFRKQ 2384
Cdd:PRK05035 525 ARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaQQAANAEAEeevdpKKAAVAAAIARAKAKkAAQQAASAEPE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 2385 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEE 2450
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1201-1529 |
5.86e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1201 AKRRQEQIQAVpIANCQAAREQLRQE-KALLEEIERHGEKVEECQKfakQYINAIKdyelQLITYKAQLEPVASPAkkpk 1279
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELKD---KYRELRK----TLLANRFSYGPAIDEL---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1280 vqsgsESVIQEYVDLRTRYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1358
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1359 AQ--------AELEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKA----------QQVEAAE 1419
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKKyveknlpeieDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1420 RSRMRIEEEIRVV----RLQLETTERQRgGAEGELQALRARAEEAE---AQKRQA----QEEAERLRRQVQD-ESQRKRQ 1487
Cdd:pfam06160 305 EQNKELKEELERVqqsyTLNENELERVR-GLEKQLEELEKRYDEIVerlEEKEVAyselQEELEEILEQLEEiEEEQEEF 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 256418964 1488 AEAELALRvkaeaeaaREKQRALQALDELRLQAEEAERRLRQ 1529
Cdd:pfam06160 384 KESLQSLR--------KDELEAREKLDEFKLELREIKRLVEK 417
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1314-1418 |
5.94e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1314 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDA----- 1386
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVlqewe 148
|
90 100 110
....*....|....*....|....*....|....*
gi 256418964 1387 ---QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA 1418
Cdd:pfam13904 149 rkkLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1447-1640 |
6.09e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1447 EGELQALRARAEEAEAQKRQAQEEAERLRRQvqdESQRKRQAEAELALRVKAEAEAAREKQRAlqaldELRLQAEEAERR 1526
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQERLKQLEKERLAAQ---EQKKQAEEAAKQAALKQKQAEEAAAKAAA-----AAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1527 LrqaeAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAReeaerel 1606
Cdd:PRK09510 156 A----AAAAKK---AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA------- 221
|
170 180 190
....*....|....*....|....*....|....
gi 256418964 1607 ERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQ 1640
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1077-1528 |
6.31e-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: 42.81 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1077 EEVLKTHEEQLKE-AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1155
Cdd:pfam05557 61 EKREAEAEEALREqAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1156 VTQLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLSAWLQDAKRRQEQiqavpIANCQAAREQLRQEKAL 1229
Cdd:pfam05557 141 LDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELAR-----IPELEKELERLREHNKH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1230 LEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSEL------- 1301
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDLSRRIEQLqqreivl 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1302 ----TTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL----------------------AEAH 1354
Cdd:pfam05557 296 keenSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgyrailesydkeltMSNY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1355 AQAKAQAELEAQELQRRMQ---EEVARR----EEAAVDAQQQKRSIQEELQHLRQ--------SSEAEIQAKAQQVEAAE 1419
Cdd:pfam05557 375 SPQLLERIEEAEDMTQKMQahnEEMEAQlsvaEEELGGYKQQAQTLERELQALRQqesladpsYSKEEVDSLRRKLETLE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1420 RSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DESQRKRQAEAELALRVK 1497
Cdd:pfam05557 455 LERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKRLLKKLEDDLEQVLRLP 534
|
490 500 510
....*....|....*....|....*....|.
gi 256418964 1498 AEAEAAREKQralqaLDELRLQAEEAERRLR 1528
Cdd:pfam05557 535 ETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2412-2634 |
6.92e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2412 QRQQSDH----DAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQEtqalQKSFLSEKDSLLQRERfIEQE 2487
Cdd:pfam17380 286 ERQQQEKfekmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAE----QERMAMERERELERIR-QEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2488 KAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQ 2567
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 2568 RLRE----RLQRLEEEHRAALAHSEIATTQAASTKALPNGRDApdgpsvEAEPEYTFEGLRQKVPAQQLQE 2634
Cdd:pfam17380 439 RLEEerarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEK------EKRDRKRAEEQRRKILEKELEE 503
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2308-2442 |
6.93e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2308 QQQKELAQEQARRLQEDKEQMAQQLVEETQgfQRTLEAERQRQLEMSAEAERLKLRMAEMSR------AQARAEEDAQRF 2381
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256418964 2382 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLKQEAK 2442
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1328-1522 |
7.05e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1328 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE 1407
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1408 IQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKR 1486
Cdd:PRK07735 156 EEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSgDEDA 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 256418964 1487 QAEAELALRVKAEAeAAREKQRALQALDELRLQAEE 1522
Cdd:PRK07735 236 KAKAIAAAKAKAAA-AARAKTKGAEGKKEEEPKQEE 270
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1416-1533 |
7.18e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1416 EAAERSRMRIE---EEIRVVRLQLETTERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDESQRKRQAEAel 1492
Cdd:COG0542 397 EAAARVRMEIDskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA-- 461
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 256418964 1493 alRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAE 1533
Cdd:COG0542 462 --RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1331-1506 |
7.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1331 AEERERLAEVEAalekQRQLAEAHAQAKA---QAELEAQELQRRMQEEvarreeaavdAQQQKRSIQEELQHLrqssEAE 1407
Cdd:PRK12704 29 AEAKIKEAEEEA----KRILEEAKKEAEAikkEALLEAKEEIHKLRNE----------FEKELRERRNELQKL----EKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1408 IQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERqrggaegELQALRARAEEAEAQKRQA--------QEEA-ERLRRQV 1478
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKV 163
|
170 180
....*....|....*....|....*...
gi 256418964 1479 QDEsqrkrqAEAELALRVKAEAEAAREK 1506
Cdd:PRK12704 164 EEE------ARHEAAVLIKEIEEEAKEE 185
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1458-1575 |
7.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1458 EEAeaqKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1537
Cdd:PRK00409 505 EEA---KKLIGEDKEKLNELIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110
....*....|....*....|....*....|....*....
gi 256418964 1538 VQVALETAQRSAEVELQSKRASFAEKTAQL-ERTLQEEH 1575
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVkAHELIEAR 613
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1320-1581 |
7.42e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1320 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEE-------VARREEAAVDAQQQKRS 1392
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1393 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEI--RVVRLQLETTE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1469
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1470 EAERLRRQV-QDESQRKRQAEAELALRVKAEAEAAREK-------QRALQALDELRLQAEEAERRLRQAEAERARQVQVa 1541
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVF- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 256418964 1542 LETAQRSAEVElQSKRASFAEKTAQLERTLQEEHVTVAQL 1581
Cdd:pfam02029 244 LEAEQKLEELR-RRRQEKESEEFEKLRQKQQEAELELEEL 282
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1859-2035 |
7.44e-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: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1859 AALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKE 1938
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1939 QAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL-----------EEVERLKAKVEEARRLRERAEQES 2007
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAER 173
|
170 180 190
....*....|....*....|....*....|
gi 256418964 2008 ARQLQL--AQEAAQKRLQAEEKAHAFVVQQ 2035
Cdd:COG4942 174 AELEALlaELEEERAALEALKAERQKLLAR 203
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1787-1948 |
7.50e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1787 EAKRQRQLAEEDAARQRAEAERvLTEKlaAISEATRLKTEAEIA-------LKEKEAENERLRRLAEdeafQRRRLEEQA 1859
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAEAER-ETEI--AIAQANREAEEAELEqereietARIAEAEAELAKKKAE----ERREAETAR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1860 ALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELElgrirsnaedtmrskEQ 1939
Cdd:COG2268 262 AEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE---------------AE 326
|
....*....
gi 256418964 1940 AELEAARQR 1948
Cdd:COG2268 327 AEAEAIRAK 335
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2315-2503 |
7.78e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.18 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2315 QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigEKLHR 2394
Cdd:pfam15665 13 EAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE--RELKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2395 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKL-LQLKSEEMQTVQQEQ---ILQETQALQKSF 2470
Cdd:pfam15665 91 EAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAkHRQEIQELLTTQRAQsasSLAEQEKLEELH 170
|
170 180 190
....*....|....*....|....*....|...
gi 256418964 2471 LSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAK 2503
Cdd:pfam15665 171 KAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQ 203
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1503-1557 |
8.25e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 256418964 1503 AREKQRALQaldelRLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1557
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
21-123 |
8.49e-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: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 256418964 97 NIRNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1401-1580 |
8.56e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1401 RQSSEAEIQAKAQQVEA-AERSRMRIE-EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1478
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1479 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSK-- 1556
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTei 212
|
170 180
....*....|....*....|....
gi 256418964 1557 RASFAEKTAQLERTLQEEHVTVAQ 1580
Cdd:pfam00529 213 RAPVDGTVAFLSVTVDGGTVSAGL 236
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2132-2596 |
9.13e-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: 42.12 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2132 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTtlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVE-----EELF 2206
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2207 SVRVQMEELgklKARIEAENRALILRDkDNTQRFLE---EEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2283
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLEmlqSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2284 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLVEETQGFQRTLEaerqrqLEMSAEAERLKlr 2363
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQMLKTNGL------LHTEDREEEIK-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2364 maemsraQARAEEDAQRFRK-QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAK 2442
Cdd:pfam10174 276 -------QMEVYKSHSKFMKnKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2443 LLQLKSEEMQTV-----QQEQILQETQALQKSFLSE-KDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQM 2516
Cdd:pfam10174 349 ALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 2517 EQEKQE--LMASMEEArrrQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLE----EEHRAALAHSEIA 2590
Cdd:pfam10174 429 TDSSNTdtALTTLEEA---LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQpeltEKESSLIDLKEHA 505
|
....*.
gi 256418964 2591 TTQAAS 2596
Cdd:pfam10174 506 SSLASS 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1182-1394 |
9.16e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1182 RQLRYYRESADPLSAWLQD-AKRRQEQIQAVpiancQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINA---IKDY 1257
Cdd:COG3206 164 QNLELRREEARKALEFLEEqLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1258 ELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQR 1330
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256418964 1331 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEE-------VARREEAAVDAQQQKRSIQ 1394
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1726-1911 |
9.21e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1726 QELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1805
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDE------------------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1806 AERvLTEKLAAISEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQK 1885
Cdd:COG1579 75 IKK-YEEQLGNVRNNKEYE-----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....*.
gi 256418964 1886 GLVEDTLRQRRQVEEEIMALKVSFEK 1911
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPP 174
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4255-4285 |
9.54e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.54e-03
10 20 30
....*....|....*....|....*....|.
gi 256418964 4255 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4285
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1654-1754 |
9.58e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1654 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1733
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 256418964 1734 KvRAEMEVLLaskarAEEESR 1754
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1156-1433 |
9.59e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1156 VTQLLERWQAVLAQTDVRQRELEQLGRQLryyrESADplsAWLQDAkrrQEQIQAVPIANCQAAREQLrqEKALLEEIER 1235
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQL----AQAP---AKLRQA---QAELEALKDDNDEETRETL--STLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1236 hgeKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFISET 1315
Cdd:PRK11281 129 ---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1316 LR-RMEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAELEAQELQ------RRMQ-EEVARREEAAV 1384
Cdd:PRK11281 193 QRvLLQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQeainskRLTLsEKTVQEAQSQD 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256418964 1385 DAQQQKRS--IQEELQHLRQSSEAEIQAKA-------------QQVEAAERSRMRIEEEIRVVR 1433
Cdd:PRK11281 270 EAARIQANplVAQELEINLQLSQRLLKATEklntltqqnlrvkNWLDRLTQSERNIKEQISVLK 333
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1384-1530 |
9.66e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1384 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ 1463
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256418964 1464 KRQAQEEAERLRRQVQdesqrkrQAEAElalrvkaeaEAAREKQRALQALDELRLqaEEAERR------LRQA 1530
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1759-1907 |
9.95e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1759 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LTEKLAAisEATRLKTE 1826
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256418964 1827 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALK 1906
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
.
gi 256418964 1907 V 1907
Cdd:PRK12705 181 I 181
|
|
| |
